TITLE OF THE INVENTION Bispecific Natural Killer Engagers That Target Siglec-7 CROSS REFERENCE TO RELATED APPLICATIONS This application claims priority to U.S. Provisional Application No. 63/325,887, filed March 31, 2022, U.S. Provisional Application No.63/375,784, filed on September 15, 2022, and U.S. Provisional Application No.63/490,156, filed March 14, 2023, each of which is hereby incorporated by reference herein in its entirety. BACKGROUND OF THE INVENTION Ovarian cancer (OC) represents the deadliest gynecologic malignancy. It stands as the fifth major driver of deaths due to cancer among women and accounts for the highest number of deaths due to cancer of the female reproductive system. As per the American Cancer Society, it is estimated that there were 21,410 women with a new ovarian cancer diagnosis and 13,770 deaths due to OC in 2021 (Kurnit et al., 2021, Obstet Gynecol 137: 108-21; www_cancer_org). OC is a highly heterogeneous cancer where 90% of tumors are of epithelial origin. The most prevalent subtype of epithelial ovarian cancer (EOC) is high-grade serous cancer constituting around 70–80% of cases, whereas low-grade serous (<5%), endometrioid (10%), clear cell (10%) and mucinous (3%) represent less predominant subtypes (Barnes et al., 2021, Genome Med 13: 140). Surgery and chemotherapy are the primary treatments for OC (Yang et al., 2020, Front Immunol 11: 577869). Unfortunately, these approaches are only partially successful as many patients develop chemoresistance within a few years after the initial treatment and thus are faced with disease recurrence (Yang et al., 2020, Front Immunol 11: 577869). OC high mortality is also linked to low rates of early detection often due to the lack of subjective symptoms as well as marginally invasive techniques for primary detection. Therefore OC remains a critical need area for improved and novel therapeutic approaches (Banno et al., 2014, Biomed Res Int 2014: 232817). There is a close interaction between the ovarian tumor cells and the tumor microenvironment, development of treatment approaches which not only target the tumor cells but also can maintain their anti-tumor function in this microenvironment is of importance (CSSOCR, 2016). A growing area of study is immune based therapies for OC. Such studies include immune checkpoint inhibitors (ICIs), chimeric antigen receptor (CAR)- and T cell receptor (TCR)-engineered T cells (Yang et al., 2020, Front Immunol 11: 577869). Notably, a prime obstacle in the development of CAR therapies is to find targets with specific expression confined to the surface of tumor cells, but not on target off tumor tissues (Perales-Puchalt et al., 2017, Clin Cancer Res 23: 441-53). The follicle- stimulating hormone receptor (FSHR) is one such target reported to have selective expression in ovarian granulosa cells versus low levels of expression in the ovarian endothelium. FSHR is expressed in 50-70% of serous ovarian carcinoma cases providing an important potential target for immune therapies (Perales-Puchalt et al., 2017, Clin Cancer Res 23: 441-53). mAbs are an important tool in the diagnosis, classification, treatment and monitoring of specific cancers. Some examples include anti-HER2 antibodies in various forms for the classification and treatment of breast cancer (Hayes et al., 2007, N Engl J Med 357: 1496-506; Pegram et al., 1998, J Clin Oncol 16: 2659-71), anti-CD20 antibodies for therapy of lymphoma (Maloney et al., 1997, Blood 90: 2188-95), anti- CA125 for the follow-up of OC (Bast et al., 1983, N Engl J Med 309: 883-7) and anti- PSA for detection of prostate cancer (Siddall et al., 1986, Clin Chem 32: 2040-3). A recent area of importance in the field of antibody therapeutics has been studies of bispecific T cell engagers (Perales-Puchalt et al., 2019, Mol Ther 27: 314-25). These represent a novel class of immunotherapy with ability to bind both T cells and tumor cells simultaneously to facilitate the cytolytic function of T cells for specific tumor cells (Hipp et al., 2017, Leukemia 31: 2278). In the case of OC, especially extremely aggressive ovarian tumors such as high-grade serous ovarian cancer (HGSOC) and ovarian carcinosarcoma (OCS) have restricted treatment choices. These tumors respond poorly to the existing ICI therapy and are frequently termed as Immunologically “cold” Tumors (Wu et al., 2021, Front Immunol 12: 672502). Thus, T cell approaches alone may not be fully effective in treating difficult OC cases. Engaging additional effector components of the immune system may be important. In this regard there are limited studies linking innate mechanisms such as NK to OC tumor impact, and no specific targeting methods have been reported for OC (Hoogstad-van Evert et al., 2020, Gynecol Oncol 157: 810-6). Skin cancer is one of the most common and dangerous of human cancers. Among its different subtypes, melanoma arising from melanocytes represents a particularly serious disease. New FDA approved immunotherapies of immune checkpoint blockade (CPI) have revolutionized melanoma therapy improving the outcomes. However, 40-50 % of the melanomas tend to be immunologically cold with poor T cell infiltration, and poorly respond to CPI. This supports the need for additional approaches. There remains a need in the art for immune therapeutics that effectively treat cancer, autoimmune and infectious diseases while minimizing negative effects. The present invention satisfies this unmet need. SUMMARY OF THE INVENTION In one embodiment, the invention provides a bispecific natural killer engager (NKCE) or fragment thereof comprising an antibody or fragment thereof that specifically binds to Siglec-7 and an antibody or fragment thereof that specifically binds to an antigen. In one embedment, the antigen is a tumor antigen. In one embodiment, the tumor antigen is Follicle stimulating hormone receptor (FSHR) or Interleukin-13 receptor subunit alpha-2 (IL-13Rα2). In one embodiment, the Siglec-7 binding arm of the bispecific NKCE comprises a variable heavy chain sequence comprising the CDR sequences of SEQ ID NO:1-3; SEQ ID NO:17-19; SEQ ID NO:33-35; SEQ ID NO:49-51; SEQ ID NO:65-67; or SEQ ID NO:81-83. In one embodiment, the Siglec-7 binding arm of the bispecific NKCE comprises a variable heavy chain sequence comprising the CDR sequences of SEQ ID NO:9-11; SEQ ID NO:25-27; SEQ ID NO:41-43; SEQ ID NO:57-59; SEQ ID NO:73-75; or SEQ ID NO:89-91. In one embodiment, the Siglec-7 binding arm of the bispecific NKCE comprises a variable heavy chain sequence of SEQ ID NO: 4, SEQ ID NO: 20, SEQ ID NO: 36, SEQ ID NO: 52, SEQ ID NO: 68, or SEQ ID NO: 84. In one embodiment, the Siglec-7 binding arm of the bispecific NKCE comprises a variable light chain sequence of SEQ ID NO: 12, SEQ ID NO: 28, SEQ ID NO: 44, SEQ ID NO: 60, SEQ ID NO: 76, or SEQ ID NO: 92. In one embodiment, the bispecific NKCE comprises an amino acid sequence of SEQ ID NO:98, SEQ ID NO:100 or SEQ ID NO:102. In one embodiment the invention relates to a nucleic acid molecule encoding a bispecific natural killer engager (NKCE) or fragment thereof comprising an antibody or fragment thereof that specifically binds to Siglec-7 and an antibody or fragment thereof that specifically binds to an antigen. In one embodiment, the nucleic acid molecule comprises heavy chain CDR encoding sequences of SEQ ID NO:5-7; SEQ ID NO:21-23; SEQ ID NO:37-39; SEQ ID NO:53-55; SEQ ID NO:69-71; or SEQ ID NO:85-87. In one embodiment, the nucleic acid molecule comprises light chain CDR encoding sequences of SEQ ID NO:13- 15; SEQ ID NO:29-31; SEQ ID NO:45-47; SEQ ID NO:61-63; SEQ ID NO:77-79; or SEQ ID NO:93-95. In one embodiment, the nucleic acid molecule comprises a nucleotide sequence encoding a variable heavy chain sequence of SEQ ID NO:8; SEQ ID NO:24; SEQ ID NO:40; SEQ ID NO:56; SEQ ID NO:72; or SEQ ID NO:88; a nucleotide sequence encoding a variable light chain sequence of SEQ ID NO:16; SEQ ID NO:32; SEQ ID NO:48; SEQ ID NO:64; SEQ ID NO:80; or SEQ ID NO:96; a nucleotide sequence having at least 95% identity to a variable heavy chain sequence of SEQ ID NO:8; SEQ ID NO:24; SEQ ID NO:40; SEQ ID NO:56; SEQ ID NO:72; or SEQ ID NO:88; a sequence having at least 95% identity to a variable light chain sequence of SEQ ID NO:16; SEQ ID NO:32; SEQ ID NO:48; SEQ ID NO:64; SEQ ID NO:80; or SEQ ID NO:96; a fragment comprising at least 80% of the full- length sequence of a variable heavy chain sequence of SEQ ID NO:8; SEQ ID NO:24; SEQ ID NO:40; SEQ ID NO:56; SEQ ID NO:72; or SEQ ID NO:88; or a fragment comprising at least 80% of the full-length of a variable light chain sequence of SEQ ID NO:16; SEQ ID NO:32; SEQ ID NO:48; SEQ ID NO:64; SEQ ID NO:80; or SEQ ID NO:96, or a combination thereof. In one embodiment, the nucleic acid molecule encoding the bispecific NKCE comprises a nucleotide sequence of SEQ ID NO:97, SEQ ID NO:99 or SEQ ID NO:101. In one embodiment, the invention provides a method of treating or preventing a disease or disorder in a subject in need thereof comprising administering a nucleic acid molecule of the invention to the subject. In one embodiment, the disease or disorder is selected from the group consisting of a disease or disorder associated with a bacterial infection, a disease or disorder associated with a viral infection, an autoimmune disease or disorder, a cancer, or a disease or disorder associated with cancer. In one embodiment, the cancer is selected from the group consisting of ovarian cancer, breast cancer, prostate cancer, renal cancer, colorectal cancer, stomach cancer, lung cancer, testicular cancer, skin cancer and endometrial cancer. In one embodiment, the invention provides a method of increasing natural killer cell function in a subject in need thereof comprising administering a nucleic acid molecule of the invention to the subject. In one embodiment, the invention provides a method of directing a natural killer cell to a target cell or particle in a subject in need thereof comprising administering a nucleic acid molecule of the invention to the subject. BRIEF DESCRIPTION OF THE DRAWINGS Figure 1A through Figure 1I depict a set of images showing generation of anti-human FSHR antibodies. (Figure 1A) Depiction of FSHR structure. (Figure 1B) Cloning strategy into pBMN-I-GFP expression vector. (Figure 1C) Mouse immunization scheme. (Figure 1D) cAMP response to different doses of FSH hormone of K562 and K562-FSHR. (Figure 1E) Western blot of phospho-Phospho-p44/42 (Erk1/2) and p44/42 (Erk1/2) 20 minutes after stimulation of K562 and K562-FSHR cells using 1µg/ml FSH. ANOVA. *** p<0.001. (F) Flow cytometry plot of CaOV3, OVCAR3 and TOV-21G stained with DDAP (the most potent down selected antibody clone) or no primary antibody followed secondary APC labelled antibody. (Figure 1G) Flow cytometry plot of TOV-21G parental or after CRISPR of FSHR stained with DDAP. (Figure 1H) Flow cytometry plot of K562, K562-FSHR and K562-LHCGR 21G stained with DDAP or no primary antibody followed secondary APC labelled antibody. (Figure 1I) Flow cytometry plot of A20(GFP-)/A20-Fhsr (GFP+) and ID8-Defb29/Vegf-a vs. ID8-Defb29/Vegf-a- Fshr cells stained with DDAP (both cell lines were transfected with murine FSHR). Figure 2A through Figure 2I depict a set of images showing that DDAP binds to FSHR in immunohistochemistry and immunocytochemistry and induces antibody-dependent cell mediated cytotoxicity. (Figure 2A) Immunohistochemistry images from frozen sections of tumors derived from K562, K562-FSHR, OVCAR3 and TOV-21G cell lines stained with DDAP.40X, Scale bar 50µm. (Figure 2B) Immunofluorescence images of 293T cells transfected with human FSHR and stained with either mouse anti-human FSHR or DDAP antibodies followed by secondary anti- mouse IgG. (Figure 2C) Immunofluorescence images of 293T cells transfected with murine FSHR and stained with either mouse anti-mouse FSHR or DDAP antibodies followed by secondary anti-mouse IgG. (Figure 2D) Immunofluorescence images of 293T cells transfected with pVax1 empty vector and stained with DDAP antibodies followed by secondary anti-mouse IgG. B-D: Scale bar 10 µm. (Figure 2E) Absorbance values of isotype ELISA performed on DDAP antibody. (Figure 2F) Cytotoxicity mediated by ADCC of DDAP or irrelevant mouse IgG2a (C1.18.4) against K562-FSHR. (Figure 2G) Cytotoxicity mediated by ADCC of DDAP or irrelevant mouse IgG2a (C1.18.4) against K562. (Figure 2H) Cytotoxicity mediated by ADCC of DDAP or irrelevant mouse IgG2a (C1.18.4) against OVCAR3 cells. t-test, ANOVA. ***p<0.001, ns not significant. (Figure 2I) In vitro cytotoxicity resulting from coculture of PBMCs with OVCAR3-FSHR cells at different concentrations of DDAP anti-FSHR antibody (1000 ng/ml, 500 ng/ml, 250 ng/ml and 31.25 ng/ml) or media alone. Modest dose dependent killing was observed; however, the killing potency was completely lost at 31.25 ng/ml. Figure 3A through Figure 3I depict is a series of images showing generation, expression, and antitumor activity of FSHR TCE. (Figure 3A) Cartoon of TCE engaging FSHR and the T cell receptor (TCR). GS, glycine-serine; VH, heavy chain variable region; VL, light chain variable region. (Figure 3B) Schematic of DNA construct encoding DDAP-TCE. (Figure 3C) Western blot of in vitro expression of DDAP-TCE or pVax1 empty vector after transfection in Expi293F cells. (Figure 3D)The binding specificity of DDAP-TCE was verified using K562 cells, which lack natural expression of FSHR. In FSHR-non expressing K562 cells, no binding of DDAP-TCE was overserved. (Figure 3E) Binding of DDAP-TCE to FSHR overexpressing K562 cells. (Figure 3F) Binding of DDAP-TCE to FSHR shown using additional FSHR expressing cell; CaOV3. Shift in the peak in DDAP-TCE compared to pVax1 and secondary Ab alone indicates its binding to FSHR. (Figure 3G) Binding of DDAP-TCE to FSHR shown using OVCAR3 cells transduced with FSHR encoding pBMN-I-GFP plasmid for overexpression of FSHR. There is a remarkable shift in peak in FSHR overexpressing OVCAR3 cells compared to empty vector and secondary antibody alone control. (Figure 3H) Flow staining of primary human T cells with DDAP-TCE and empty vector control (Figure 3I) In vitro cytotoxicity resulting from coculture of PBMCs (Effector cells; E) with OVCAR3-FSHR cells (Target cells; T) in the presence of in vitro produced DDAP- TCE at two different concentrations (31.25 ng/ml and 7.81 ng/ml) or media alone. Highly potent killing induced by DDAP-TCE was observed, the concentrations at which FSHR antibody alone was not able to induce killing of OVCAR3-FSHR cells indicating the enhanced potency of the designed TCE. Figure 4A through Figure 4L depict a series of images showing anti-Siglec 7 antibody clones induce specific killing of target ovarian cancer cells. Assessing the cytotoxic effect of DB-S7-1, DB-S7-2 and DB-S7-7 anti-Siglec 7 clones in non-target human cells; (Figure 4A& Figure 4B) A549 lung adenocarcinoma cells, (Figure 4C& Figure 4D) HaCaT human keratinocyte cells, (Figure 4E& Figure 4F) GMO5389 human fibroblast cells; as well as in target human ovarian cancer cells (Figure 4G& Figure 4H) OVISE cells, (Figure 4I& Figure 4J) OVCAR8 cells, (Figure 4K& Figure 4L) SKOV3 cells. In vitro cytotoxicity was measured based on impedance using xCELLigence real time cell analyzer equipment (RTCA), Agilent Technologies, USA. The electrical conductivity is converted into the unitless cell index (CI) parameter by the xCELLigence device in every 15 minutes and images were captured at the interval of 1 hour. The data generated are normalized as per the time point when the effector (E) cells (PBMCs), and antibodies were added to the target (T)cells (E:T=5:1 for all). The data were analyzed using RTCA/RTCA Pro Software. No non-specific killing was obtained in A549, HaCaT and GMO5389 cells, whereas potent killing was observed in OVISE, OVCAR8 and SKOV3 target OC cells. The specific killing efficacy of DB-S7-2 is found to be the highest. Arrow indicates the time point at which antibodies and effector cells were added to the target cells. Images shown display killing, 3 days after the addition of effector cells and antibodies. Figure 5A through Figure 5J depict a series showing design, expression, and functionality of human Siglec 7 DMAb in vitro. (Figure 5A) Schematic of dual plasmid DNA constructs encoding Siglec 7 DMAb. (Figure 5B) Western blot analysis of Siglec 7 DMAbs expressed in Expi293F cells. Numbers indicate molecular weight (kDa). (Figure 5C) Quantification of human IgG in human Siglec 7 DMAbs transfected Expi293F supernatant by ELISA. In vitro cytotoxicity induced by fully human Siglec 7 recombinant antibodies in (Figure 5D& Figure 5E) OVCAR8, (Figure 5F)TOV-21G, (Figure 5G) OVISE, and (Figure 5H) PEO-4 cells. All the recombinant antibodies effectively killed the mentioned panel of human ovarian cancer cells including BRCA2 mutated and PARPi resistant PEO-4 cells. DB-S7-2 recombinant ab is found to exhibit the highest killing efficacy. The killing ability of DB-S7-2 was further confirmed in two additional ovarian cancer cells; (Figure 5I) CaOV3 and (Figure 5J) OVCAR3 cells. Arrows indicate the time point at which antibodies and effector cells (human PBMCs) were added to target cells; E: T=5:1. Images shown in (Figure 5D) display killing in OVCAR8 target OC cells after 3 days of addition of human PBMCs and anti-Siglec 7 antibodies. Figure 6A through Figure 6G depict a series of images showing siglec 7 DMAbs express in vivo, delays cancer progression in ovarian cancer challenged model and FcγR blockage enhances Siglec 7 mediated NK cytotoxicity. (Figure 6A) Schematic of Human Siglec 7 DMAb administration into Balb/c mice. CD4 and CD8 T cells of the mice were first depleted using anti-mouse CD4 and anti-mouse CD8 (both from InVivoMab) antibodies. The mice were then electroporated with 50 µg of heavy chain+50 µg of Light chain human Siglec 7 DMAbs. Mice sera were collected at the time points indicated. (Figure 6B) Western blot of human IgG from mouse sera electroporated with DB-S7-1, DB-S7-2 and DB-S7-7 DMAbs, 14 days post DNA injection and electroporation or naïve sera. (Figure 6C) Staining of human NK cells with mouse sera electroporated with empty vector, DB-S7-1, DB-S7-2 and DB-S7-7 DMAbs, 14 days post DNA injection and electroporation or naïve sera along with irrelevant ab control and only secondary ab control. Day 14 sera of Siglec 7 DMAbs’ immunized mice showed positive and strong NK cell staining whereas no staining was observed in case of empty vector control, irrelevant Ab control or naïve sera. (Figure 6D) Schematic of Siglec 7 DMAb electroporation to NSG mice challenged with OVISE OC cells (Figure 6E) Growth curve of OVISE tumors grafted into NSG mice treated with Siglec 7 DMAbs or empty vector (n = 5 mice per group) (Figure 6F) xCELLigence real time analysis of OVCAR3 cells’ killing by DB-S7-2 human Ab in the presence and absence of Fc block (Figure 6G) Fc block led to enhanced Siglec 7 mediated NK toxicity in OVISE cells. Images were captured two days after addition of effector cells (E:T=5:1) and DB-S7-2 antibody to OVISE cells in the presence and absence of Fc block. Figure 7A through Figure 7H depict a series of images showing generation and expression of DDAP-NKCE and cytokine secretion profile and specificity analysis of FSHR targeted bispecific T and NK cell engagers. (Figure 7A) Schematic of DNA construct encoding DDAP-NKCE; GS, glycine-serine, ScFV: single chain variable fragment. (Figure 7B) Western blot of in vitro expression of DDAP-NKCE or pVax1 empty vector after transfection in expi293F cells. (Figure 7C) Flow cytometry plot of Siglec 7 overexpressing HEK293T cells stained with only secondary antibody, DDAP- TCE, commercial Siglec 7 antibody, DB-S7-2 anti-Siglec 7 ab and DDAP-NKCE. (Figure 7D) Flow cytometry plot of FSHR overexpressing K562 cells stained with secondary ab only, non-FSHR targeting TCE (IL13 Receptor alpha 2xCD3) and DDAP- NKCE. (Figure 7E) IFA analysis of DDAP-NKCE in Siglec 7 overexpressing HEK293T cells. Staining with only secondary antibody served as negative control. High resolution, confocal images of fixed cells were captured using a Leica TCS SP8 WLL scanning laser confocal microscope and Leica LAS-X software (Leica Microsystems, Inc., Buffalo Grove, IL). Image post-processing included importing into Huygens software for deconvolution (Scientific Volume Imaging, Laapersveld, Hilversum, The Netherlands). Fixed cell preparations were acquired using a 63X/1.40 oil objective, 2X zoom and a pinhole of 1 AU. Cells were labeled with DAPI (nuclei), GFP (Siglec 7) and Texas Red (DDAP-NKCE) and acquired with HyD detectors in sequence to maximize signal and minimize cross-talk. Scale bars are equivalent to 20.0 microns. (Figure 7F) Secretion profile of cytokines; sFas, and granulysin in the presence of DDAP-NKCE upon co culturing of OVCAR3-FSHR and human PBMCS; E:T=5:1. The supernatants analyzed for cytokine secretion profile were collected 48 hours after the addition of effectors cells and NKCE to target OVCAR3-FSHR cells. Two-way ANOVA; *P<0.05, **P<0.01, ***P < 0.001. (Figure 7G) Specificity analysis of FSHR targeting T and NK cell engagers in FSHR negative HEK293T cells. (Figure 7H) Images showing no cytotoxicity induced in HEK293T cells over 3 days post addition of effector cells (Human PBMCs; E:T=5:1) and DDAP-NKCE/DDAP-TCE . Figure 8A through Figure 8J depict is a series of images showing FSHR targeted bispecific T and NK cell engagers induced ovarian cancer cytotoxicity in vitro and in vivo. In vitro cytotoxicity resulting from co-culture of PBMCs with (Figure 8A & Figure 8B) OVISE cells, (Figure 8C & Figure 8D) CaOV3 cells, (Figure 8E) OVCAR3- FSHR cells, (Figure 8F) PEO-4 cells, and (Figure 8G) Kuramochi-FSHR cells in the presence and absence of DDAP-TCE/DDAP-NKCE. The real time in vitro cytotoxicity analysis was done by xCELLigence. E:T is 10:1(Figure 8A- Figure 8D) and 5:1(Figure 8E- Figure 8G); images shown (Figure 8B & Figure 8D) were captured 3 days after addition of human PBMCs and bispecifics to target cells. (Figure 8H) Comparison of the killing efficacy of DDAP-NKCE in the presence and absence of anti-Fas antibody. In the presence of anti-Fas ab, DDAP-NKCE led to reduced killing of target OVCAR3-FSHR cells; red line: E+T (only tumor cells and PBMCs as effector cells), grey line: tumor cells, PBMCs and anti-Fas ab, magenta line tumor cells, PBMCs and DDAP-NKCE and purple line: tumor cells, PBMCs and DDAP-NKCE in the presence of anti-Fas ab. (Figure 8I) Schematic of tumor study to evaluate the effect of bispecifics on tumor progression in OVCAR3-FSHR challenged NSG mice model. (Figure 8J) Average growth curve of OVCAR3-FSHR tumors grafted into NSG mice treated with DDAP- NKCE/DDAP-TCE or empty vector (n = 5 mice per group). Two-way ANOVA; *P<0.05, **P<0.01, ***P < 0.001. Figure 9A through Figure 9D depict is series of images showing screening of anti-human FSHR antibodies. (Figure 9A) Scheme of flow cytometry plots representing the potential outcomes in the screening process with K562 and K562-FSHR. (Figure 9B) Flow cytometry plot of K562 (GFP-)/K562-Fhsr (GFP+) cells stained with sera from mice immunized with human FSHR or empty vector at 1:1000 dilution and anti-mouse IgG APC. (Figure 9C) Representative of flow cytometric screening output strategy for detection of FSHR binding antibodies from hybridomas as flow plot and fold mean fluorescent intensity of K562-FSHR/K562 (Figure 9D) Waterfall plot depicting the hybridoma supernatant binding to FSHR measured as fold-MFI K562-FSHR/K562. After the first round of screening, experiments went forward with the top 20 clones (left of the red bar). Figure 10A through Figure 10C depict is a series of images showing anti- Siglec 7 antibodies bind efficiently to human Siglec7. (Figure 10A) Flow cytometry plot of Siglec 7 overexpressing HEK293T cells stained with DB-S7-1, DB-S7-2, DB-S7-7 anti-Siglec 7 clones and isotype control (anti-Siglec 3) (Figure 10B) Flow cytometry plot of Siglec 9 overexpressing HEK293T cells stained with DB-S7-1, DB-S7-2, DB-S7-7 anti-Siglec 7 clones and anti-Siglec 9 Ab (K8, Biolegend) (Figure 10C) IFA analysis of DB-S7-1, DB-S7-2 and DB-S7-7 anti-Siglec 7 clones in Siglec 7 overexpressing HEK293T cells. High resolution, confocal images of fixed cells were captured using a Leica TCS SP8 WLL scanning laser confocal microscope and Leica LAS-X software (Leica Microsystems, Inc., Buffalo Grove, IL). Image post-processing included importing into Huygens software for deconvolution (Scientific Volume Imaging, Laapersveld, Hilversum, The Netherlands). Fixed cell preparations were acquired using a 63X/1.40 oil objective, 2X zoom and a pinhole of 1 AU. Cells were labeled with DAPI (nuclei), GFP (Siglec 7) and Texas Red (Anti-Siglec 7) and acquired with HyD detectors in sequence to maximize signal and minimize crosstalk. Scale bars are equivalent to 20.0 microns. Figure 11A through Figure 11C depict is a set of images showing quantification of human IgG in the sera of mice immunized with Siglec 7 DMAbs. Balb/c mice (CD4 and CD8 T cells depleted) were electroporated with 50 µg of heavy chain+50 µg of light chain human Siglec 7 DMAbs. Mice sera were collected at different time points. Expression levels of human IgG quantified by ELISA from sera of mice electroporated with (Figure 11A) DB-S7-1 DMAb (Figure 11B) DB-S7-2 DMAb and (Figure 11C) DB-S7-7 DMAb (n = 5 mice per group). Figure 12 is a schematic of FcγR blocking on immune cells and its effect on Siglec 7 mediated toxicity. Figure 13A through Figure 13D depict a series of images showing FSHR targeted bispecific T and NK cell engagers induced ovarian cancer cytotoxicity in the presence of purified immune cells and no killing by non FSHR targeting NKCE. In vitro cytotoxicity resulting from co-culture of (Figure 13A) T cells with OVCAR3-FSHR cells in the presence of DDAP-TCE, (Figure 13B) NK cells with OVCAR3-FSHR cells in the presence of DDAP-NKCE. The real time in vitro cytotoxicity analysis was done by xCELLigence; E: T= 5:1 (Figure 13B) No toxicity induced in FSHR overexpressing OVCAR3 cells by a (Figure 13C) non FSHR targeting TCE; IL13Rα2-TCE and (Figure 13D) non FSHR targeting NKCE; IL13Rα2-NKCE in the presence of human PBMCs. Arrow indicates the time at which the effector cells and TCE/NKCE were added. Figure 14 is an image showing combination studies to engage both T cells and NK cells to target Kuramochi-FSHR cells. DDAP-NKCE and DDAP-TCE were combined at sub optimal doses to evaluate the combinatorial effect. The combination exhibited synergy against FSHR expressing Kuramochi cells; green line: where both DDAP-TCE and DDAP-NKCE were added. PBMCs were added as effector cells; E: T= 5:1. Arrow indicates the time point at which effector cells, and DDAP-TCE/NKCE/both were added. Figure 15 is an image demonstrating the development of an IL-13Ra2 targeting T cell engager. Figure 16 is an image showing treatment of GBM with IL-13Ra2 targeting T cell engager. Figure 17 is an image showing design of IL13Ra2 and Siglec 7 targeting bispecific NK cell engager. Figure 18 is an image showing IL13Ra2-NKCE did not induce killing of OVCAR or OVISE cells (ovarian cancer cells that do not express IL13Ra2). Figure 19 is an image showing expression of IL-13Ra2 on human melanoma cell lines. Figure 20 is an image showing melanoma cells cytotoxicity by IL13Ra2- NKCE. Figure 21A through Figure 21C depict the design and in vitro expression of Siglec-7 MAbs. (Figure 21A) Schematic of dual plasmid DNA constructs encoding Siglec-7 MAb. (Figure 21B) Expression analysis of Siglec-7 MAbs by western blot. Numbers indicate molecular weight (kDa). (Figure 21C) Quantification of human IgG in anti-Siglec-7 transfected Expi293F supernatant by ELISA. Figure 22A through Figure 22E depict the binding characterization of human Siglec-7 MAb in vitro. (Figure 22A) Binding of Siglec-7 MAbs to recombinant human Siglec-7, analyzed by ELISA. Dose dependent binding of DB7.1, DB7.2 and DB7.7 to human Siglec-7 was observed, whereas no binding in case of irrelevant control. (Figure 22B) Binding of human Siglec7 MAbs to Siglec-7 expressing HEK293T cells, analyzed by flow cytometry. No binding is observed in case of only secondary antibody control or Irrelevant MAb. There is binding in commercial Siglec-7 Ab (F023-420, BD Pharmingen) and Siglec-7 MAbs DB7.1, DB7.2 and DB7.3, with highest binding observed in DB7.2. (Figure 22C) Representative flow plots showing the binding of DB7.2 anti-Siglec-7 antibody to human NK and T cells. DB7.2 predominantly binds to NK cells. Positive (commercial flurochrome-conjugated mouse anti human Siglec-7 antibody) and negative controls (0 μg/ml DB7.2 or no secondary antibody) are shown (Figure 22D). Summary plot of DB7.2 anti-Siglec-7 binding to different immune populations analyzed in PBMCs from multiple donors (n=4). (Figure 22E) Binding analysis of DB7.2 anti-Siglec-7 Ab to CD56dim and CD56bright NK cell subsets (n=4). Figure 23 depicts a gating strategy used for flow cytometric analysis of Siglec-7 binding. Representative example of a ND is shown. The most stable acquisition was first selected. Then, to ensure that only live single cells were analyzed from mononuclear cells, forward scatter height (FSC-H)-versus-forward scatter area (FSC-A) and side scatter area (SSC-A)-versus-FSC-A plots were used to exclude doublets and focus on singlet small lymphocytes. Dead cells were excluded by gating on cells negative for the viability marker Aqua Blue and positive for CD45. CD4+ and CD8+ T lymphocytes were gated within CD3+ cells and NK cells were identified by CD56 and CD16 expression within the CD19-CD3- population. Figure 24A through Figure 24D depict the binding of Siglec-7 DMAb to human Siglec-7 protein. (Figure 24A) Binding of DB7.2 Siglec-7 DMAb to human Siglec-7 as analyzed by Western blot. There is no binding in irrelevant protein on in case of pVax1. (Figure 24B) SPR analysis of DB7.2 to Human Siglec-7 protein. Strong binding of DB7.2 was observed with a KD value of 44 pM. No binding of (Figure 24C) irrelevant ab to Siglec-7 or (Figure 24D) DB7.2 to irrelevant protein was observed, indicating the specificity of DB7.2 for human Siglec-7. Figure 25A through Figure 25I depict the in vitro cytotoxicity induced by human Siglec-7 MAbs. In vitro cytotoxicity induced by human Siglec-7 MAbs in non- target (Figure 25A&B) HaCaT human keratinocyte cells and target OC cells; (Figure 25C&D) OVCAR10, (Figure 25E) OVISE, (Figure 25F) PEO-4, and (Figure 25G) TOV- 21G cells. In vitro cytotoxicity was measured based on impedance using xCELLigence real time cell analyzer equipment (RTCA), Agilent Technologies, USA. The electrical conductivity is converted into cell index (CI) by the xCELLigence device in every 15 minutes. DB7.1, DB7.2 and DB7.7 did not induce killing in HaCaT cells. As shown in the images captured post 2 days of treatment, killing was not observed in No Ab control and as well as in DB7.1, DB7.2 and DB7.7 treated wells, indicating that they do not have any off target toxic effects. All the three Siglec-7 MAbs effectively killed the mentioned panel of human OC cells including BRCA2 mutated and PARPi resistant PEO-4 cells. DB7.2 MAb is found to exhibit the highest killing potency. The killing ability of DB7.2 was further confirmed in two additional OC cells; (Figure 25H) CaOV3 and (Figure 25I) OVCAR3 cells. Arrow indicates the time point at which antibodies and effector cells (human PBMCs) were added to target cells; E: T=5:1/10:1. Red: No Ab (Only Effector cells+ Target cells); Green: DB7.1 (Effector cells+ Target cells+ DB7.1); Blue: DB7.2 (Effector cells+ Target cells+DB7.2) and Yellow: DB7.7 (Effector cells+ Target cells+ DB7.7). Figure 26A through Figure 26C depict the ablation of FcR binding of Siglec-7 Mab. (Figure 26A) Schematic of FcR blocking on immune cells and its effect on Siglec-7 mediated killing. (Figure 26B) xCELLigence real time analysis of OVCAR3 cells’ killing by DB7.2 human MAb in the presence and absence of Fc block. (Figure 26C) Fc block maintained DB7.2 Siglec-7 MAb mediated NK toxicity in OVISE cells. Images were captured two days after addition of effector cells (E: T=5:1) and DB7.2 MAb to OVISE cells in the presence and absence of Fc block. Figure 27A through Figure 27I depict the ablation of FcR binding maintained the killing potential of Siglec-7 MAb and the combination of Siglec-7 MAb and anti-PD1 led to enhanced OC cell killing. (Figure 27A) Comparison of OVISE cells killing by DB7.2 and DB7.2_TM Mod. DB7.2_TM Mod is the variant of DB7.2 DMAb which contain triple-residue modifications (“TM”; L234F/ L235E/ P331S) in the Fc domain to ablate FcR and C1q binding. The killing potency of DB7.2_TM Mod was maintained in OVISE cells. Red: No Ab (Only Effector cells +Target cells); Dark blue: DB7.2 (Effector cells+Target cells+DB7.2); Light blue (Effector cells+Target cells+DB7.2_TM Mod). (Figure 27B) Images post 24 h of treatment with effector cells and DB7.2/DB7.2_TM Mod to target OVISE cells. Cell Index vs treatment dose curve for (Figure 27C) DB7.2 and (Figure 27D) DB7.2_TM Mod at 72 h of coculture of OVISE cells and human PBMCs. Cell Index vs treatment dose curve for (Figure 27E) DB7.2_TM Mod and (Figure 27F) anti-PD1 (Pembrolizumab) at 72 h of coculture of PEO4 cells and human PBMCs. Killing of target PEO4 cells by (Figure 27G) DB7.2_TM Mod, (Figure 27H) Anti-PD1 (Pembrolizumab) and (Figure 27I) individual treatment and combination of DB7.2_TM Mod and anti-PD1 in presence of human PBMCs; (E: T=5:1). The combination led to enhanced killing compared to individual CPI treatments. Figure 28A through Figure 28E depict Siglec-7 DNA delivered MAbs express in vivo and delays cancer progression in ovarian cancer challenged model. (Figure 28A) Schematic of Human Siglec-7 DNA delivered MAbs administration into Balb/c mice. CD4 and CD8 T cells of the mice were first depleted using antimouse CD4 and anti-mouse CD8 (both from InVivoMab) antibodies. The mice were then electroporated with 50 μg of heavy chain+50 μg of Light chain human Siglec-7 DMAbs. Mice sera were collected at the time points indicated. (Figure 28B) Staining of human NK cells with mouse sera electroporated with empty vector, DB7.1, DB7.2 and DB7.7, 14 days post DNA injection and electroporation or naive sera along with irrelevant control and only secondary Ab control. Day 14 sera of Siglec-7 MAbs’ immunized mice showed positive and strong NK cell staining whereas no staining was observed in case of empty vector control, irrelevant MAb or naive sera. (Figure 28C) Schematic of Siglec-7 DNA delivered MAb electroporation to NSG-K mice challenged with OVISE cells (Figure 28D) Growth curve of OVISE tumors grafted into NSG-K mice treated with DB7.2 or empty vector (n = 5 mice per group). (Figure 28E) Survival benefit in DB7.2 treated mice compared to empty vector control. DB7.2 treated group had significantly attenuated tumor burden and enhanced survival compared to pVax1 control group. Figure 29A and Figure 29B depict Siglec-7 DMAb impacted the tumor growth in OVISE challenged mice model. (Figure 29A) Individual growth curve of OVISE tumors grafted into NSG-K mice treated with DB7.2 DMAb or pVax1 empty vector (n = 5 mice per group). (Figure 29B) Representative images of ovarian tumor bearing mice treated with DB7.2 DMAb or pVax1 on Day 37. Figure 30A through Figure 30K depicts the generation, expression, binding, and specificity analysis of DB7.2xD2AP11: FSHR targeted bispecific NK cell engager. (Figure 30A) Schematic of DNA construct encoding DB7.2xD2AP11 NKCE; GS, glycine-serine, ScFV: single chain variable fragment. (Figure 30B) Western blot of in vitro expression of DB7.2xD2AP11 NKCE or pVax1 empty vector after transfection in expi293F cells. (Figure 30C) Flow cytometry plot of Siglec-7 overexpressing HEK293T cells stained with only secondary antibody, DB7.2xD2AP11 NKCE, Siglec-7 antibodies (F023-420/DB7.2) and DB7.2xD2AP11 NKCE. (Figure 30D) Flow cytometry plot of FSHR overexpressing K562 cells stained with secondary Ab only, non- FSHR targeting T cell engager (IL13 Receptor alpha2xCD3), D22AP11-TCE(FSHRxCD3) and DB7.2xD2AP11 NKCE. (Figure 30E) IFA of DB7.2xD2AP11 NKCE in Siglec-7 overexpressing HEK293T cells. Staining with only secondary Ab served as negative control. High resolution, confocal images of fixed cells were captured using a Leica TCS SP8 WLL scanning laser confocal microscope and Leica LAS-X software (Leica Microsystems, Inc., Buffalo Grove, IL). Image postprocessing included importing into Huygens software for deconvolution (Scientific Volume Imaging, Laapersveld, Hilversum, The Netherlands). Fixed cell preparations were acquired using a 63X/1.40 oil objective, 2X zoom and a pinhole of 1 AU. Cells were labeled with DAPI (nuclei), GFP (Siglec-7) and Texas Red (DB7.2xD2AP11 NKCE) and acquired with HyD detectors in sequence to maximize signal and minimize crosstalk. Scale bars are equivalent to 20.0 microns. Specificity analysis of DB7.2xD2AP11 NKCE in FSHR negative (Figure 30F&G) HEK293T, (Figure 30H) GM05389 (Figure 30I&J) AGS and (Figure 30K)WM3743 cells, using xCELLigence real time cell analyzer. Cell killing was not observed in any of these non FSHR expressing cells. Images show no cytotoxicity induced in HEK293T(G) and AGS(J) cells, post 3 days addition of effector cells (Human PBMCs; E:T=10:1) and DB7.2xD2AP11. Red: No Ab (Only Effector cells +Target cells); Purple: DB7.2xD2AP11 (Effector cells + Target cells+DB7.2xD2AP11 NKCE). Figure 31A through Figure 31I depicts FSHR targeted NK cell engager; DB7.2xD2AP11 NKCE induced ovarian cancer cytotoxicity in vitro. In vitro cytotoxicity induced by DB7.2xD2AP11 NKCE in presence of human PBMCs in (Figure 31A&B) OVISE cells, and (Figure 31C) OVCAR3-FSHR cells. (Figure 31D&E) CaOV3, (Figure 31F)Kuramochi-FSHR and (Figure 31G)PEO-4 cells in the presence of human PBMCs. The real time in vitro cytotoxicity analysis was done by xCELLigence. E:T is 10:1(A&B, F&G) and 5:1(C-E); images shown (B&E) were captured 3 days after addition of human PBMCs and the NKCE to target cells. (Figure 31H) Dose dependent cytolysis induced by DB7.2xD2AP11 NKCE in FSHR expressing OVISE cells in the presence of human PBMCs (E: T=5:1). IC50 value was obtained at 142.87 pM, indicating the efficacy of the NKCE. (Figure 31I) Cell index vs dose curve for DB7.2xD2AP11 NKCE in OVCAR3 cells. IC50 value was obtained at 236.6 pM, confirming its high potency. Figure 32A through Figure 32D depict the specificity analysis of FSHR targeted bispecific NK cell engager. (Figure 32A) In vitro cytotoxicity resulting from coculture of NK cells with OVCAR3-FSHR cells in the presence of DB7.2xD2AP11 NKCE. (Figure 32B) Killing of AGS (FSHR-negative) cells by anti-Siglec-7 MAb (DB7.2xD2AP11 NKCE did not induce killing of this cell line indicating the specificity of the bispecific engager approach). An irrelevant NKCE; DB7.2xIL13Rα2 NKCE did not induce toxicity in (Figure 32C) FSHR overexpressing OVCAR3 cells and (Figure 32D) OVISE cells in presence of human PBMCs. The real time in vitro cytotoxicity analysis was done by xCELLigence; E: T= 5:1. Arrow indicates the time at which the effector cells and NKCE were added. Figure 33A through Figure 33C depict the DB7.2xD2AP11 NKCE induced dose dependent cytotoxicity in target FSHR overexpressing OVSE cells. DB7.2xD2AP11 NKCE induced dose dependent killing in OVISE-FSHR cells in presence of human PBMCs obtained from 3 different healthy human donors (Figure 33A) ND578, (Figure 33B) ND502 and (Figure 33C) ND609, analyzed at different concentrations; 120, 60, 30, 15, 7.5, 3.75 and 1.875 ng/ml. Red lines indicate No Ab (Only Effector cells Target cells). In vitro cytotoxicity was measured based on impedance using xCELLigence real time cell analyzer. E:T=5:1; Arrow indicates the time at which effector cells and NKCE were added to the target OVISE-FSHR cells. Figure 34 depicts DB7.2xD2AP11 NKCE induced dose dependent cytotoxicity in target OVCAR3 cells. DB7.2xD2AP11 NKCE induced dose dependent killing in OVCAR3 cells in the presence of human PBMCs, analyzed at different concentrations; 120, 60, 30, 15, 7.5, 3.75 and 1.875 ng/ml. Red lines indicate No Ab (Only Effector cells Target cells). In vitro cytotoxicity was measured based on impedance using xCELLigence real time cell analyzer equipment. E:T=10:1, Arrow indicates the time at which effector cells and NKCE were added to the target OVCAR3 cells. Figure 35A through Figure 35E depict DB7.2xD2AP11 NKCE led to secretion of cytokines/cytotoxic molecules and impacted ovarian tumor growth in vivo. (Figure 35A) OVCAR3-FSHR cells were co cultured with human PBMCs in the presence and absence of DB7.2xD2AP11 NKCE. (Figure 35B) The supernatants were collected post 72 hours and analyzed for cytokine/cytotoxic molecule secretion profile. (Figure 35C) Schematic of tumor study to evaluate the effect of DB7.2xD2AP11 NKCE on tumor progression in OVCAR3-FSHR challenged NSG-K mice model. (Figure 35D) Average growth curve of OVCAR3-FSHR tumors grafted into NSG-K mice treated with DB7.2xD2AP11 NKCE or empty vector (n = 5 mice per group). (Figure 35E) Survival benefit in DB7.2xD2AP11 NKCE mice compared to empty vector control. Two-way ANOVA; *P<0.05, **P<0.01, ***P < 0.001. DETAILED DESCRIPTION The present invention relates to the development of a novel class of bispecific NK cell engager (NKCE) that simultaneously target both Siglec 7 and FSHR (DDAP NKCE). In another embodiment, the bispecific NKCE simultaneously target both Siglec 7 and IL13Ra2. In one aspect, the present invention relates to a composition that can be used to increase or enhance an immune response, i.e., create a more effective immune response, by administering the NKCEs, fragments thereof, variants thereof, or a nucleic acid molecule encoding the same. In one embodiment, the NKCE targets Siglec-7. In one aspect, the present invention relates to a NKCE comprising a combination of a sialic acid receptor antibody, or a fragment thereof, or variant thereof, and an antibody specific for binding to a tumor antigen, or a fragment thereof, or variant thereof. In some embodiments, the invention relates to a nucleic acid molecule encoding a NKCE comprising a combination of a sialic acid receptor antibody, or a fragment thereof, or variant thereof, and an antibody specific for binding to a tumor antigen, or a fragment thereof, or variant thereof. In one aspect, the present invention relates to methods of treating a disease or disorder in a subject in need thereof, comprising administering to the subject a NKCE, fragment thereof, variant thereof, or a nucleic acid molecule encoding the same. In one embodiment, the disease or disorder is cancer. In one embodiment, the disease or disorder is an infectious disease. In one embodiment, the present invention relates to methods of treating cancer or a disease or disorder associated therewith in a subject in need thereof, comprising administering to the subject a NKCE comprising a combination of a sialic acid receptor antibody, or a fragment thereof, or variant thereof, and an antibody specific for binding to a tumor antigen, viral glycoprotein, MHC binding antibody fragment, or a fragment thereof, or variant thereof, or a nucleic acid molecule encoding the same. Definitions Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. Although any methods and materials similar or equivalent to those described herein can be used in the practice or testing of the present invention, exemplary methods and materials are described. As used herein, each of the following terms has the meaning associated with it in this section. The articles “a” and “an” are used herein to refer to one or to more than one (i.e., to at least one) of the grammatical object of the article. By way of example, “an element” means one element or more than one element. “About” as used herein when referring to a measurable value such as an amount, a temporal duration, and the like, is meant to encompass variations of ±20%, ±10%, ±5%, ±1%, or ±0.1% from the specified value, as such variations are appropriate to perform the disclosed methods. “Antibody” may mean an antibody of classes IgG, IgM, IgA, IgD or IgE, or fragments, fragments or derivatives thereof, including Fab, F(ab')2, Fd, and single chain antibodies, and derivatives thereof. The antibody may be an antibody isolated from the serum sample of mammal, a polyclonal antibody, affinity purified antibody, or mixtures thereof which exhibits sufficient binding specificity to a desired epitope, or a sequence derived therefrom. “Antigen” refers to proteins that have the ability to generate an immune response in a host. An antigen may be recognized and bound by an antibody. An antigen may originate from within the body or from the external environment. “CDRs” are defined as the complementarity determining region amino acid sequences of an antibody which are the hypervariable regions of immunoglobulin heavy and light chains. See, e.g., Kabat et al., Sequences of Proteins of Immunological Interest, 4th Ed., U.S. Department of Health and Human Services, National Institutes of Health (1987). There are three heavy chain and three light chain CDRs (or CDR regions) in the variable portion of an immunoglobulin. Thus, “CDRs” as used herein refers to all three heavy chain CDRs, or all three light chain CDRs (or both all heavy and all light chain CDRs, if appropriate). The structure and protein folding of the antibody may mean that other residues are considered part of the antigen binding region and would be understood to be so by a skilled person. See for example Chothia et al., (1989) Conformations of immunoglobulin hypervariable regions; Nature 342, p 877-883. “Antibody fragment” or “fragment of an antibody” as used interchangeably herein refers to a portion of an intact antibody comprising the antigen- binding site or variable region. The portion does not include the constant heavy chain domains (i.e. CH2, CH3, or CH4, depending on the antibody isotype) of the Fc region of the intact antibody. Examples of antibody fragments include, but are not limited to, Fab fragments, Fab' fragments, Fab'-SH fragments, F(ab')2 fragments, Fd fragments, Fv fragments, diabodies, single-chain Fv (scFv) molecules, single-chain polypeptides containing only one light chain variable domain, single-chain polypeptides containing the three CDRs of the light-chain variable domain, single-chain polypeptides containing only one heavy chain variable region, and single-chain polypeptides containing the three CDRs of the heavy chain variable region. “Adjuvant” as used herein means any molecule added to the vaccine described herein to enhance the immunogenicity of the antigen. “Coding sequence” or “encoding nucleic acid” as used herein may refer to the nucleic acid (RNA or DNA molecule) that comprise a nucleotide sequence which encodes an antibody as set forth herein. The coding sequence may also comprise a DNA sequence which encodes an RNA sequence. The coding sequence may further include initiation and termination signals operably linked to regulatory elements including a promoter and polyadenylation signal capable of directing expression in the cells of an individual or mammal to whom the nucleic acid is administered. The coding sequence may further include sequences that encode signal peptides. “Complement” or “complementary” as used herein may mean a nucleic acid may have Watson-Crick (e.g., A-T/U and C-G) or Hoogsteen base pairing between nucleotides or nucleotide analogs of nucleic acid molecules. A “disease” is a state of health of an animal wherein the animal cannot maintain homeostasis, and wherein if the disease is not ameliorated then the animal’s health continues to deteriorate. In contrast, a “disorder” in an animal is a state of health in which the animal is able to maintain homeostasis, but in which the animal’s state of health is less favorable than it would be in the absence of the disorder. Left untreated, a disorder does not necessarily cause a further decrease in the animal’s state of health. A disease or disorder is “alleviated” if the severity of a sign or symptom of the disease or disorder, the frequency with which such a sign or symptom is experienced by a patient, or both, is reduced. “Encoding” refers to the inherent property of specific sequences of nucleotides in a polynucleotide, such as a gene, a cDNA, or an mRNA, to serve as templates for synthesis of other polymers and macromolecules in biological processes having either a defined sequence of nucleotides (i.e., rRNA, tRNA and mRNA) or a defined sequence of amino acids and the biological properties resulting therefrom. Thus, a gene encodes a protein if transcription and translation of mRNA corresponding to that gene produces the protein in a cell or other biological system. Both the coding strand, the nucleotide sequence of which is identical to the mRNA sequence and is usually provided in sequence listings, and the non-coding strand, used as the template for transcription of a gene or cDNA, can be referred to as encoding the protein or other product of that gene or cDNA. An “effective amount” of a compound is that amount of compound which is sufficient to provide an effect to the subject or system to which the compound is administered. “Expression vector” refers to a vector comprising a recombinant polynucleotide comprising expression control sequences operatively linked to a nucleotide sequence to be expressed. An expression vector comprises sufficient cis-acting elements for expression; other elements for expression can be supplied by the host cell or in an in vitro expression system. Expression vectors include all those known in the art, such as cosmids, plasmids (e.g., naked or contained in liposomes) and viruses (e.g., lentiviruses, retroviruses, adenoviruses, and adeno-associated viruses) that incorporate the recombinant polynucleotide. “Feedback mechanism” as used herein may refer to a process performed by either software or hardware (or firmware), which process receives and compares the impedance of the desired tissue (before, during, and/or after the delivery of pulse of energy) with a present value, preferably current, and adjusts the pulse of energy delivered to achieve the preset value. A feedback mechanism may be performed by an analog closed loop circuit. “Fragment” may mean a polypeptide fragment of an antibody that is function, i.e., can bind to desired target and have the same intended effect as a full length antibody. A fragment of an antibody may be 100% identical to the full length except missing at least one amino acid from the N and/or C terminal, in each case with or without signal peptides and/or a methionine at position 1. Fragments may comprise 20% or more, 25% or more, 30% or more, 35% or more, 40% or more, 45% or more, 50% or more, 55% or more, 60% or more, 65% or more, 70% or more, 75% or more, 80% or more, 85% or more, 90% or more, 91% or more, 92% or more, 93% or more, 94% or more, 95% or more, 96% or more, 97% or more, 98% or more, 99% or more percent of the length of the particular full length antibody, excluding any heterologous signal peptide added. The fragment may comprise a fragment of a polypeptide that is 95% or more, 96% or more, 97% or more, 98% or more or 99% or more identical to the antibody and additionally comprise an N terminal methionine or heterologous signal peptide which is not included when calculating percent identity. Fragments may further comprise an N terminal methionine and/or a signal peptide such as an immunoglobulin signal peptide, for example an IgE or IgG signal peptide. The N terminal methionine and/or signal peptide may be linked to a fragment of an antibody. A fragment of a nucleic acid sequence that encodes an antibody may be 100% identical to the full length except missing at least one nucleotide from the 5' and/or 3' end, in each case with or without sequences encoding signal peptides and/or a methionine at position 1. Fragments may comprise 20% or more, 25% or more, 30% or more, 35% or more, 40% or more, 45% or more, 50% or more, 55% or more, 60% or more, 65% or more, 70% or more, 75% or more, 80% or more, 85% or more, 90% or more, 91% or more, 92% or more, 93% or more, 94% or more, 95% or more, 96% or more, 97% or more, 98% or more, 99% or more percent of the length of the particular full length coding sequence, excluding any heterologous signal peptide added. The fragment may comprise a fragment that encode a polypeptide that is 95% or more, 96% or more, 97% or more, 98% or more or 99% or more identical to the antibody and additionally optionally comprise sequence encoding an N terminal methionine or heterologous signal peptide which is not included when calculating percent identity. Fragments may further comprise coding sequences for an N terminal methionine and/or a signal peptide such as an immunoglobulin signal peptide, for example an IgE or IgG signal peptide. The coding sequence encoding the N terminal methionine and/or signal peptide may be linked to a fragment of coding sequence. “Genetic construct” as used herein refers to the DNA or RNA molecules that comprise a nucleotide sequence which encodes a protein, such as an antibody. The genetic construct may also refer to a DNA molecule which transcribes an RNA. The coding sequence includes initiation and termination signals operably linked to regulatory elements including a promoter and polyadenylation signal capable of directing expression in the cells of the individual to whom the nucleic acid molecule is administered. As used herein, the term “expressible form” refers to gene constructs that contain the necessary regulatory elements operable linked to a coding sequence that encodes a protein such that when present in the cell of the individual, the coding sequence will be expressed. “Homologous” refers to the sequence similarity or sequence identity between two polypeptides or between two nucleic acid molecules. When a position in both of the two compared sequences is occupied by the same base or amino acid monomer subunit, e.g., if a position in each of two DNA molecules is occupied by adenine, then the molecules are homologous at that position. The percent of homology between two sequences is a function of the number of matching or homologous positions shared by the two sequences divided by the number of positions compared X 100. For example, if 6 of 10 of the positions in two sequences are matched or homologous then the two sequences are 60% homologous. By way of example, the DNA sequences ATTGCC and TATGGC share 50% homology. Generally, a comparison is made when two sequences are aligned to give maximum homology. “Identical” or “identity” as used herein in the context of two or more nucleic acids or polypeptide sequences means that the sequences have a specified percentage of residues that are the same over a specified region. The percentage can be calculated by optimally aligning the two sequences, comparing the two sequences over the specified region, determining the number of positions at which the identical residue occurs in both sequences to yield the number of matched positions, dividing the number of matched positions by the total number of positions in the specified region, and multiplying the result by 100 to yield the percentage of sequence identity. In cases where the two sequences are of different lengths or the alignment produces one or more staggered ends and the specified region of comparison includes only a single sequence, the residues of the single sequence are included in the denominator but not the numerator of the calculation. When comparing DNA and RNA, thymine (T) and uracil (U) can be considered equivalent. Identity can be performed manually or by using a computer sequence algorithm such as BLAST or BLAST 2.0. “Isolated” means altered or removed from the natural state. For example, a nucleic acid or a peptide naturally present in a living animal is not “isolated,” but the same nucleic acid or peptide partially or completely separated from the coexisting materials of its natural state is “isolated.” An isolated nucleic acid or protein can exist in substantially purified form, or can exist in a non-native environment such as, for example, a host cell. In the context of the present invention, the following abbreviations for the commonly occurring nucleic acid bases are used. “A” refers to adenosine, “C” refers to cytosine, “G” refers to guanosine, “T” refers to thymidine, and “U” refers to uridine. Unless otherwise specified, a “nucleotide sequence encoding an amino acid sequence” includes all nucleotide sequences that are degenerate versions of each other and that encode the same amino acid sequence. The phrase nucleotide sequence that encodes a protein or an RNA may also include introns to the extent that the nucleotide sequence encoding the protein may in some version contain an intron(s). “Impedance” as used herein may be used when discussing the feedback mechanism and can be converted to a current value according to Ohm's law, thus enabling comparisons with the preset current. “Immune response” as used herein may mean the activation of a host’s immune system, e.g., that of a mammal, in response to the introduction of one or more nucleic acids and/or peptides. The immune response can be in the form of a cellular or humoral response, or both. The terms “patient,” “subject,” “individual,” and the like are used interchangeably herein, and refer to any animal, or cells thereof whether in vitro or in situ, amenable to the methods described herein. In some embodiments, the patient, subject or individual is a human. “Parenteral” administration of a composition includes, e.g., subcutaneous (s.c.), intravenous (i.v.), intramuscular (i.m.), or intradermal injection, or infusion techniques. “Nucleic acid” or “oligonucleotide” or “polynucleotide” as used herein may mean at least two nucleotides covalently linked together. The depiction of a single strand also defines the sequence of the complementary strand. Thus, a nucleic acid also encompasses the complementary strand of a depicted single strand. Many variants of a nucleic acid may be used for the same purpose as a given nucleic acid. Thus, a nucleic acid also encompasses substantially identical nucleic acids and complements thereof. A single strand provides a probe that may hybridize to a target sequence under stringent hybridization conditions. Thus, a nucleic acid also encompasses a probe that hybridizes under stringent hybridization conditions. Nucleic acids may be single stranded or double stranded or may contain portions of both double stranded and single stranded sequence. The nucleic acid may be DNA, both genomic and cDNA, RNA, or a hybrid, where the nucleic acid may contain combinations of deoxyribo- and ribo-nucleotides, and combinations of bases including uracil, adenine, thymine, cytosine, guanine, inosine, xanthine hypoxanthine, isocytosine and isoguanine. Nucleic acids may be obtained by chemical synthesis methods or by recombinant methods. “Operably linked” as used herein may mean that expression of a gene is under the control of a promoter with which it is spatially connected. A promoter may be positioned 5' (upstream) or 3' (downstream) of a gene under its control. The distance between the promoter and a gene may be approximately the same as the distance between that promoter and the gene it controls in the gene from which the promoter is derived. As is known in the art, variation in this distance may be accommodated without loss of promoter function. A “peptide,” “protein,” or “polypeptide” as used herein can mean a linked sequence of amino acids and can be natural, synthetic, or a modification or combination of natural and synthetic. “Promoter” as used herein may mean a synthetic or naturally-derived molecule which is capable of conferring, activating or enhancing expression of a nucleic acid in a cell. A promoter may comprise one or more specific transcriptional regulatory sequences to further enhance expression and/or to alter the spatial expression and/or temporal expression of same. A promoter may also comprise distal enhancer or repressor elements, which can be located as much as several thousand base pairs from the start site of transcription. A promoter may be derived from sources including viral, bacterial, fungal, plants, insects, and animals. A promoter may regulate the expression of a gene component constitutively or differentially with respect to cell, the tissue or organ in which expression occurs or, with respect to the developmental stage at which expression occurs, or in response to external stimuli such as physiological stresses, pathogens, metal ions, or inducing agents. Representative examples of promoters include the bacteriophage T7 promoter, bacteriophage T3 promoter, SP6 promoter, lac operator-promoter, tac promoter, SV40 late promoter, SV40 early promoter, RSV-LTR promoter, CMV IE promoter, SV40 early promoter or SV 40 late promoter and the CMV IE promoter. As used herein, the term “promoter/regulatory sequence” means a nucleic acid sequence which is required for expression of a gene product operably linked to the promoter/regulatory sequence. In some instances, this sequence may be the core promoter sequence and in other instances, this sequence may also include an enhancer sequence and other regulatory elements which are required for expression of the gene product. The promoter/regulatory sequence may, for example, be one which expresses the gene product in a tissue specific manner. A “constitutive” promoter is a nucleotide sequence which, when operably linked with a polynucleotide which encodes or specifies a gene product, causes the gene product to be produced in a cell under most or all physiological conditions of the cell. An “inducible” promoter is a nucleotide sequence which, when operably linked with a polynucleotide which encodes or specifies a gene product, causes the gene product to be produced in a cell substantially only when an inducer which corresponds to the promoter is present in the cell. A “tissue-specific” promoter is a nucleotide sequence which, when operably linked with a polynucleotide encodes or specified by a gene, causes the gene product to be produced in a cell substantially only if the cell is a cell of the tissue type corresponding to the promoter. “Signal peptide” and “leader sequence” are used interchangeably herein and refer to an amino acid sequence that can be linked at the amino terminus of a protein set forth herein. Signal peptides/leader sequences typically direct localization of a protein. Signal peptides/leader sequences used herein may facilitate secretion of the protein from the cell in which it is produced. Signal peptides/leader sequences are often cleaved from the remainder of the protein, often referred to as the mature protein, upon secretion from the cell. Signal peptides/leader sequences are linked at the N terminus of the protein. “Stringent hybridization conditions” as used herein may mean conditions under which a first nucleic acid sequence (e.g., probe) will hybridize to a second nucleic acid sequence (e.g., target), such as in a complex mixture of nucleic acids. Stringent conditions are sequence dependent and will be different in different circumstances. Stringent conditions may be selected to be about 5-10°C lower than the thermal melting point (T _m ) for the specific sequence at a defined ionic strength pH. The T _m may be the temperature (under defined ionic strength, pH, and nucleic concentration) at which 50% of the probes complementary to the target hybridize to the target sequence at equilibrium (as the target sequences are present in excess, at T _m , 50% of the probes are occupied at equilibrium). Stringent conditions may be those in which the salt concentration is less than about 1.0 M sodium ion, such as about 0.01-1.0 M sodium ion concentration (or other salts) at pH 7.0 to 8.3 and the temperature is at least about 30°C for short probes (e.g., about 10-50 nucleotides) and at least about 60°C for long probes (e.g., greater than about 50 nucleotides). Stringent conditions may also be achieved with the addition of destabilizing agents such as formamide. For selective or specific hybridization, a positive signal may be at least 2 to 10 times background hybridization. Exemplary stringent hybridization conditions include the following: 50% formamide, 5x SSC, and 1% SDS, incubating at 42°C, or, 5x SSC, 1% SDS, incubating at 65°C, with wash in 0.2x SSC, and 0.1% SDS at 65°C. “Subject” and “patient” as used herein interchangeably refers to any vertebrate, including, but not limited to, a mammal (e.g., cow, pig, camel, llama, horse, goat, rabbit, sheep, hamsters, guinea pig, cat, dog, rat, and mouse, a non-human primate (for example, a monkey, such as a cynomolgous or rhesus monkey, chimpanzee, etc) and a human). In some embodiments, the subject may be a human or a non-human. The subject or patient may be undergoing other forms of treatment. “Substantially complementary” as used herein may mean that a first sequence is at least 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the complement of a second sequence over a region of 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100 or more nucleotides or amino acids, or that the two sequences hybridize under stringent hybridization conditions. “Substantially identical” as used herein may mean that a first and second sequence are at least 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical over a region of 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 200, 300, 400, 500, 600, 700, 800, 900, 1000, 1100 or more nucleotides or amino acids, or with respect to nucleic acids, if the first sequence is substantially complementary to the complement of the second sequence. “Synthetic antibody” as used herein refers to an antibody that is encoded by the recombinant nucleic acid sequence described herein and is generated in a subject. “Treatment” or “treating,” as used herein can mean protecting of a subject from a disease through means of preventing, suppressing, repressing, or completely eliminating the disease. Preventing the disease involves administering a vaccine of the present invention to a subject prior to onset of the disease. Suppressing the disease involves administering a vaccine of the present invention to a subject after induction of the disease but before its clinical appearance. Repressing the disease involves administering a vaccine of the present invention to a subject after clinical appearance of the disease. A “therapeutic” treatment is a treatment administered to a subject who exhibits signs or symptoms of a disease or disorder, for the purpose of diminishing or eliminating the frequency or severity of those signs or symptoms. As used herein, “treating a disease or disorder” means reducing the frequency or severity, or both, of at least one sign or symptom of the disease or disorder experienced by a patient. The phrase “therapeutically effective amount,” as used herein, refers to an amount that is sufficient or effective to prevent or treat (delay or prevent the onset of, prevent the progression of, inhibit, decrease or reverse) a disease or disorder, including alleviating signs and/or symptoms of such diseases and disorders. To “treat” a disease or disorder as the term is used herein, means to reduce the frequency or severity of at least one sign or symptom of a disease or disorder experienced by a subject. “Variant” used herein with respect to a nucleic acid means (i) a portion or fragment of a referenced nucleotide sequence; (ii) the complement of a referenced nucleotide sequence or portion thereof; (iii) a nucleic acid that is substantially identical to a referenced nucleic acid or the complement thereof; or (iv) a nucleic acid that hybridizes under stringent conditions to the referenced nucleic acid, complement thereof, or a sequences substantially identical thereto. Variant can further be defined as a peptide or polypeptide that differs in amino acid sequence by the insertion, deletion, or conservative substitution of amino acids, but retain at least one biological activity. Representative examples of “biological activity” include the ability to be bound by a specific antibody or to promote an immune response. Variant can also mean a protein with an amino acid sequence that is substantially identical to a referenced protein with an amino acid sequence that retains at least one biological activity. A conservative substitution of an amino acid, i.e., replacing an amino acid with a different amino acid of similar properties (e.g., hydrophilicity, degree and distribution of charged regions) is recognized in the art as typically involving a minor change. These minor changes can be identified, in part, by considering the hydropathic index of amino acids, as understood in the art. Kyte et al., J. Mol. Biol. 157:105-132 (1982). The hydropathic index of an amino acid is based on a consideration of its hydrophobicity and charge. It is known in the art that amino acids of similar hydropathic indexes can be substituted and still retain protein function. In one aspect, amino acids having hydropathic indexes of ±2 are substituted. The hydrophilicity of amino acids can also be used to reveal substitutions that would result in proteins retaining biological function. A consideration of the hydrophilicity of amino acids in the context of a peptide permits calculation of the greatest local average hydrophilicity of that peptide, a useful measure that has been reported to correlate well with antigenicity and immunogenicity. Substitution of amino acids having similar hydrophilicity values can result in peptides retaining biological activity, for example immunogenicity, as is understood in the art. Substitutions can be performed with amino acids having hydrophilicity values within ±2 of each other. Both the hydrophobicity index and the hydrophilicity value of amino acids are influenced by the particular side chain of that amino acid. Consistent with that observation, amino acid substitutions that are compatible with biological function are understood to depend on the relative similarity of the amino acids, and particularly the side chains of those amino acids, as revealed by the hydrophobicity, hydrophilicity, charge, size, and other properties. A variant may be a nucleic acid sequence that is substantially identical over the full length of the full gene sequence or a fragment thereof. The nucleic acid sequence may be 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical over the full length of the gene sequence or a fragment thereof. A variant may be an amino acid sequence that is substantially identical over the full length of the amino acid sequence or fragment thereof. The amino acid sequence may be 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical over the full length of the amino acid sequence or a fragment thereof. A “vector” is a composition of matter which comprises an isolated nucleic acid and which can be used to deliver the isolated nucleic acid to the interior of a cell. Numerous vectors are known in the art including, but not limited to, linear polynucleotides, polynucleotides associated with ionic or amphiphilic compounds, plasmids, and viruses. Thus, the term “vector” includes an autonomously replicating plasmid or a virus. The term should also be construed to include non-plasmid and non- viral compounds which facilitate transfer of nucleic acid into cells, such as, for example, polylysine compounds, liposomes, and the like. Examples of viral vectors include, but are not limited to, adenoviral vectors, adeno-associated virus vectors, retroviral vectors, and the like. Ranges: throughout this disclosure, various aspects of the invention can be presented in a range format. It should be understood that the description in range format is merely for convenience and brevity and should not be construed as an inflexible limitation on the scope of the invention. Accordingly, the description of a range should be considered to have specifically disclosed all the possible subranges as well as individual numerical values within that range. For example, description of a range such as from 1 to 6 should be considered to have specifically disclosed subranges such as from 1 to 3, from 1 to 4, from 1 to 5, from 2 to 4, from 2 to 6, from 3 to 6 etc., as well as individual numbers within that range, for example, 1, 2, 2.7, 3, 4, 5, 5.3, and 6. This applies regardless of the breadth of the range. Description Provided herein are NKCEs comprising a domain which specifically binds to a sialic acid-binding receptor, a fragment thereof, a variant thereof, and further comprising a domain which specifically binds to an antigen expressed by a target cell of interest, and nucleic acid molecules encoding the same. In one embodiment, the sialic acid-binding receptor is a sialic acid binding immunoglobulin type lectin (Siglec) polypeptide or a selectin polypeptide. In one embodiment the NKCEs are specific for binding to Siglec-7 which directly engage NK cells and can direct killing and clearance of pathogenic cells. In one embodiment, the invention provides immunogenic compositions comprising a NKCE of the invention or a nucleic acid molecule encoding the same. The immunogenic compositions of the invention can be used to protect against diseases or disorders, including, but not limited to, cancers and infectious disease. In some embodiments, the immunogenic compositions of the invention can be used for cell specific targeting of glycoproteins on cancer cells, autoimmune cells or infected target cells. Therefore, in some embodiments, the invention provides compositions comprising a nucleic acid molecule encoding one or more NKCE comprising a domain which specifically binds to a sialic acid-binding receptor, a fragment thereof, a variant thereof, and further comprising a domain which specifically binds to an antigen expressed by a target cell of interest. In some embodiments, the invention provides methods of treating or preventing a disease or disorder comprising administering to a subject or a bispecific sialic acid-binding receptor antibody of the invention or a nucleic acid molecule encoding the same. In some embodiments, the invention provides methods of treating or preventing a cancer comprising administering to a subject a bispecific sialic acid-binding receptor antibody, a fragment thereof, or a variant thereof, comprising a domain which specifically binds to a sialic acid-binding receptor, a fragment thereof, a variant thereof, and further comprising a domain which specifically binds to a cancer antigen, or a nucleic acid molecule encoding the same. Antibody compositions In some embodiments, the invention relates to compositions comprising at least one NKCE comprising a domain specific for binding to a sialic acid-binding receptor. In one embodiment, the sialic acid-binding receptor is a Siglec polypeptide or a selectin polypeptide. In one embodiment, the Siglec is Siglec-7. In one embodiment, the invention relates to compositions comprising a NKCE comprising at least one Silgec-7 binding domain, or fragment thereof. In one embodiment, the Silgec-7 binding domain of the bispecific NKCE, or fragment thereof, comprises a variable heavy chain sequence of SEQ ID NO: 4, SEQ ID NO: 20, SEQ ID NO: 36, SEQ ID NO: 52, SEQ ID NO: 68, or SEQ ID NO: 84. In one embodiment, the Silgec-7 binding domain of the bispecific NKCE, or fragment thereof, comprises a variable light chain sequence of SEQ ID NO: 12, SEQ ID NO: 28, SEQ ID NO: 44, SEQ ID NO: 60, SEQ ID NO: 76, or SEQ ID NO: 92. In one embodiment, the bispecific NKCE, or fragment thereof, comprises a sequence of SEQ ID NO: 98, SEQ ID NO: 100, or SEQ ID NO: 102. In some embodiments, a variant of an amino acid sequence as described herein comprises at least about 60% identity, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93% ,94%, 95%, 96%, 97%, 98%, 99% or higher identity over a specified region when compared to a defined amino acid sequence. In some embodiments, a variant of an amino acid sequence as described herein comprises at least about 60% identity, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93% ,94%, 95%, 96%, 97%, 98%, 99% or higher identity over the full length of an amino acid sequence of at least one of SEQ ID NO: 4, SEQ ID NO: 12, SEQ ID NO: 20, SEQ ID NO: 28, SEQ ID NO: 36, SEQ ID NO: 44, SEQ ID NO: 52, SEQ ID NO: 60, SEQ ID NO: 68, SEQ ID NO: 76, SEQ ID NO: 84, SEQ ID NO: 92, SEQ ID NO:98, SEQ ID NO:100, or SEQ ID NO:102. In some embodiments, a fragment of an amino acid sequence as described herein comprises at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93% ,94%, 95%, 96%, 97%, 98%, or 99% of the full length sequence of a defined amino acid sequence. In some embodiments, a fragment of an amino acid sequence as described herein comprises at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93% ,94%, 95%, 96%, 97%, 98%, or 99% of the full length sequence of at least one of SEQ ID NO: 4, SEQ ID NO: 12, SEQ ID NO: 20, SEQ ID NO: 28, SEQ ID NO: 36, SEQ ID NO: 44, SEQ ID NO: 52, SEQ ID NO: 60, SEQ ID NO: 68, SEQ ID NO: 76, SEQ ID NO: 84, SEQ ID NO: 92, SEQ ID NO:98, SEQ ID NO:100, or SEQ ID NO:102. As used herein, the term "antibody" or "immunoglobulin" refers to proteins (including glycoproteins) of the immunoglobulin (Ig) superfamily of proteins. An antibody or immunoglobulin (Ig) molecule may be tetrameric, comprising two identical light chain polypeptides and two identical heavy chain polypeptides. The two heavy chains are linked together by disulfide bonds, and each heavy chain is linked to a light chain by a disulfide bond. Each full-length Ig molecule contains at least two binding sites for a specific target or antigen. A sialic acid-binding receptor antibody, or antigen-binding fragment thereof, includes, but is not limited to a polyclonal antibody, a monoclonal fusion proteins, antibodies or fragments thereof , chimerized or chimeric fusion proteins, antibodies or fragments thereof , humanized fusion proteins, antibodies or fragments thereof , deimmunized humfusion proteins, antibodies or fragments thereof , fully humfusion proteins, antibodies or fragments thereof , single chain antibody, single chain Fv fragment (scFv), Fv, Fd fragment, Fab fragment, Fab' fragment, F(ab')2 fragment, diabody or antigen- binding fragment thereof, minibody or antigen-binding fragment thereof, triabody or antigen- binding fragment thereof, domain fusion proteins, antibodies or fragments thereof , camelid fusion proteins, antibodies or fragments thereof , dromedary fusion proteins, antibodies or fragments thereof , phage-displayed fusion proteins, antibodies or fragments thereof , or antibody, or antigen- binding fragment thereof, identified with a repetitive backbone array (e.g. repetitive antigen display). The immune system produces several different classes of Ig molecules (isotypes), including IgA, IgD, IgE, IgG, and IgM, each distinguished by the particular class of heavy chain polypeptide present: alpha (a) found in IgA, delta (δ) found in IgD, epsilon (ε) found in IgE, gamma (γ) found in IgG, and mu (μ) found in IgM. There are at least five different γ heavy chain polypeptides (isotypes) found in IgG. In contrast, there are only two light chain polypeptide isotypes, referred to as kappa (κ) and lambda (λ) chains. The distinctive characteristics of antibody isotypes are defined by sequences of the constant domains of the heavy chain. An IgG molecule comprises two light chains (either κ or λ form) and two heavy chains (γ form) bound together by disulfide bonds. The κ and λ forms of IgG light chain each contain a domain of relatively variable amino acid sequences, called the variable region (variously referred to as a "V _L -," "V _κ -," or " ^" V _λ -region") and a domain of relatively conserved amino acid sequences, called the constant region (C _L -region). Similarly, each IgG heavy chain contains a variable region (VH-region) and one or more conserved regions: a complete IgG heavy chain contains three constant domains ("C _H 1-," " C _H 2-," and " C _H 3-regions") and a hinge region. Within each V _L - or V _H -region, hypervariable regions, also known as complementarity-determining regions ("CDR"), are interspersed between relatively conserved framework regions ("FR"). Generally, the variable region of a light or heavy chain polypeptide contains four FRs and three CDRs arranged in the following order along the polypeptide: NH2-FR1-CDR1-FR2-CDR2-FR3- CDR3-FR4-COOH. Together the CDRs and FRs determine the three-dimensional structure of the IgG binding site and thus, the specific target protein or antigen to which that IgG molecule binds. Each IgG molecule is dimeric, able to bind two antigen molecules. Cleavage of a dimeric IgG with the protease papain produces two identical antigen-binding fragments ("Fab"') and an "Fc" fragment or Fc domain, so named because it is readily crystallized. As used throughout the present disclosure, the term "antibody" further refers to a whole or intact antibody (e.g., IgM, IgG, IgA, IgD, or IgE) molecule that is generated by any one of a variety of methods that are known in the art and described herein. The term "antibody" includes a polyclonal antibody, a monoclonal antibody, a chimerized or chimeric antibody, a humanized antibody, a deimmunized human antibody, and a fully human antibody. The antibody can be made in or derived from any of a variety of species, e.g., mammals such as humans, non-human primates (e.g., monkeys, baboons, or chimpanzees), horses, cattle, pigs, sheep, goats, dogs, cats, rabbits, guinea pigs, gerbils, hamsters, rats, and mice. The antibody can be a purified or a recombinant antibody. As used herein, the term "epitope" refers to the site on a protein that is bound by an antibody. "Overlapping epitopes" include at least one (e.g., two, three, four, five, or six) common amino acid residue(s). In one embodiment, the antibody of the invention specifically binds to a Siglec polypeptide. As used herein, the terms "specific binding" or "specifically binds" refer to two molecules forming a complex that is relatively stable under physiologic conditions. Typically, binding is considered specific when the association constant (K _a ) is higher than 10 ⁶ M-1. Thus, an antibody can specifically bind to a target with a Ka of at least (or greater than) 10 ⁶ (e.g., at least or greater than 10 ⁷ , 10 ⁸ , 10 ⁹ , 10 ¹⁰ , 10 ¹¹ , 10 ¹² , 10 ¹³ , 10 ¹⁴ , or 10 ¹⁵ or higher) M ^-1 . In one embodiment, the NKCE of the invention comprises a domain that specifically binds to Siglec-7. Methods for determining whether an antibody binds to a protein antigen and/or the affinity for an antibody to a protein antigen are known in the art. For example, the binding of an antibody to a protein antigen can be detected and/or quantified using a variety of techniques such as, but not limited to, Western blot, dot blot, surface plasmon resonance method (e.g., BIAcore system; Pharmacia Biosensor AB, Uppsala, Sweden and Piscataway, N.J.), or enzyme-linked immunosorbent assays (ELISA). See, e.g., Harlow and Lane (1988) "Antibodies: A Laboratory Manual" Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.; Benny K. C. Lo (2004) "Antibody Engineering: Methods and Protocols," Humana Press (ISBN: 1588290921); Borrebaek (1992) "Antibody Engineering, A Practical Guide," W.H. Freeman and Co., NY; Borrebaek (1995) "Antibody Engineering," 2nd Edition, Oxford University Press, NY, Oxford; Johne et al. (1993) J. Immunol. Meth.160: 191-198; Jonsson et al. (1993) Ann. Biol. Clin.51: 19- 26; and Jonsson et al. (1991) Biotechniques 11 :620-627. See also, U.S. Patent No.6,355,245. Immunoassays which can be used to analyze immunospecific binding and cross-reactivity of the antibodies include, but are not limited to, competitive and non- competitive assay systems using techniques such as Western blots, RIA, ELISA (enzyme linked immunosorbent assay), "sandwich" immunoassays, immunoprecipitation assays, immunodiffusion assays, agglutination assays, complement-fixation assays, immunoradiometric assays, fluorescent immunoassays, and protein A immunoassays. Such assays are routine and well known in the art. Antibodies can also be assayed using any surface plasmon resonance (SPR)- based assays known in the art for characterizing the kinetic parameters of the interaction of the antibody with its target or epitope. Any SPR instrument commercially available including, but not limited to, BIAcore Instruments (Biacore AB; Uppsala, Sweden); lAsys instruments (Affinity Sensors; Franklin, Massachusetts); IBIS system (Windsor Scientific Limited; Berks, UK), SPR-CELLIA systems (Nippon Laser and Electronics Lab; Hokkaido, Japan), and SPR Detector Spreeta (Texas Instruments; Dallas, Texas) can be used in the methods described herein. See, e.g., Mullett et al. (2000) Methods 22: 77-91; Dong et al. (2002) Reviews in Mol Biotech 82: 303-323; Fivash et al. (1998) Curr Opin Biotechnol 9: 97-101; and Rich et al. (2000) Curr Opin Biotechnol 11:54-61. The antibodies and fragments thereof can be, in some embodiments, "chimeric." Chimeric antibodies and antigen-binding fragments thereof comprise portions from two or more different species (e.g., mouse and human). Chimeric antibodies can be produced with mouse variable regions of desired specificity spliced onto human constant domain gene segments (see, for example, U.S. Patent No.4,816,567). In this manner, non-human antibodies can be modified to make them more suitable for human clinical application (e.g., methods for treating or preventing a complement associated disorder in a human subject). The monoclonal antibodies of the present disclosure include "humanized" forms of the non-human (e.g., mouse) antibodies. Humanized or CDR-grafted mAbs are particularly useful as therapeutic agents for humans because they are not cleared from the circulation as rapidly as mouse antibodies and do not typically provoke an adverse immune reaction. Methods of preparing humanized antibodies are generally well known in the art. For example, humanization can be essentially performed following the method of Winter and co-workers (see, e.g., Jones et al. (1986) Nature 321 :522-525; Riechmann et al. (1988) Nature 332:323-327; and Verhoeyen et al. (1988) Science 239: 1534-1536), by substituting rodent CDRs or CDR sequences for the corresponding sequences of a human antibody. Also see, e.g., Staelens et al. (2006) Mol Immunol 43:1243-1257. In some embodiments, humanized forms of non-human (e.g., mouse) antibodies are human antibodies (recipient antibody) in which hypervariable (CDR) region residues of the recipient antibody are replaced by hypervariable region residues from a non- human species (donor antibody) such as a mouse, rat, rabbit, or non-human primate having the desired specificity, affinity, and binding capacity. In some instances, framework region residues of the human immunoglobulin are also replaced by corresponding non-human residues (so called "back mutations"). In addition, phage display libraries can be used to vary amino acids at chosen positions within the antibody sequence. The properties of a humanized antibody are also affected by the choice of the human framework. Furthermore, humanized and chimerized antibodies can be modified to comprise residues that are not found in the recipient antibody or in the donor antibody in order to further improve antibody properties, such as, for example, affinity or effector function. Fully human antibodies are also provided in the disclosure. The term "human antibody" includes antibodies having variable and constant regions (if present) derived from human germline immunoglobulin sequences. Human antibodies can include amino acid residues not encoded by human germline immunoglobulin sequences (e.g., mutations introduced by random or site-specific mutagenesis in vitro or by somatic mutation in vivo). However, the term "human antibody" does not include antibodies in which CDR sequences derived from the germline of another mammalian species, such as a mouse, have been grafted onto human framework sequences (i.e., humanized antibodies). Fully human or human antibodies may be derived from transgenic mice carrying human antibody genes (carrying the variable (V), diversity (D), joining (J), and constant (C) exons) or from human cells. For example, it is now possible to produce transgenic animals (e.g., mice) that are capable, upon immunization, of producing a full repertoire of human antibodies in the absence of endogenous immunoglobulin production. (See, e.g., Jakobovits et al. (1993) Proc. Natl. Acad. Sci. USA 90:2551; Jakobovits et al. (1993) Nature 362:255-258; Bruggemann et al. (1993) Year in Immunol. 7:33; and Duchosal et al. (1992) Nature 355:258.) Transgenic mice strains can be engineered to contain gene sequences from unrearranged human immunoglobulin genes. The human sequences may code for both the heavy and light chains of human antibodies and would function correctly in the mice, undergoing rearrangement to provide a wide antibody repertoire similar to that in humans. The transgenic mice can be immunized with the target protein (to create a diverse array of specific antibodies and their encoding RNA. Nucleic acids encoding the antibody chain components of such antibodies may then be cloned from the animal into a display vector. Typically, separate populations of nucleic acids encoding heavy and light chain sequences are cloned, and the separate populations then recombined on insertion into the vector, such that any given copy of the vector receives a random combination of a heavy and a light chain. The vector is designed to express antibody chains so that they can be assembled and displayed on the outer surface of a display package containing the vector. For example, antibody chains can be expressed as fusion proteins with a phage coat protein from the outer surface of the phage. Thereafter, display packages can be screened for display of antibodies binding to a target. Thus, in some embodiments, the disclosure provides, e.g., humanized, deimmunized or primatized antibodies comprising one or more of the complementarity determining regions (CDRs) of the mouse monoclonal antibodies described herein, which retain the ability (e.g., at least 50, 60, 70, 80, 90, or 100%, or even greater than 100%) of the mouse monoclonal antibody counterpart to bind to its antigen. In addition, human antibodies can be derived from phage-display libraries (Hoogenboom et al. (1991) J. Mol. Biol.227:381; Marks et al. (1991) J. Mol. Biol, 222:581-597; and Vaughan et al. (1996) Nature Biotech 14:309 (1996)). Synthetic phage libraries can be created which use randomized combinations of synthetic human antibody V-regions. By selection on antigen fully human antibodies can be made in which the V- regions are very human-like in nature. See, e.g., U.S. Patent Nos.6,794,132, 6,680,209, 4,634,666, and Ostberg et al. (1983), Hybridoma 2:361- 367, the contents of each of which are incorporated herein by reference in their entirety. For the generation of human antibodies, also see Mendez et al. (1998) Nature Genetics 15: 146-156 and Green and Jakobovits (1998) J. Exp. Med.188:483- 495, the disclosures of which are hereby incorporated by reference in their entirety. Human antibodies are further discussed and delineated in U.S. Patent Nos.: 5,939,598; 6,673,986; 6,114,598; 6,075, 181; 6, 162,963; 6,150,584; 6,713,610; and 6,657, 103 as well as U.S. Patent Application Publication Nos.2003- 0229905 Al, 2004-0010810 Al, US 2004-0093622 Al, 2006-0040363 Al, 2005-0054055 Al, 2005-0076395 Al, and 2005- 0287630 Al . See also International Publication Nos. WO 94/02602, WO 96/34096, and WO 98/24893, and European Patent No. EP 0463151 B1. The disclosures of each of the above-cited patents, applications, and references are hereby incorporated by reference in their entirety. In an alternative approach, others, including GenPharm International, Inc., have utilized a "minilocus" approach. In the minilocus approach, an exogenous Ig locus is mimicked through the inclusion of pieces (individual genes) from the Ig locus. Thus, one or more VH genes, one or more DH genes, one or more JH genes, a mu constant region, and a second constant region (preferably a gamma constant region) are formed into a construct for insertion into an animal. This approach is described in, e.g., U.S. Patent Nos.: 5,545,807; 5,545,806; 5,625,825; 5,625, 126; 5,633,425; 5,661,016; 5,770,429; 5,789,650; and 5,814,318; 5,591,669; 5,612,205; 5,721,367; 5,789,215; 5,643,763; 5,569,825; 5,877,397; 6,300,129; 5,874,299; 6,255,458; and 7,041,871, the disclosures of which are hereby incorporated by reference. See also European Patent No. 0546073 Bl, International Patent Publication Nos. WO 92/03918, WO 92/22645, WO 92/22647, WO 92/22670, WO 93/12227, WO 94/00569, WO 94/25585, WO 96/14436, WO 97/13852, and WO 98/24884, the disclosures of each of which are hereby incorporated by reference in their entirety. See further Taylor et al. (1992) Nucleic Acids Res.20: 6287; Chen et al. (1993) Int. Immunol.5: 647; Tuaillon et al. (1993) Proc. Natl. Acad. Sci. USA 90: 3720-4; Choi et al. (1993) Nature Genetics 4: 117; Lonberg et al. (1994) Nature 368: 856-859; Taylor et al. (1994) International Immunology 6: 579-591 ; Tuaillon et al. (1995) J. Immunol.154: 6453- 65; Fishwild et al. (1996) Nature Biotechnology 14: 845; and Tuaillon et al. (2000) Eur. J. Immunol.10: 2998-3005, the disclosures of each of which are hereby incorporated by reference in their entirety. In some embodiments, de-immunized antibodies or antigen-binding fragments thereof are provided. De-immunized antibodies or antigen-binding fragments thereof are antibodies that have been modified so as to render the antibody or antigen- binding fragment thereof non- immunogenic, or less immunogenic, to a given species (e.g., to a human). De-immunization can be achieved by modifying the fusion proteins, antibodies or fragments thereof utilizing any of a variety of techniques known to those skilled in the art (see, e.g., PCT Publication Nos. WO 04/108158 and WO 00/34317). For example, fusion proteins, antibodies or fragments thereof may be de-immunized by identifying potential T cell epitopes and/or B cell epitopes within the amino acid sequence of the fusion proteins, antibodies or fragments thereof and removing one or more of the potential T cell epitopes and/or B cell epitopes from the fusion proteins, antibodies or fragments thereof, for example, using recombinant techniques. The modified antibody or antigen- binding fragment thereof may then optionally be produced and tested to identify antibodies or antigen-binding fragments thereof that have retained one or more desired biological activities, such as, for example, binding affinity, but have reduced immunogenicity. Methods for identifying potential T cell epitopes and/or B cell epitopes may be carried out using techniques known in the art, such as, for example, computational methods (see e.g., PCT Publication No. WO 02/069232), in vitro or in silico techniques, and biological assays or physical methods (such as, for example, determination of the binding of peptides to MHC molecules, determination of the binding of peptide:MHC complexes to the T cell receptors from the species to receive the fusion proteins, antibodies or fragments thereof , testing of the protein or peptide parts thereof using transgenic animals with the MHC molecules of the species to receive the antibody or antigen- binding fragment thereof, or testing with transgenic animals reconstituted with immune system cells from the species to receive the fusion proteins, antibodies or fragments thereof , etc.). In various embodiments, the de- immunized antibodies described herein include de-immunized antigen-binding fragments, Fab, Fv, scFv, Fab' and F(ab') ₂ , monoclonal antibodies, murine antibodies, engineered antibodies (such as, for example, chimeric, single chain, CDR-grafted, humanized, fully human antibodies, and artificially selected antibodies), synthetic antibodies and semi-synthetic antibodies. In some embodiments, the present disclosure also provides bispecific antibodies. Bispecific antibodies are monoclonal, preferably human or humanized, antibodies that have binding specificities for at least two different antigens. For example, in one embodiment, a NKCE of the invention comprises one domain with a binding specificity for a Siglec protein or polypeptide, and one domain with a binding specificity for an alternative protein or polypeptide. In one embodiment, a NKCE of the invention comprises one domain with a binding specificity for a Siglec protein or polypeptide, and one domain with a binding specificity for an alternative Siglec protein or polypeptide. Methods for making NKCEs are within the purview of those skilled in the art. Traditionally, the recombinant production of bispecific antibodies is based on the co- expression of two immunoglobulin heavy -chain/light-chain pairs, where the two heavy chain/light-chain pairs have different specificities (Milstein and Cuello (1983) Nature 305:537- 539). Antibody variable domains with the desired binding specificities (antibody-antigen combining sites) can be fused to immunoglobulin constant domain sequences. The fusion of the heavy chain variable region is preferably with an immunoglobulin heavy-chain constant domain, including at least part of the hinge, CH2, and CH3 regions. DNAs encoding the immunoglobulin heavy -chain fusions and, if desired, the immunoglobulin light chain, are inserted into separate expression vectors, and are co-transfected into a suitable host organism. For further details of illustrative currently known methods for generating bispecific antibodies see, e.g., Suresh et al. (1986) Methods in Enzymology 121 :210; PCT Publication No. WO 96/27011 ; Brennan et al. (1985) Science 229:81 ; Shalaby et al, J Exp Med (1992) 175:217-225; Kostelny et al. (1992) J Immunol 148(5): 1547-1553; Hollinger et al. (1993) Proc Natl Acad Sci USA 90:6444-6448; Gruber et al. (1994) J Immunol 152:5368; and Tutt et al. (1991) J Immunol 147:60. Bispecific antibodies also include cross-linked or hetero-conjugate antibodies. Hetero-conjugate antibodies may be made using any convenient cross-linking methods. Suitable cross-linking agents are well known in the art, and are disclosed in U.S. Patent No.4,676,980, along with a number of cross- linking techniques. Various techniques for making and isolating bispecific antibody fragments directly from recombinant cell culture have also been described. For example, bispecific antibodies have been produced using leucine zippers. See, e.g., Kostelny et al. (1992) J Immunol 148(5): 1547-1553. The leucine zipper peptides from the Fos and Jun proteins may be linked to the Fab' portions of two different antibodies by gene fusion. The antibody homodimers may be reduced at the hinge region to form monomers and then re- oxidized to form the antibody heterodimers. This method can also be utilized for the production of antibody homodimers. The "diabody" technology described by Hollinger et al. (1993) Proc Natl Acad Sci USA 90:6444-6448 has provided an alternative mechanism for making bispecific antibody fragments. The fragments comprise a heavy- chain variable domain (VH) connected to a light-chain variable domain (VL) by a linker which is too short to allow pairing between the two domains on the same chain. Accordingly, the VH and VL domains of one fragment are forced to pair with the complementary VL and VH domains of another fragment, thereby forming two antigen- binding sites. Another strategy for making bispecific antibody fragments by the use of single-chain Fv (scFv) dimers has also been reported. See, e.g., Gruber et al. (1994) J Immunol 152:5368. Alternatively, the antibodies can be "linear antibodies" as described in, e.g., Zapata et al. (1995) Protein Eng.8(10): 1057-1062. Briefly, these antibodies comprise a pair of tandem Fd segments (VH-CH1-VH-CH1) which form a pair of antigen binding regions. Linear antibodies can be bispecific or monospecific. Antibodies with more than two valencies (e.g., trispecific antibodies) are also contemplated and described in, e.g., Tutt et al. (1991) J Immunol 147:60. The disclosure also embraces variant forms of multi-specific antibodies such as the dual variable domain immunoglobulin (DVD-lg) molecules described in Wu et al. (2007) Nat Biotechnol 25(11): 1290-1297. The DVD-lg molecules are designed such that two different light chain variable domains (VL) from two different parent antibodies are linked in tandem directly or via a short linker by recombinant DNA techniques, followed by the light chain constant domain. Similarly, the heavy chain comprises two different heavy chain variable domains (VH) linked in tandem, followed by the constant domain CH1 and Fc region. Methods for making DVD-Ig molecules from two parent antibodies are further described in, e.g., PCT Publication Nos. WO 08/024188 and WO 07/024715. The disclosure also provides camelid or dromedary antibodies (e.g., antibodies derived from Camelus bactrianus, Calelus dromaderius, or lama paccos). Such antibodies, unlike the typical two-chain (fragment) or four-chain (whole antibody) antibodies from most mammals, generally lack light chains. See U.S. patent no. 5,759,808; Stijlemans et al. (2004) J Biol Chem 279: 1256-1261; Dumoulin et al. (2003) Nature 424:783-788; and Pleschberger et al. (2003) Bioconjugate Chem 14:440-448. Engineered libraries of camelid antibodies and antibody fragments are commercially available, for example, from Ablynx (Ghent, Belgium). As with other antibodies of non-human origin, an amino acid sequence of a camelid antibody can be altered recombinantly to obtain a sequence that more closely resembles a human sequence, i.e., the nanobody can be "humanized" to thereby further reduce the potential immunogenicity of the antibody. In some embodiments, the present disclosure also provides antibodies, or antigen-binding fragments thereof, which are variants of a peptide, protein or antibody described herein. In some embodiments, such a variant peptide, protein or antibody maintains the binding or inhibitory ability of the parent peptide, protein or antibody. Methods to prepare variants of known proteins, peptides or antibodies are known in the art. In some embodiments, such a variant comprises at least a single amino acid substitution, deletion, insertion, or other modification. In some embodiments, fusion proteins, antibodies or fragments thereof described herein comprises two or more (e.g.2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more) amino acid modifications (e.g., amino acid substitutions, deletions, or additions). In some embodiments, fusion proteins, antibodies or fragments thereof described herein does not contain an amino acid modification in a CDR. In some embodiments, fusion proteins, antibodies or fragments thereof described herein does contain one or more (e.g.1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20) amino acid modifications in a CDR. As used herein, the term "antibody fragment", "antigen-binding fragment", "antigen binding fragment", or similar terms refer to fragment of an antibody that retains the ability to bind to an antigen wherein the antigen binding fragment may optionally include additional compositions not part of the original antibody (e.g. different framework regions or mutations) as well as the fragment(s) from the original antibody. Examples include, but are not limited to, a single chain antibody, a single chain Fv fragment (scFv), an Fd fragment, an Fab fragment, an Fab' fragment, or an F(ab') ₂ fragment. An scFv fragment is a single polypeptide chain that includes both the heavy and light chain variable regions of the antibody from which the scFv is derived. In addition, diabodies (Poljak (1994) Structure 2(12): 1121-1123; Hudson et al. (1999) J. Immunol. Methods 23(1-2): 177-189, the disclosures of each of which are incorporated herein by reference in their entirety), minibodies, triabodies (Schoonooghe et al. (2009) BMC Biotechnol 9:70), and domain antibodies (also known as "heavy chain immunoglobulins" or camelids; Holt et al. (2003) Trends Biotechnol 21(11):484-490), (the disclosures of each of which are incorporated herein by reference in their entirety) that bind to a complement component protein can be incorporated into the compositions, and used in the methods, described herein. In some embodiments, any of the antigen binding fragments described herein may be included under "antigen binding fragment thereof or equivalent terms, when referring to fragments related to an antibody, whether such fragments were actually derived from the antibody or are antigen binding fragments that bind the same epitope or an overlapping epitope or an epitope contained in the antibody's epitope. An antigen binding fragment thereof may include antigen-binding fragments that bind the same, or overlapping, antigen as the original antibody and wherein the antigen binding fragment includes a portion (e.g. one or more CDRs, one or more variable regions, etc.) that is a fragment of the original antibody. In some embodiments, the antibodies described herein comprise an altered or mutated sequence that leads to altered stability or half-life compared to parent antibodies. This includes, for example, an increased stability or half- life for higher affinity or longer clearance time in vitro or in vivo, or a decreased stability or half-life for lower affinity or quicker removal. Additionally, the antibodies described herein may contain one or more (e.g.1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20) amino acid substitutions, deletions, or insertions that result in altered post- translational modifications, including, for example, an altered glycosylation pattern (e.g., the addition of one or more sugar components, the loss of one or more sugar components, or a change in composition of one or more sugar components. In some embodiments, the antibodies described herein comprise reduced (e.g. or no) effector function. Altered effector functions include, for example, a modulation in one or more of the following activities: antibody-dependent cellular cytotoxicity (ADCC), complement-dependent cytotoxicity (CDC), apoptosis, binding to one or more Fc- receptors, and pro-inflammatory responses. Modulation refers to an increase, decrease, or elimination of an effector function activity exhibited by a subject antibody containing an altered constant region as compared to the activity of the unaltered form of the constant region. In particular embodiments, modulation includes situations in which an activity is abolished or completely absent. Antibodies with altered or no effector functions may be generated by engineering or producing antibodies with variant constant, Fc, or heavy chain regions; recombinant DNA technology and/or cell culture and expression conditions may be used to produce antibodies with altered function and/or activity. For example, recombinant DNA technology may be used to engineer one or more amino acid substitutions, deletions, or insertions in regions (such as, for example, Fc or constant regions) that affect antibody function including effector functions. Alternatively, changes in post- translational modifications, such as, e.g., glycosylation patterns, may be achieved by manipulating the cell culture and expression conditions by which the antibody is produced. Suitable methods for introducing one or more substitutions, additions, or deletions into an Fc region of an antibody are well known in the art and include, e.g., standard DNA mutagenesis techniques as described in, e.g., Sambrook et al. (1989) "Molecular Cloning: A Laboratory Manual, 2nd Edition," Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.; Harlow and Lane (1988), supra; Borrebaek (1992), supra; Johne et al. (1993), supra; PCT publication no. WO 06/53301 ; and U.S. patent no. 7,704,497. Nucleic Acid Molecules Provided herein are polynucleotides that encode the NKCE antibodies, or fragments thereof, of the invention. In some embodiments, the polynucleotide also comprises a sequence encoding a signal peptide operably linked at the 5' end of the encoding sequence. In some embodiments, the polynucleotide also comprises a sequence encoding a linker sequence. In one embodiment, the nucleic acid molecule comprises a nucleotide sequence that encodes a NKCE comprising a Siglec-7 binding arm comprising at least one of SEQ ID NO: 4, SEQ ID NO: 12, SEQ ID NO: 20, SEQ ID NO: 28, SEQ ID NO: 36, SEQ ID NO: 44, SEQ ID NO: 52, SEQ ID NO: 60, SEQ ID NO: 68, SEQ ID NO: 76, SEQ ID NO: 84, or SEQ ID NO: 92. In one embodiment, the nucleic acid molecule comprises a nucleotide sequence that encodes a NKCE of SEQ ID NO:98, SEQ ID NO:100, or SEQ ID NO:102. In one embodiment, the nucleic acid molecule comprises a nucleotide sequence of SEQ ID NO: 8, SEQ ID NO: 16, SEQ ID NO: 24, SEQ ID NO: 32, SEQ ID NO: 40, SEQ ID NO: 48, SEQ ID NO: 56, SEQ ID NO: 64, SEQ ID NO: 72, SEQ ID NO: 80, SEQ ID NO: 88, or SEQ ID NO: 96 that encodes a NKCE comprising a Siglec-7 binding arm. In one embodiment, the nucleic acid molecule comprises a nucleotide sequence of SEQ ID NO:97, SEQ ID NO:99, or SEQ ID NO:101, that encodes a bispecific NKCE. In one embodiment, the nucleic acid molecule comprises an RNA molecule corresponding to a nucleotide sequence of at least one of SEQ ID NO: 8, SEQ ID NO: 16, SEQ ID NO: 24, SEQ ID NO: 32, SEQ ID NO: 40, SEQ ID NO: 48, SEQ ID NO: 56, SEQ ID NO: 64, SEQ ID NO: 72, SEQ ID NO: 80, SEQ ID NO: 88, SEQ ID NO: 96, SEQ ID NO:97, SEQ ID NO:99, or SEQ ID NO:101. In one embodiment, the nucleic acid molecule comprises a DNA molecule corresponding to a nucleotide sequence of at least one of SEQ ID NO: 8, SEQ ID NO: 16, SEQ ID NO: 24, SEQ ID NO: 32, SEQ ID NO: 40, SEQ ID NO: 48, SEQ ID NO: 56, SEQ ID NO: 64, SEQ ID NO: 72, SEQ ID NO: 80, SEQ ID NO: 88, SEQ ID NO: 96, SEQ ID NO:97, SEQ ID NO:99, or SEQ ID NO:101. In some embodiments, a variant of a nucleotide sequence as described herein comprises at least about 60% identity, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93% ,94%, 95%, 96%, 97%, 98%, 99% or higher identity over a specified region when compared to a defined nucleotide sequence. In some embodiments, a variant of a nucleotide sequence as described herein comprises at least about 60% identity, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93% ,94%, 95%, 96%, 97%, 98%, 99% or higher identity over the full length of a nucleotide sequence of at least one of SEQ ID NO: 8, SEQ ID NO: 16, SEQ ID NO: 24, SEQ ID NO: 32, SEQ ID NO: 40, SEQ ID NO: 48, SEQ ID NO: 56, SEQ ID NO: 64, SEQ ID NO: 72, SEQ ID NO: 80, SEQ ID NO: 88, SEQ ID NO: 96, SEQ ID NO:97, SEQ ID NO:99, or SEQ ID NO:101. In some embodiments, a fragment of a nucleotide sequence as described herein comprises at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93% ,94%, 95%, 96%, 97%, 98%, or 99% of the full length sequence of a defined nucleotide sequence. In some embodiments, a fragment of a nucleotide sequence as described herein comprises at least about 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93% ,94%, 95%, 96%, 97%, 98%, or 99% of the full length sequence of SEQ ID NO: 8, SEQ ID NO: 16, SEQ ID NO: 24, SEQ ID NO: 32, SEQ ID NO: 40, SEQ ID NO: 48, SEQ ID NO: 56, SEQ ID NO: 64, SEQ ID NO: 72, SEQ ID NO: 80, SEQ ID NO: 88, SEQ ID NO: 96, SEQ ID NO:97, SEQ ID NO:99, or SEQ ID NO:101. The isolated nucleic acid may comprise any type of nucleic acid, including, but not limited to DNA, cDNA, and RNA. In one embodiment, the composition comprises an isolated RNA molecule encoding a NKCE or a functional fragment thereof. The nucleic acid molecules of the present invention can be modified to improve stability. Modifications can be added to enhance stability, functionality, and/or specificity and to minimize immunostimulatory properties of the nucleic acid molecule of the invention. For example, in order to enhance the stability, the 3’-residues may be stabilized against degradation, e.g., they may be selected such that they consist of purine nucleotides, particularly adenosine or guanosine nucleotides. Alternatively, substitution of pyrimidine nucleotides by modified analogues, e.g., substitution of uridine by 2’- deoxythymidine is tolerated and does not affect function of the molecule. In one embodiment of the present invention the nucleic acid molecule may contain at least one modified nucleotide analogue. For example, the ends may be stabilized by incorporating modified nucleotide analogues. Non-limiting examples of nucleotide analogues include sugar- and/or backbone-modified ribonucleotides (i.e., include modifications to the phosphate-sugar backbone). For example, the phosphodiester linkages of natural RNA may be modified to include at least one of a nitrogen or sulfur heteroatom. In exemplary backbone-modified ribonucleotides the phosphoester group connecting to adjacent ribonucleotides is replaced by a modified group, e.g., of phosphothioate group. Other examples of modifications are nucleobase-modified ribonucleotides, i.e., ribonucleotides, containing at least one non-naturally occurring nucleobase instead of a naturally occurring nucleobase. Bases may be modified to block the activity of adenosine deaminase. Exemplary modified nucleobases include, but are not limited to, uridine and/or cytidine modified at the 5-position, e.g., 5-(2-amino)propyl uridine, 5- bromo uridine; adenosine and/or guanosines modified at the 8 position, e.g., 8-bromo guanosine; deaza nucleotides, e.g., 7-deaza-adenosine; O- and N-alkylated nucleotides, e.g., N6-methyl adenosine are suitable. The above modifications may be combined. In some instances, the nucleic acid molecule comprises at least one of the following chemical modifications: 2’-H, 2’-O-methyl, or 2’-OH modification of one or more nucleotides. In some embodiments, a nucleic acid molecule of the invention can have enhanced resistance to nucleases. For increased nuclease resistance, a nucleic acid molecule, can include, for example, 2’-modified ribose units and/or phosphorothioate linkages. For example, the 2’ hydroxyl group (OH) can be modified or replaced with a number of different “oxy” or “deoxy” substituents. For increased nuclease resistance the nucleic acid molecules of the invention can include 2’-O-methyl, 2’-fluorine, 2’-O- methoxyethyl, 2’-O-aminopropyl, 2’-amino, and/or phosphorothioate linkages. Inclusion of locked nucleic acids (LNA), ethylene nucleic acids (ENA), e.g., 2’-4’-ethylene- bridged nucleic acids, and certain nucleobase modifications such as 2-amino-A, 2-thio (e.g., 2-thio-U), G-clamp modifications, can also increase binding affinity to a target. In one embodiment, the nucleic acid molecule includes a 2’-modified nucleotide, e.g., a 2’-deoxy, 2’-deoxy-2’-fluoro, 2’-O-methyl, 2’-O-methoxyethyl (2’-O- MOE), 2’-O-aminopropyl (2’-O-AP), 2’-O-dimethylaminoethyl (2’-O-DMAOE), 2’-O- dimethylaminopropyl (2’-O-DMAP), 2’-O-dimethylaminoethyloxyethyl (2’-O- DMAEOE), or 2’-O-N-methylacetamido (2’-O-NMA). In one embodiment, the nucleic acid molecule includes at least one 2’-O-methyl-modified nucleotide, and in some embodiments, all of the nucleotides of the nucleic acid molecule include a 2’-O-methyl modification. Nucleic acid agents discussed herein include otherwise unmodified RNA and DNA as well as RNA and DNA that have been modified, e.g., to improve efficacy, and polymers of nucleoside surrogates. Unmodified RNA refers to a molecule in which the components of the nucleic acid, namely sugars, bases, and phosphate moieties, are the same or essentially the same as that which occur in nature, for example as occur naturally in the human body. The art has referred to rare or unusual, but naturally occurring, RNAs as modified RNAs, see, e.g., Limbach et al. (Nucleic Acids Res., 1994, 22:2183-2196). Such rare or unusual RNAs, often termed modified RNAs, are typically the result of a post-transcriptional modification and are within the term unmodified RNA as used herein. Modified RNA, as used herein, refers to a molecule in which one or more of the components of the nucleic acid, namely sugars, bases, and phosphate moieties, are different from that which occur in nature, for example different from that which occurs in the human body. While they are referred to as “modified RNAs” they will of course, because of the modification, include molecules that are not, strictly speaking, RNAs. Nucleoside surrogates are molecules in which the ribophosphate backbone is replaced with a non-ribophosphate construct that allows the bases to be presented in the correct spatial relationship such that hybridization is substantially similar to what is seen with a ribophosphate backbone, e.g., non-charged mimics of the ribophosphate backbone. Modifications of the nucleic acid of the invention may be present at one or more of, a phosphate group, a sugar group, backbone, N-terminus, C-terminus, or nucleobase. The present invention also includes a vector in which the isolated nucleic acid of the present invention is inserted. The art is replete with suitable vectors that are useful in the present invention. Therefore, in another aspect, the invention relates to a vector, comprising the nucleotide sequence of the invention or the construct of the invention. The choice of the vector will depend on the host cell in which it is to be subsequently introduced. In some embodiments, the vector of the invention is an expression vector. Suitable host cells include a wide variety of prokaryotic and eukaryotic host cells. In specific embodiments, the expression vector is selected from the group consisting of a viral vector, a bacterial vector and a mammalian cell vector. Prokaryote- and/or eukaryote-vector based systems can be employed for use with the present invention to produce polynucleotides, or their cognate polypeptides. Many such systems are commercially and widely available. In some embodiments, the expression of synthetic nucleic acids encoding a protein is typically achieved by operably linking a nucleic acid encoding the protein or portions thereof to a promoter and incorporating the construct into an expression vector. The vectors to be used are suitable for replication and, optionally, integration in eukaryotic cells. Typical vectors contain transcription and translation terminators, initiation sequences, and promoters useful for regulation of the expression of the desired nucleic acid sequence. The recombinant nucleic acid sequence construct can include one or more transcription termination regions. The transcription termination region can be downstream of the coding sequence to provide for efficient termination. The transcription termination region can be obtained from the same gene as the promoter described above or can be obtained from one or more different genes. The recombinant nucleic acid sequence construct can include one or more initiation codons. The initiation codon can be located upstream of the coding sequence. The initiation codon can be in frame with the coding sequence. The initiation codon can be associated with one or more signals required for efficient translation initiation, for example, but not limited to, a ribosome binding site. The recombinant nucleic acid sequence construct can include one or more termination or stop codons. The termination codon can be downstream of the coding sequence. The termination codon can be in frame with the coding sequence. The termination codon can be associated with one or more signals required for efficient translation termination. The recombinant nucleic acid sequence construct can include one or more polyadenylation signals. The polyadenylation signal can include one or more signals required for efficient polyadenylation of the transcript. The polyadenylation signal can be positioned downstream of the coding sequence. The polyadenylation signal may be a SV40 polyadenylation signal, LTR polyadenylation signal, bovine growth hormone (bGH) polyadenylation signal, human growth hormone (hGH) polyadenylation signal, or human β-globin polyadenylation signal. The SV40 polyadenylation signal may be a polyadenylation signal from a pCEP4 plasmid (Invitrogen, San Diego, CA). The recombinant nucleic acid sequence construct can include one or more leader sequences. The leader sequence can encode a signal peptide. The signal peptide can be an immunoglobulin (Ig) signal peptide, for example, but not limited to, an IgG signal peptide and an IgE signal peptide. The vectors of the present invention may also be used for nucleic acid immunization, using standard gene delivery protocols. Methods for gene delivery are known in the art. See, e.g., U.S. Pat. Nos.5,399,346, 5,580,859, 5,589,466, incorporated by reference herein in their entireties. The isolated nucleic acid of the invention can be cloned into a number of types of vectors. For example, the nucleic acid can be cloned into a vector including, but not limited to a plasmid, a phagemid, a phage derivative, an animal virus, and a cosmid. Vectors of particular interest include expression vectors, replication vectors, probe generation vectors, and sequencing vectors. Further, the vector may be provided to a cell in the form of a viral vector. Viral vector technology is well known in the art and is described, for example, in Sambrook et al. (2012, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory, New York), and in other virology and molecular biology manuals. Viruses, which are useful as vectors include, but are not limited to, retroviruses, adenoviruses, adeno-associated viruses, herpes viruses, and lentiviruses. In general, a suitable vector contains an origin of replication functional in at least one organism, a promoter sequence, convenient restriction endonuclease sites, and one or more selectable markers, (e.g., WO 01/96584; WO 01/29058; and U.S. Pat. No.6,326,193). Further, the expression vector may be provided to a cell in the form of a viral vector. Viral vector technology is well known in the art and is described, for example, in Sambrook et al. (2012), and in Ausubel et al. (1997), and in other virology and molecular biology manuals. Viruses, which are useful as vectors include, but are not limited to, retroviruses, adenoviruses, adeno-associated viruses, herpes viruses, and lentiviruses. In general, a suitable vector contains an origin of replication functional in at least one organism, a promoter sequence, convenient restriction endonuclease sites, and one or more selectable markers. (See, e.g., WO 01/96584; WO 01/29058; and U.S. Pat. No.6,326,193. By way of illustration, the vector in which the nucleic acid sequence is introduced can be a plasmid, which is or is not integrated in the genome of a host cell when it is introduced in the cell. Illustrative, non-limiting examples of vectors in which the nucleotide sequence of the invention or the gene construct of the invention can be inserted include a tet-on inducible vector for expression in eukaryote cells. The vector may be obtained by conventional methods known by persons skilled in the art (Sambrook et al., 2012). In a particular embodiment, the vector is a vector useful for transforming animal cells. In one embodiment, the recombinant expression vectors may also contain nucleic acid molecules, which encode a peptide or protein of invention, described elsewhere herein. A number of viral based systems have been developed for gene transfer into mammalian cells. For example, retroviruses provide a convenient platform for gene delivery systems. A selected gene can be inserted into a vector and packaged in retroviral particles using techniques known in the art. The recombinant virus can then be isolated and delivered to cells of the subject either in vivo or ex vivo. A number of retroviral systems are known in the art. In some embodiments, adenovirus vectors are used. A number of adenovirus vectors are known in the art. In one embodiment, lentivirus vectors are used. For example, vectors derived from retroviruses such as the lentivirus are suitable tools to achieve long-term gene transfer since they allow long-term, stable integration of a transgene and its propagation in daughter cells. Lentiviral vectors have the added advantage over vectors derived from onco-retroviruses such as murine leukemia viruses in that they can transduce non-proliferating cells, such as hepatocytes. They also have the added advantage of low immunogenicity. In one embodiment, the composition includes a vector derived from an adeno-associated virus (AAV). Adeno- associated viral (AAV) vectors have become powerful gene delivery tools for the treatment of various disorders. AAV vectors possess a number of features that render them ideally suited for gene therapy, including a lack of pathogenicity, minimal immunogenicity, and the ability to transduce postmitotic cells in a stable and efficient manner. Expression of a particular gene contained within an AAV vector can be specifically targeted to one or more types of cells by choosing the appropriate combination of AAV serotype, promoter, and delivery method. In some embodiments, the vector also includes conventional control elements which are operably linked to the transgene in a manner which permits its transcription, translation and/or expression in a cell transfected with the plasmid vector or infected with the virus produced by the invention. As used herein, “operably linked” sequences include both expression control sequences that are contiguous with the gene of interest and expression control sequences that act in trans or at a distance to control the gene of interest. Expression control sequences include appropriate transcription initiation, termination, promoter and enhancer sequences; efficient RNA processing signals such as splicing and polyadenylation (polyA) signals; sequences that stabilize cytoplasmic mRNA; sequences that enhance translation efficiency (i.e., Kozak consensus sequence); sequences that enhance protein stability; and when desired, sequences that enhance secretion of the encoded product. A great number of expression control sequences, including promoters which are native, constitutive, inducible and/or tissue-specific, are known in the art and may be utilized. A promoter may be one naturally associated with a gene or polynucleotide sequence, as may be obtained by isolating the 5 ^ non-coding sequences located upstream of the coding segment and/or exon. Such a promoter can be referred to as “endogenous.” Similarly, an enhancer may be one naturally associated with a polynucleotide sequence, located either downstream or upstream of that sequence. Alternatively, certain advantages will be gained by positioning the coding polynucleotide segment under the control of a recombinant or heterologous promoter, which refers to a promoter that is not normally associated with a polynucleotide sequence in its natural environment. A recombinant or heterologous enhancer refers also to an enhancer not normally associated with a polynucleotide sequence in its natural environment. Such promoters or enhancers may include promoters or enhancers of other genes, and promoters or enhancers isolated from any other prokaryotic, viral, or eukaryotic cell, and promoters or enhancers not “naturally occurring,” i.e., containing different elements of different transcriptional regulatory regions, and/or mutations that alter expression. In addition to producing nucleic acid sequences of promoters and enhancers synthetically, sequences may be produced using recombinant cloning and/or nucleic acid amplification technology, including PCR, in connection with the compositions disclosed herein (U.S. Patent 4,683,202, U.S. Patent 5,928,906). Furthermore, it is contemplated the control sequences that direct transcription and/or expression of sequences within non-nuclear organelles such as mitochondria, chloroplasts, and the like, can be employed as well. Naturally, it will be important to employ a promoter and/or enhancer that effectively directs the expression of the DNA segment in the cell type, organelle, and organism chosen for expression. Those of skill in the art of molecular biology generally know how to use promoters, enhancers, and cell type combinations for protein expression, for example, see Sambrook et al. (2012). The promoters employed may be constitutive, tissue-specific, inducible, and/or useful under the appropriate conditions to direct high-level expression of the introduced DNA segment, such as is advantageous in the large-scale production of recombinant proteins and/or peptides. The promoter may be heterologous or endogenous. The recombinant expression vectors may also contain a selectable marker gene, which facilitates the selection of transformed or transfected host cells. Suitable selectable marker genes are genes encoding proteins such as G418 and hygromycin, which confer resistance to certain drugs, β-galactosidase, chloramphenicol acetyltransferase, firefly luciferase, or an immunoglobulin or portion thereof such as the Fc portion of an immunoglobulin, such as IgG. The selectable markers may be introduced on a separate vector from the nucleic acid of interest. Additional promoter elements, e.g., enhancers, regulate the frequency of transcriptional initiation. Typically, these are located in the region 30-110 bp upstream of the start site, although a number of promoters have recently been shown to contain functional elements downstream of the start site as well. The spacing between promoter elements frequently is flexible, so that promoter function is preserved when elements are inverted or moved relative to one another. In the thymidine kinase (tk) promoter, the spacing between promoter elements can be increased to 50 bp apart before activity begins to decline. Depending on the promoter, it appears that individual elements can function either cooperatively or independently to activate transcription. One example of a suitable promoter is the immediate early cytomegalovirus (CMV) promoter sequence. This promoter sequence is a strong constitutive promoter sequence capable of driving high levels of expression of any polynucleotide sequence operatively linked thereto. Another example of a suitable promoter is Elongation Growth Factor -1α (EF-1α). However, other constitutive promoter sequences may also be used, including, but not limited to the simian virus 40 (SV40) early promoter, mouse mammary tumor virus (MMTV), human immunodeficiency virus (HIV) long terminal repeat (LTR) promoter, MoMuLV promoter, an avian leukemia virus promoter, an Epstein-Barr virus immediate early promoter, a Rous sarcoma virus promoter, as well as human gene promoters such as, but not limited to, the actin promoter, the myosin promoter, the hemoglobin promoter, and the creatine kinase promoter. Further, the invention should not be limited to the use of constitutive promoters. Inducible promoters are also contemplated as part of the invention. The use of an inducible promoter provides a molecular switch capable of turning on expression of the polynucleotide sequence which it is operatively linked when such expression is desired or turning off the expression when expression is not desired. Examples of inducible promoters include, but are not limited to a metallothionine promoter, a glucocorticoid promoter, a progesterone promoter, and a tetracycline promoter. Enhancer sequences found on a vector also regulates expression of the gene contained therein. Typically, enhancers are bound with protein factors to enhance the transcription of a gene. Enhancers may be located upstream or downstream of the gene it regulates. Enhancers may also be tissue-specific to enhance transcription in a specific cell or tissue type. In one embodiment, the vector of the present invention comprises one or more enhancers to boost transcription of the gene present within the vector. In order to assess the expression of a protein inhibitor, the expression vector to be introduced into a cell can also contain either a selectable marker gene or a reporter gene or both to facilitate identification and selection of expressing cells from the population of cells sought to be transfected or infected through viral vectors. In other aspects, the selectable marker may be carried on a separate piece of DNA and used in a co-transfection procedure. Both selectable markers and reporter genes may be flanked with appropriate regulatory sequences to enable expression in the host cells. Useful selectable markers include, for example, antibiotic-resistance genes, such as neo and the like. Reporter genes are used for identifying potentially transfected cells and for evaluating the functionality of regulatory sequences. In general, a reporter gene is a gene that is not present in or expressed by the recipient organism or tissue and that encodes a polypeptide whose expression is manifested by some easily detectable property, e.g., enzymatic activity. Expression of the reporter gene is assayed at a suitable time after the DNA has been introduced into the recipient cells. Suitable reporter genes may include genes encoding luciferase, beta-galactosidase, chloramphenicol acetyl transferase, secreted alkaline phosphatase, or the green fluorescent protein gene (e.g., Ui-Tei et al., 2000 FEBS Letters 479: 79-82). Suitable expression systems are well known and may be prepared using known techniques or obtained commercially. In general, the construct with the minimal 5' flanking region showing the highest level of expression of reporter gene is identified as the promoter. Such promoter regions may be linked to a reporter gene and used to evaluate agents for the ability to modulate promoter-driven transcription. Methods of introducing and expressing genes into a cell are known in the art. In the context of an expression vector, the vector can be readily introduced into a host cell, e.g., mammalian, bacterial, yeast, or insect cell by any method in the art. For example, the expression vector can be transferred into a host cell by physical, chemical, or biological means. Physical methods for introducing a peptide or protein into a host cell include calcium phosphate precipitation, lipofection, particle bombardment, microinjection, and the like. Methods for producing cells comprising vectors and/or exogenous nucleic acids are well-known in the art. See, for example, Sambrook et al. (2012, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory, New York). Biological methods for introducing a peptide or protein of interest into a host cell include the use of DNA and RNA vectors. Viral vectors, and especially retroviral vectors, have become the most widely used method for inserting genes into mammalian, e.g., human cells. Other viral vectors can be derived from lentivirus, poxviruses, herpes simplex virus I, adenoviruses and adeno-associated viruses, and the like. See, for example, U.S. Pat. Nos.5,350,674 and 5,585,362. Chemical means for introducing a peptide or protein into a host cell include colloidal dispersion systems, such as macromolecule complexes, nanocapsules, microspheres, beads, and lipid-based systems including oil-in-water emulsions, micelles, mixed micelles, and liposomes. An exemplary colloidal system for use as a delivery vehicle in vitro and in vivo is a liposome (e.g., an artificial membrane vesicle). In the case where a non-viral delivery system is utilized, an exemplary delivery vehicle is a liposome. The use of lipid formulations is contemplated for the introduction of the nucleic acids into a host cell (in vitro, ex vivo or in vivo). In another aspect, the nucleic acid may be associated with a lipid. The nucleic acid associated with a lipid may be encapsulated in the aqueous interior of a liposome, interspersed within the lipid bilayer of a liposome, attached to a liposome via a linking molecule that is associated with both the liposome and the oligonucleotide, entrapped in a liposome, complexed with a liposome, dispersed in a solution containing a lipid, mixed with a lipid, combined with a lipid, contained as a suspension in a lipid, contained or complexed with a micelle or lipid nanoparticle, or otherwise associated with a lipid. Lipid, lipid/DNA or lipid/expression vector associated compositions are not limited to any particular structure in solution. For example, they may be present in a bilayer structure, as micelles, or with a “collapsed” structure. They may also simply be interspersed in a solution, possibly forming aggregates that are not uniform in size or shape. Lipids are fatty substances which may be naturally occurring or synthetic lipids. For example, lipids include the fatty droplets that naturally occur in the cytoplasm as well as the class of compounds which contain long-chain aliphatic hydrocarbons and their derivatives, such as fatty acids, alcohols, amines, amino alcohols, and aldehydes. Lipids suitable for use can be obtained from commercial sources. For example, dimyristyl phosphatidylcholine (“DMPC”) can be obtained from Sigma, St. Louis, MO; dicetyl phosphate (“DCP”) can be obtained from K & K Laboratories (Plainview, NY); cholesterol (“Choi”) can be obtained from Calbiochem-Behring; dimyristyl phosphatidylglycerol (“DMPG”) and other lipids may be obtained from Avanti Polar Lipids, Inc. (Birmingham, AL). Stock solutions of lipids in chloroform or chloroform/methanol can be stored at about -20°C. Chloroform is used as the only solvent since it is more readily evaporated than methanol. “Liposome” is a generic term encompassing a variety of single and multilamellar lipid vehicles formed by the generation of enclosed lipid bilayers or aggregates. Liposomes can be characterized as having vesicular structures with a phospholipid bilayer membrane and an inner aqueous medium. Multilamellar liposomes have multiple lipid layers separated by aqueous medium. They form spontaneously when phospholipids are suspended in an excess of aqueous solution. The lipid components undergo self-rearrangement before the formation of closed structures and entrap water and dissolved solutes between the lipid bilayers (Ghosh et al., 1991 Glycobiology 5: 505-10). However, compositions that have different structures in solution than the normal vesicular structure are also encompassed. For example, the lipids may assume a micellar structure or merely exist as nonuniform aggregates of lipid molecules. Also contemplated are lipofectamine-nucleic acid complexes. ScFv Antibody In one embodiment, the antibody fragment comprises an scFv fragment. In one embodiment, the ScFv antibody fragment relates to a Fab fragment without the CH1 and CL regions. Thus, in one embodiment, the scFv antibody fragment relates to a Fab fragment comprising the VH and VL. In one embodiment, the scFv antibody fragment comprises a linker between VH and VL. In one embodiment, the scFv antibody fragment comprises the VH, VL and the CH2 and CH3 regions. In one embodiment, the scFv antibody fragment of the invention has modified expression, stability, half-life, antigen binding, heavy chain - light chain pairing, tissue penetration or a combination thereof as compared to a parental MAb. In one embodiment, the scFv antibody fragment of the invention has at least 1.1 fold, at least 1.2 fold, fold, at least 1.3 fold, at least 1.4 fold, at least 1.5 fold, at least 1.6 fold, at least 1.7 fold, at least 1.8 fold, at least 1.9 fold, at least 2 fold, at least 2.1 fold, at least 2.2 fold, at least 2.3 fold, at least 2.4 fold, at least 2.5 fold, at least 2.6 fold, at least 2.7 fold, at least 2.8 fold, at least 2.9 fold, at least 3 fold, at least 3.5 fold, at least 4 fold, at least 4.5 fold, at least 5 fold, at least5.5 fold, at least 6 fold, at least 6.5 fold, at least 7 fold, at least 7.5 fold, at least 8 fold, at least 8.5 fold, at least 9 fold, at least 9.5 fold, at least10 fold, at least 20 fold, at least 30 fold, at least 40 fold, at least 50 fold or greater than 50 fold higher expression than the parental MAb. In one embodiment, the scFv antibody fragment of the invention has at least 1.1 fold, at least 1.2 fold, fold, at least 1.3 fold, at least 1.4 fold, at least 1.5 fold, at least 1.6 fold, at least 1.7 fold, at least 1.8 fold, at least 1.9 fold, at least 2 fold, at least 2.1 fold, at least 2.2 fold, at least 2.3 fold, at least 2.4 fold, at least 2.5 fold, at least 2.6 fold, at least 2.7 fold, at least 2.8 fold, at least 2.9 fold, at least 3 fold, at least 3.5 fold, at least 4 fold, at least 4.5 fold, at least 5 fold, at least5.5 fold, at least 6 fold, at least 6.5 fold, at least 7 fold, at least 7.5 fold, at least 8 fold, at least 8.5 fold, at least 9 fold, at least 9.5 fold, at least10 fold, at least 20 fold, at least 30 fold, at least 40 fold, at least 50 fold or greater than 50 fold higher antigen binding than the parental MAb. In one embodiment, the scFv antibody fragment of the invention has at least 1.1 fold, at least 1.2 fold, fold, at least 1.3 fold, at least 1.4 fold, at least 1.5 fold, at least 1.6 fold, at least 1.7 fold, at least 1.8 fold, at least 1.9 fold, at least 2 fold, at least 2.1 fold, at least 2.2 fold, at least 2.3 fold, at least 2.4 fold, at least 2.5 fold, at least 2.6 fold, at least 2.7 fold, at least 2.8 fold, at least 2.9 fold, at least 3 fold, at least 3.5 fold, at least 4 fold, at least 4.5 fold, at least 5 fold, at least5.5 fold, at least 6 fold, at least 6.5 fold, at least 7 fold, at least 7.5 fold, at least 8 fold, at least 8.5 fold, at least 9 fold, at least 9.5 fold, at least10 fold, at least 20 fold, at least 30 fold, at least 40 fold, at least 50 fold or greater than 50 fold longer half-life than the parental MAb. In one embodiment, the scFv antibody fragment of the invention has at least 1.1 fold, at least 1.2 fold, fold, at least 1.3 fold, at least 1.4 fold, at least 1.5 fold, at least 1.6 fold, at least 1.7 fold, at least 1.8 fold, at least 1.9 fold, at least 2 fold, at least 2.1 fold, at least 2.2 fold, at least 2.3 fold, at least 2.4 fold, at least 2.5 fold, at least 2.6 fold, at least 2.7 fold, at least 2.8 fold, at least 2.9 fold, at least 3 fold, at least 3.5 fold, at least 4 fold, at least 4.5 fold, at least 5 fold, at least5.5 fold, at least 6 fold, at least 6.5 fold, at least 7 fold, at least 7.5 fold, at least 8 fold, at least 8.5 fold, at least 9 fold, at least 9.5 fold, at least10 fold, at least 20 fold, at least 30 fold, at least 40 fold, at least 50 fold or greater than 50 fold higher stability than the parental MAb. In one embodiment, the scFv antibody fragment of the invention has at least 1.1 fold, at least 1.2 fold, fold, at least 1.3 fold, at least 1.4 fold, at least 1.5 fold, at least 1.6 fold, at least 1.7 fold, at least 1.8 fold, at least 1.9 fold, at least 2 fold, at least 2.1 fold, at least 2.2 fold, at least 2.3 fold, at least 2.4 fold, at least 2.5 fold, at least 2.6 fold, at least 2.7 fold, at least 2.8 fold, at least 2.9 fold, at least 3 fold, at least 3.5 fold, at least 4 fold, at least 4.5 fold, at least 5 fold, at least5.5 fold, at least 6 fold, at least 6.5 fold, at least 7 fold, at least 7.5 fold, at least 8 fold, at least 8.5 fold, at least 9 fold, at least 9.5 fold, at least10 fold, at least 20 fold, at least 30 fold, at least 40 fold, at least 50 fold or greater than 50 fold greater tissue penetration than the parental MAb. In one embodiment, the scFv antibody fragment of the invention has at least 1.1 fold, at least 1.2 fold, fold, at least 1.3 fold, at least 1.4 fold, at least 1.5 fold, at least 1.6 fold, at least 1.7 fold, at least 1.8 fold, at least 1.9 fold, at least 2 fold, at least 2.1 fold, at least 2.2 fold, at least 2.3 fold, at least 2.4 fold, at least 2.5 fold, at least 2.6 fold, at least 2.7 fold, at least 2.8 fold, at least 2.9 fold, at least 3 fold, at least 3.5 fold, at least 4 fold, at least 4.5 fold, at least 5 fold, at least5.5 fold, at least 6 fold, at least 6.5 fold, at least 7 fold, at least 7.5 fold, at least 8 fold, at least 8.5 fold, at least 9 fold, at least 9.5 fold, at least10 fold, at least 20 fold, at least 30 fold, at least 40 fold, at least 50 fold or greater than 50 fold greater heavy chain - light chain pairing than the parental MAb. Delivery Vehicles In one embodiment, the present invention provides a composition comprising a delivery vehicle comprising a NKCE, fragment thereof, or nucleic acid molecule encoding the same, as described herein. In one embodiment, the nucleic acid molecule encoding the NKCE comprises an mRNA molecule. Exemplary delivery vehicles include, but are not limited to, microspheres, microparticles, nanoparticles, polymerosomes, liposomes, and micelles. For example, in some embodiments, the delivery vehicle is a lipid nanoparticle loaded with a nucleic acid molecule encoding a NKCE of the invention or a fragment thereof. In one embodiment, the nucleic acid molecule encoding the NKCE comprises an mRNA molecule. In some embodiments, the delivery vehicle provides for controlled release, delayed release, or continual release of its loaded cargo. In some embodiments, the delivery vehicle comprises a targeting moiety that targets the delivery vehicle to a treatment site. In certain instances, expressing a protein by delivering the encoding mRNA has many benefits over methods that use protein, plasmid DNA or viral vectors. During mRNA transfection, the coding sequence of the desired protein is the only substance delivered to cells, thus avoiding all the side effects associated with plasmid backbones, viral genes, and viral proteins. More importantly, unlike DNA- and viral- based vectors, the mRNA does not carry the risk of being incorporated into the genome and protein production starts immediately after mRNA delivery. For example, high levels of circulating proteins have been measured within 15 to 30 min of in vivo injection of the encoding mRNA. In certain embodiments, using mRNA rather than the protein also has many advantages. Half-lives of proteins in the circulation are often short, thus protein treatment would need frequent dosing, while mRNA provides a template for continuous protein production for several days. Purification of proteins is problematic and they can contain aggregates and other impurities that cause adverse effects (Kromminga and Schellekens, 2005, Ann NY Acad Sci 1050:257-265). In order to confirm the presence of the mRNA sequence in the host cell, a variety of assays may be performed. Such assays include, for example, “molecular biological” assays well known to those of skill in the art, such as Northern blotting and RT-PCR; “biochemical” assays, such as detecting the presence or absence of a particular peptide, e.g., by immunogenic means (ELISAs and Western blots) or by assays described herein to identify agents falling within the scope of the invention. CAR Molecules In one embodiment, the invention provides a chimeric antigen receptor (CAR) comprising a binding domain comprising a NKCE of the invention. In one embodiment, the CAR comprises an antigen binding domain. In one embodiment, the antigen binding domain is a targeting domain, wherein the targeting domain directs the cell expressing the CAR to a cell or particle expressing a sialic acid-binding receptor. In various embodiments, the CAR can be a “first generation,” “second generation,” “third generation,” “fourth generation” or “fifth generation” CAR (see, for example, Sadelain et al., Cancer Discov.3(4):388-398 (2013); Jensen et al., Immunol. Rev.257:127-133 (2014); Sharpe et al., Dis. Model Mech.8(4):337-350 (2015); Brentjens et al., Clin. Cancer Res.13:5426-5435 (2007); Gade et al., Cancer Res. 65:9080-9088 (2005); Maher et al., Nat. Biotechnol.20:70-75 (2002); Kershaw et al., J. Immunol.173:2143-2150 (2004); Sadelain et al., Curr. Opin. Immunol. (2009); Hollyman et al., J. Immunother.32:169-180 (2009)). “First generation” CARs for use in the invention comprise an antigen binding domain, for example, a single-chain variable fragment (scFv), fused to a transmembrane domain, which is fused to a cytoplasmic/intracellular domain of the T cell receptor chain. “First generation” CARs typically have the intracellular domain from the CD3ζ-chain, which is the primary transmitter of signals from endogenous T cell receptors (TCRs). “First generation” CARs can provide de novo antigen recognition and cause activation of both CD4+ and CD8+ T cells through their CD3ζ chain signaling domain in a single fusion molecule, independent of HLA-mediated antigen presentation. “Second-generation” CARs for use in the invention comprise an antigen binding domain, for example, a single-chain variable fragment (scFv), fused to an intracellular signaling domain capable of activating T cells and a co-stimulatory domain designed to augment T cell potency and persistence (Sadelain et al., Cancer Discov. 3:388-398 (2013)). CAR design can therefore combine antigen recognition with signal transduction, two functions that are physiologically borne by two separate complexes, the TCR heterodimer and the CD3 complex. “Second generation” CARs include an intracellular domain from various co-stimulatory molecules, for example, CD28, 4-1BB, ICOS, OX40, and the like, in the cytoplasmic tail of the CAR to provide additional signals to the cell. “Second generation” CARs provide both co-stimulation, for example, by CD28 or 4-1BB domains, and activation, for example, by a CD3ζ signaling domain. Preclinical studies have indicated that “Second Generation” CARs can improve the anti- tumor activity of T cells. For example, robust efficacy of “Second Generation” CAR modified T cells was demonstrated in clinical trials targeting the CD19 molecule in patients with chronic lymphoblastic leukemia (CLL) and acute lymphoblastic leukemia (ALL) (Davila et al., Oncoimmunol.1(9):1577-1583 (2012)). “Third generation” CARs provide multiple co-stimulation, for example, by comprising both CD28 and 4-1BB domains, and activation, for example, by comprising a CD3ζ activation domain. “Fourth generation” CARs provide co-stimulation, for example, by CD28 or 4-1BB domains, and activation, for example, by a CD3ζ signaling domain in addition to a constitutive or inducible chemokine component. “Fifth generation” CARs provide co-stimulation, for example, by CD28 or 4-1BB domains, and activation, for example, by a CD3ζ signaling domain, a constitutive or inducible chemokine component, and an intracellular domain of a cytokine receptor, for example, IL-2Rβ. In various embodiments, the CAR can be included in a multivalent CAR system, for example, a DualCAR or “TandemCAR” system. Multivalent CAR systems include systems or cells comprising multiple CARs and systems or cells comprising bivalent/bispecific CARs targeting more than one antigen. In the embodiments disclosed herein, the CARs generally comprise an antigen binding domain, a transmembrane domain and an intracellular domain, as described above. In a particular non-limiting embodiment, the antigen-binding domain is a bispecific sialic acid-binding receptor antibody, or a variant thereof, specific for binding to a sialic acid-binding receptor. Substrates In one embodiment, the present invention provides a scaffold, substrate, or device comprising a NKCE, fragment thereof, or nucleic acid molecule encoding the same. For example, in some embodiments, the present invention provides a tissue engineering scaffold, including but not limited to, a hydrogel, electrospun scaffold, polymeric matrix, or the like, comprising the modulator. In certain embodiments, a NKCE, fragment thereof, or nucleic acid molecule encoding the same, may be coated along the surface of the scaffold, substrate, or device. In certain embodiments, the NKCE, fragment thereof, or nucleic acid molecule encoding the same is encapsulated within the scaffold, substrate, or device. Pharmaceutical Compositions The present invention also provides pharmaceutical compositions comprising one or more of the compositions described herein. Formulations may be employed in admixtures with conventional excipients, i.e., pharmaceutically acceptable organic or inorganic carrier substances suitable for administration to a treatment site. The pharmaceutical compositions may be sterilized and if desired mixed with auxiliary agents, e.g., lubricants, preservatives, stabilizers, wetting agents, emulsifiers, salts for influencing osmotic pressure buffers, coloring, and/or aromatic substances and the like. They may also be combined where desired with other active agents, e.g., other analgesic agents. Administration of the compositions of this invention may be carried out, for example, by parenteral, by intravenous, subcutaneous, intramuscular, or intraperitoneal injection, or by infusion or by any other acceptable systemic method. As used herein, “additional ingredients” include, but are not limited to, one or more of the following: excipients; surface active agents; dispersing agents; inert diluents; granulating and disintegrating agents; binding agents; lubricating agents; coloring agents; preservatives; physiologically degradable compositions such as gelatin; aqueous vehicles and solvents; oily vehicles and solvents; suspending agents; dispersing or wetting agents; emulsifying agents, demulcents; buffers; salts; thickening agents; fillers; emulsifying agents; antioxidants; antibiotics; antifungal agents; stabilizing agents; and pharmaceutically acceptable polymeric or hydrophobic materials. Other “additional ingredients” that may be included in the pharmaceutical compositions of the invention are known in the art and described, for example in Genaro, ed. (1985, Remington’s Pharmaceutical Sciences, Mack Publishing Co., Easton, PA), which is incorporated herein by reference. The composition of the invention may comprise a preservative from about 0.005% to 2.0% by total weight of the composition. The preservative is used to prevent spoilage in the case of exposure to contaminants in the environment. Examples of preservatives useful in accordance with the invention included but are not limited to those selected from the group: benzyl alcohol, sorbic acid, parabens, imidurea and combinations thereof. In one embodiment, the composition includes an anti-oxidant and a chelating agent that inhibits the degradation of one or more components of the composition. Exemplary antioxidants for some compounds are BHT, BHA, alpha- tocopherol and ascorbic acid. Exemplary chelating agents include edetate salts (e.g. disodium edetate) and citric acid. The chelating agent is useful for chelating metal ions in the composition that may be detrimental to the shelf life of the formulation. While BHT and disodium edetate may be the antioxidant and chelating agent respectively for some compounds, other suitable and equivalent antioxidants and chelating agents may be substituted therefore as would be known to those skilled in the art. Liquid suspensions may be prepared using conventional methods to achieve suspension of the compounds or other compositions of the invention in an aqueous or oily vehicle. Aqueous vehicles include, for example, water, and isotonic saline. Oily vehicles include, for example, almond oil, oily esters, ethyl alcohol, vegetable oils such as arachis, olive, sesame, or coconut oil, fractionated vegetable oils, and mineral oils such as liquid paraffin. Liquid suspensions may further comprise one or more additional ingredients including, but not limited to, suspending agents, dispersing or wetting agents, emulsifying agents, demulcents, preservatives, buffers, salts, flavorings, coloring agents, and sweetening agents. Oily suspensions may further comprise a thickening agent. Known suspending agents include, but are not limited to, sorbitol syrup, hydrogenated edible fats, sodium alginate, polyvinylpyrrolidone, gum tragacanth, gum acacia, and cellulose derivatives such as sodium carboxymethylcellulose, methylcellulose, hydroxypropylmethylcellulose. Known dispersing or wetting agents include, but are not limited to, naturally occurring phosphatides such as lecithin, condensation products of an alkylene oxide with a fatty acid, with a long chain aliphatic alcohol, with a partial ester derived from a fatty acid and a hexitol, or with a partial ester derived from a fatty acid and a hexitol anhydride (e.g., polyoxyethylene stearate, heptadecaethyleneoxycetanol, polyoxyethylene sorbitol monooleate, and polyoxyethylene sorbitan monooleate, respectively). Known emulsifying agents include, but are not limited to, lecithin, and acacia. Known preservatives include, but are not limited to, methyl, ethyl, or n-propyl para hydroxybenzoates, ascorbic acid, and sorbic acid. For oral application, particularly suitable are tablets, dragees, liquids, drops, suppositories, or capsules, caplets and gelcaps. Other formulations suitable for oral administration include, but are not limited to, a powdered or granular formulation, an aqueous or oily suspension, an aqueous or oily solution, a paste, a gel, toothpaste, a mouthwash, a coating, an oral rinse, chewing gum, varnishes, sealants, oral and teeth “dissolving strips”, or an emulsion. The compositions intended for oral use may be prepared according to any method known in the art and such compositions may contain one or more agents selected from the group consisting of inert, non-toxic pharmaceutically excipients that are suitable for the manufacture of tablets. Such excipients include, for example an inert diluent such as lactose; granulating and disintegrating agents such as cornstarch; binding agents such as starch; and lubricating agents such as magnesium stearate. Tablets may be non-coated or they may be coated using known methods to achieve delayed disintegration in the gastrointestinal tract of a subject, thereby providing sustained release and absorption of the active ingredient. By way of example, a material such as glyceryl monostearate or glyceryl distearate may be used to coat tablets. Further by way of example, tablets may be coated using methods described in U.S. Patents numbers 4,256,108; 4,160,452; and 4,265,874 to form osmotically controlled release tablets. Tablets may further comprise a sweetening agent, a flavoring agent, a coloring agent, a preservative, or some combination of these in order to provide for pharmaceutically elegant and palatable preparation. Hard capsules comprising the active ingredient may be made using a physiologically degradable composition, such as gelatin. Such hard capsules comprise the active ingredient, and may further comprise additional ingredients including, for example, an inert solid diluent such as calcium carbonate, calcium phosphate, or kaolin. Soft gelatin capsules comprising the active ingredient may be made using a physiologically degradable composition, such as gelatin. Such soft capsules comprise the active ingredient, which may be mixed with water or an oil medium such as peanut oil, liquid paraffin, or olive oil. For oral administration, the compositions of the invention may be in the form of tablets or capsules prepared by conventional means with pharmaceutically acceptable excipients such as binding agents; fillers; lubricants; disintegrates; or wetting agents. If desired, the tablets may be coated using suitable methods and coating materials such as OPADRY™ film coating systems available from Colorcon, West Point, Pa. (e.g., OPADRY™ OY Type, OYC Type, Organic Enteric OY-P Type, Aqueous Enteric OY-A Type, OY-PM Type and OPADRY™ White, 32K18400). Liquid preparation for oral administration may be in the form of solutions, syrups or suspensions. The liquid preparations may be prepared by conventional means with pharmaceutically acceptable additives such as suspending agents (e.g., sorbitol syrup, methyl cellulose or hydrogenated edible fats); emulsifying agent (e.g., lecithin or acacia); non-aqueous vehicles (e.g., almond oil, oily esters or ethyl alcohol); and preservatives (e.g., methyl or propyl p-hydroxy benzoates or sorbic acid). Liquid formulations of a pharmaceutical composition of the invention which are suitable for oral administration may be prepared, packaged, and sold either in liquid form or in the form of a dry product intended for reconstitution with water or another suitable vehicle prior to use. A tablet comprising the active ingredient may, for example, be made by compressing or molding the active ingredient, optionally with one or more additional ingredients. Compressed tablets may be prepared by compressing, in a suitable device, the active ingredient in a free-flowing form such as a powder or granular preparation, optionally mixed with one or more of a binder, a lubricant, an excipient, a surface active agent, and a dispersing agent. Molded tablets may be made by molding, in a suitable device, a mixture of the active ingredient, a pharmaceutically acceptable carrier, and at least sufficient liquid to moisten the mixture. Pharmaceutically acceptable excipients used in the manufacture of tablets include, but are not limited to, inert diluents, granulating and disintegrating agents, binding agents, and lubricating agents. Known dispersing agents include, but are not limited to, potato starch and sodium starch glycollate. Known surface-active agents include, but are not limited to, sodium lauryl sulphate. Known diluents include, but are not limited to, calcium carbonate, sodium carbonate, lactose, microcrystalline cellulose, calcium phosphate, calcium hydrogen phosphate, and sodium phosphate. Known granulating and disintegrating agents include, but are not limited to, corn starch and alginic acid. Known binding agents include, but are not limited to, gelatin, acacia, pre-gelatinized maize starch, polyvinylpyrrolidone, and hydroxypropyl methylcellulose. Known lubricating agents include, but are not limited to, magnesium stearate, stearic acid, silica, and talc. Formulations of a pharmaceutical composition suitable for parenteral administration comprise the active ingredient combined with a pharmaceutically acceptable carrier, such as sterile water or sterile isotonic saline. Such formulations may be prepared, packaged, or sold in a form suitable for bolus administration or for continuous administration. Injectable formulations may be prepared, packaged, or sold in unit dosage form, such as in ampules or in multi-dose containers containing a preservative. Formulations for parenteral administration include, but are not limited to, suspensions, solutions, emulsions in oily or aqueous vehicles, pastes, and implantable sustained-release or biodegradable formulations. Such formulations may further comprise one or more additional ingredients including, but not limited to, suspending, stabilizing, or dispersing agents. In one embodiment of a formulation for parenteral administration, the active ingredient is provided in dry (i.e., powder or granular) form for reconstitution with a suitable vehicle (e.g., sterile pyrogen-free water) prior to parenteral administration of the reconstituted composition. The pharmaceutical compositions may be prepared, packaged, or sold in the form of a sterile injectable aqueous or oily suspension or solution. This suspension or solution may be formulated according to the known art, and may comprise, in addition to the active ingredient, additional ingredients such as the dispersing agents, wetting agents, or suspending agents described herein. Such sterile injectable formulations may be prepared using a non-toxic parenterally-acceptable diluent or solvent, such as water or 1,3-butane diol, for example. Other acceptable diluents and solvents include, but are not limited to, Ringer’s solution, isotonic sodium chloride solution, and fixed oils such as synthetic mono- or di-glycerides. Other parentally-administrable formulations that are useful include those that comprise the active ingredient in microcrystalline form, in a liposomal preparation, or as a component of a biodegradable polymer system. Compositions for sustained release or implantation may comprise pharmaceutically acceptable polymeric or hydrophobic materials such as an emulsion, an ion exchange resin, a sparingly soluble polymer, or a sparingly soluble salt. Excipients and Other Components of the Composition The composition may further comprise a pharmaceutically acceptable excipient. The pharmaceutically acceptable excipient can be functional molecules such as vehicles, adjuvants, carriers, or diluents. The pharmaceutically acceptable excipient can be a transfection facilitating agent, which can include surface active agents, such as immune-stimulating complexes (ISCOMS), Freunds incomplete adjuvant, LPS analog including monophosphoryl lipid A, muramyl peptides, quinone analogs, vesicles such as squalene and squalene, hyaluronic acid, lipids, liposomes, calcium ions, viral proteins, polyanions, polycations, or nanoparticles, or other known transfection facilitating agents. The transfection facilitating agent is a polyanion, polycation, including poly-L-glutamate (LGS), or lipid. The transfection facilitating agent is poly-L-glutamate, and the poly-L-glutamate may be present in the composition at a concentration less than 6 mg/ml. The transfection facilitating agent may also include surface active agents such as immune-stimulating complexes (ISCOMS), Freunds incomplete adjuvant, LPS analog including monophosphoryl lipid A, muramyl peptides, quinone analogs and vesicles such as squalene and squalene, and hyaluronic acid may also be used administered in conjunction with the composition. The composition may also include transfection facilitating agents such as lipids, liposomes, including lecithin liposomes or other liposomes known in the art, as a DNA-liposome mixture (see for example W09324640), calcium ions, viral proteins, polyanions, polycations, or nanoparticles, or other known transfection facilitating agents. The transfection facilitating agent is a polyanion, polycation, including poly-L-glutamate (LGS), or lipid. Concentration of the transfection agent in the composition is less than 4 mg/ml, less than 2 mg/ml, less than 1 mg/ml, less than 0.750 mg/ml, less than 0.500 mg/ml, less than 0.250 mg/ml, less than 0.100 mg/ml, less than 0.050 mg/ml, or less than 0.010 mg/ml. The pharmaceutically acceptable excipient can be an adjuvant in addition to the checkpoint inhibitor antibodies of the invention. The additional adjuvant can be other genes that are expressed in an alternative plasmid or are delivered as proteins in combination with the plasmid above in the composition. The adjuvant may be selected from the group consisting of: α-interferon(IFN- α), β-interferon (IFN-β), γ-interferon, platelet derived growth factor (PDGF), TNFα, TNFβ, GM-CSF, epidermal growth factor (EGF), cutaneous T cell-attracting chemokine (CTACK), epithelial thymus-expressed chemokine (TECK), mucosae-associated epithelial chemokine (MEC), IL-12, IL-15, MHC, CD80, CD86 including IL-15 having the signal sequence deleted and optionally including the signal peptide from IgE. The adjuvant can be IL-12, IL-15, IL-28, CTACK, TECK, platelet derived growth factor (PDGF), TNF ^, TNF ^, GM-CSF, epidermal growth factor (EGF), IL-1, IL-2, IL-4, IL-5, PD-1, IL-10, IL-12, IL-18, or a combination thereof. Other genes that can be useful as adjuvants in addition to the antibodies of the invention include those encoding: MCP-1, MIP-la, MIP-1p, IL-8, RANTES, L- selectin, P-selectin, E-selectin, CD34, GlyCAM-1, MadCAM-1, LFA-1, VLA-1, Mac-1, pl50.95, PECAM, ICAM-1, ICAM-2, ICAM-3, CD2, LFA-3, M-CSF, G-CSF, IL-4, mutant forms of IL-18, CD40, CD40L, vascular growth factor, fibroblast growth factor, IL-7, IL-22, nerve growth factor, vascular endothelial growth factor, Fas, TNF receptor, Flt, Apo-1, p55, WSL-1, DR3, TRAMP, Apo-3, AIR, LARD, NGRF, DR4, DR5, KILLER, TRAIL-R2, TRICK2, DR6, Caspase ICE, Fos, c-jun, Sp-1, Ap-1, Ap-2, p38, p65Rel, MyD88, IRAK, TRAF6, IkB, Inactive NIK, SAP K, SAP-1, JNK, interferon response genes, NFkB, Bax, TRAIL, TRAILrec, TRAILrecDRC5, TRAIL-R3, TRAIL- R4, RANK, RANK LIGAND, Ox40, Ox40 LIGAND, NKG2D, MICA, MICB, NKG2A, NKG2B, NKG2C, NKG2E, NKG2F, TAP1, TAP2 and functional fragments thereof. The composition may further comprise a genetic facilitator agent as described in U.S. Serial No.021,579 filed April 1, 1994, which is fully incorporated by reference. The composition may comprise DNA at quantities of from about 1 nanogram to 100 milligrams; about 1 microgram to about 10 milligrams; or preferably about 0.1 microgram to about 10 milligrams; or more preferably about 1 milligram to about 2 milligrams. In some preferred embodiments, composition according to the present invention comprises about 5 nanogram to about 1000 micrograms of DNA. In some preferred embodiments, composition can contain about 10 nanograms to about 800 micrograms of DNA. In some preferred embodiments, the composition can contain about 0.1 to about 500 micrograms of DNA. In some preferred embodiments, the composition can contain about 1 to about 350 micrograms of DNA. In some preferred embodiments, the composition can contain about 25 to about 250 micrograms, from about 100 to about 200 microgram, from about 1 nanogram to 100 milligrams; from about 1 microgram to about 10 milligrams; from about 0.1 microgram to about 10 milligrams; from about 1 milligram to about 2 milligram, from about 5 nanogram to about 1000 micrograms, from about 10 nanograms to about 800 micrograms, from about 0.1 to about 500 micrograms, from about 1 to about 350 micrograms, from about 25 to about 250 micrograms, from about 100 to about 200 microgram of DNA. The composition can be formulated according to the mode of administration to be used. An injectable pharmaceutical composition can be sterile, pyrogen free and particulate free. An isotonic formulation or solution can be used. Additives for isotonicity can include sodium chloride, dextrose, mannitol, sorbitol, and lactose. The composition can comprise a vasoconstriction agent. The isotonic solutions can include phosphate buffered saline. The composition can further comprise stabilizers including gelatin and albumin. The stabilizers can allow the formulation to be stable at room or ambient temperature for extended periods of time, including LGS or polycations or polyanions. Methods of Delivery Using Engineered Immune Cells In one embodiment, the present invention provides a method for delivery of a bispecific sialic acid-binding receptor antibody to a target cell providing an engineered immune cell expressing the bispecific sialic acid-binding receptor antibody. In one embodiment, the immune cell is engineered for endogenous secretion of the bispecific sialic acid-binding receptor antibody of the invention. In various embodiments, the invention relates to a composition comprising an immune cell engineered for expression or endogenous secretion of a bispecific anti- sialic acid-binding receptor antibody targeting a tumor cell. Examples of immune cells that can be engineered for expression or secretion of a bispecific sialic acid-binding receptor antibody of the invention include, but are not limited to, T cells, B cells, natural killer (NK) cells, or macrophages. In some embodiments, the immune cell further comprises a chimeric antigen receptor (CAR). Therefore, in some embodiments, the invention relates to the use of CAR T-cells for expression or delivery of a bispecific sialic acid-binding receptor antibody of the invention. Methods of Administration The present invention provides a method for increasing a function or activity of natural killer (NK) cells. This can be measured for example in a standard NK- or T-cell based cytotoxicity assay, in which the capacity of a therapeutic compound to stimulate killing of sialic-acid ligand positive cells by Siglec positive lymphocytes is measured. In one embodiment, an antibody preparation causes at least a 10% augmentation in the cytotoxicity of a Siglec-restricted lymphocyte, optionally at least a 40% or 50% augmentation in lymphocyte cytotoxicity, or optionally at least a 70% augmentation in NK cytotoxicity, and referring to the cytotoxicity assays described. In one embodiment, an antibody preparation causes at least a 10% augmentation in cytokine release by a Siglec-restricted lymphocyte, optionally at least a 40% or 50% augmentation in cytokine release, or optionally at least a 70% augmentation in cytokine release, and referring to the cytotoxicity assays described. In one embodiment, an antibody preparation causes at least a 10% augmentation in cell surface expression of a marker of cytotoxicity (e.g. CD107 and/or CD137) by a Siglec-restricted lymphocyte, optionally at least a 40% or 50% augmentation, or optionally at least a 70% augmentation in cell surface expression of a marker of cytotoxicity (e.g. CD107 and/or CD137). The present invention is also directed to a method of increasing an immune response in a subject. Increasing the immune response can be used to treat and/or prevent disease in the subject. The method can include administering the herein disclosed vaccine to the subject. The subject administered the vaccine can have an increased or boosted immune response as compared to a subject administered the antigen alone. In some embodiments, the immune response can be increased by about 0.5-fold to about 15-fold, about 0.5-fold to about 10-fold, or about 0.5-fold to about 8-fold. Alternatively, the immune response in the subject administered the vaccine can be increased by at least about 0.5-fold, at least about 1.0-fold, at least about 1.5-fold, at least about 2.0-fold, at least about 2.5-fold, at least about 3.0-fold, at least about 3.5-fold, at least about 4.0-fold, at least about 4.5-fold, at least about 5.0-fold, at least about 5.5-fold, at least about 6.0-fold, at least about 6.5-fold, at least about 7.0-fold, at least about 7.5- fold, at least about 8.0-fold, at least about 8.5-fold, at least about 9.0-fold, at least about 9.5-fold, at least about 10.0-fold, at least about 10.5-fold, at least about 11.0-fold, at least about 11.5-fold, at least about 12.0-fold, at least about 12.5-fold, at least about 13.0-fold, at least about 13.5-fold, at least about 14.0-fold, at least about 14.5-fold, or at least about 15.0-fold. In still other alternative embodiments, the immune response in the subject administered the vaccine can be increased about 50% to about 1500%, about 50% to about 1000%, or about 50% to about 800%. In other embodiments, the immune response in the subject administered the vaccine can be increased by at least about 50%, at least about 100%, at least about 150%, at least about 200%, at least about 250%, at least about 300%, at least about 350%, at least about 400%, at least about 450%, at least about 500%, at least about 550%, at least about 600%, at least about 650%, at least about 700%, at least about 750%, at least about 800%, at least about 850%, at least about 900%, at least about 950%, at least about 1000%, at least about 1050%, at least about 1100%, at least about 1150%, at least about 1200%, at least about 1250%, at least about 1300%, at least about 1350%, at least about 1450%, or at least about 1500%. The vaccine dose can be between 1 μg to 10 mg active component/kg body weight/time, and can be 20 μg to 10 mg component/kg body weight/time. The vaccine can be administered every 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, or 31 days. The number of vaccine doses for effective treatment can be 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10. Vaccine In one embodiment, the invention relates to the administration of a bispecific antibody comprising a combination of a sialic acid receptor antibody, or a fragment thereof, or variant thereof, and an antibody specific for binding to a tumor antigen, or a nucleic acid molecule encoding a bispecific antibody comprising a combination of a sialic acid receptor antibody, or a fragment thereof, or variant thereof, and an antibody specific for binding to a tumor antigen. The immunogenic composition can be used to increase the killing of a target cell expressing the tumor antigen. The immunogenic composition can be a DNA vaccine, a peptide vaccine, or a combination DNA and peptide vaccine. The DNA vaccine can include a nucleic acid sequence encoding the tumor antigen. The nucleic acid sequence can be DNA, RNA, cDNA, a variant thereof, a fragment thereof, or a combination thereof. The nucleic acid sequence can also include additional sequences that encode linker, leader, or tag sequences that are linked to the sequence encoding the bispecific antibody of the invention by a peptide bond. The tumor cell killing induced by the vaccine can include an increased level of killing of cells expressing the targeted tumor antigen in the subject administered the vaccine as compared to a subject not administered the vaccine. The level of tumor cell killing in a subject administered the vaccine can be increased by about 1.5-fold to about 16-fold, about 2-fold to about 12-fold, or about 3-fold to about 10-fold as compared to the subject not administered the vaccine. The level of tumor cell killing in a subject administered the vaccine can be increased by at least about 1.5-fold, at least about 2.0- fold, at least about 2.5-fold, at least about 3.0-fold, at least about 3.5-fold, at least about 4.0-fold, at least about 4.5-fold, at least about 5.0-fold, at least about 5.5-fold, at least about 6.0-fold, at least about 6.5-fold, at least about 7.0-fold, at least about 7.5-fold, at least about 8.0-fold, at least about 8.5-fold, at least about 9.0-fold, at least about 9.5-fold, at least about 10.0-fold, at least about 10.5-fold, at least about 11.0-fold, at least about 11.5-fold, at least about 12.0-fold, at least about 12.5-fold, at least about 13.0-fold, at least about 13.5-fold, at least about 14.0-fold, at least about 14.5-fold, at least about 15.0- fold, at least about 15.5-fold, or at least about 16.0-fold as compared to the subject not administered the vaccine. The vaccine of the present invention can have features required of effective vaccines such as being safe so the vaccine itself does not cause illness or death; is protective against illness resulting from the presence of cells expressing the target antigen; and provides ease of administration, few side effects, biological stability, and low cost per dose. In some embodiments, the NKCE is directed to a pathogen associated or viral antigen, which can be used to direct NK cells to a pathogen or virus infected cell. In some embodiments, the antigen comprises a viral antigen, including but not limited to, an antigen of a coronavirus (e.g., SARS-CoV-2), Influenza virua, Zika virus, Ebola virus, Japanese encephalitis virus, mumps virus, measles virus, rabies virus, varicella-zoster, Epstein-Barr virus (HHV-4), cytomegalovirus, herpes simplex virus 1 (HSV-1) and herpes simplex virus 2 (HSV-2), human immunodeficiency virus-1 (HIV-1), JC virus, arborviruses, enteroviruses, West Nile virus, dengue virus, poliovirus, and varicella zoster virus. In some embodiments, the antigen comprises a bacterial antigen, including, but not limited to, an antigen of Streptococcus pneumoniae, Neisseria meningitides, Streptococcus agalactia, and Escherichia coli. In some embodiments, the antigen comprises a fungal or protozoan antigen, including, but not limited to, an antigen of Candidiasis, Aspergillosis, Cryptococcosis, and Toxoplasma gondii. Self Antigen The NKCE of the invention can be specific for binding to a self-antigen. In some embodiments, the self-antigen is an antigen associated with an autoimmune disease or disorder. In some embodiments, the self-antigen is a tumor antigen. Therefore, in some embodiments, the present invention includes compositions for directing natural killer cells to a tumor cell. In some embodiments, the tumor cell expresses an antigen targeted by the NKCE of the invention. As a non-limiting example, in one embodiment, the invention provides a bi-specific FSHR-siglec 7 NKCE which directs natural killer cells to a tumor cell expressing FSHR. Exemplary tumor cells expressing FSHR may include, but are not limited to, tumor cells from an ovarian cancer, breast cancer, prostate cancer, renal cancer, colo-rectal cancer, stomach cancer, lung cancer, testicular cancer, endometrial cancer, and thyroid cancer. In one embodiment, the antigen targeted by the NKCE of the invention is a tumor associated surface antigen. Illustrative examples of a tumor associated surface antigen are CD10, CD19, CD20, CD22, CD33, Fms-like tyrosine kinase 3 (FLT-3, CD135), chondroitin sulfate proteoglycan 4 (CSPG4, melanoma-associated chondroitin sulfate proteoglycan), Epidermal growth factor receptor (EGFR), Her2neu, Her3, IGFR, CD133, IL3R, fibroblast activating protein (FAP), CDCP1, Derlin1, Tenascin, frizzled 1- 10, the vascular antigens VEGFR2 (KDR/FLK1), VEGFR3 (FLT4, CD309), PDGFR- .alpha. (CD140a), PDGFR-.beta. (CD140b) Endoglin, CLEC14, Tem1-8, and Tie2. Further examples may include A33, CAMPATH-1 (CDw52), Carcinoembryonic antigen (CEA), Carboanhydrase IX (MN/CA IX), CD21, CD25, CD30, CD34, CD37, CD44v6, CD45, CD133, de2-7 EGFR, EGFRvIII, EpCAM, Ep-CAM, Folate-binding protein, G250, Fms-like tyrosine kinase 3 (FLT-3, CD135), c-Kit (CD117), CSF1R (CD115), HLA-DR, IGFR, IL-2 receptor, IL3R, MCSP (Melanoma-associated cell surface chondroitin sulphate proteoglycane), Muc-1, Prostate-specific membrane antigen (PSMA), Prostate stem cell antigen (PSCA), Prostate specific antigen (PSA), and TAG- 72. In the context of the present invention, “tumor antigen” or “hyperproliferative disorder antigen” or “antigen associated with a hyperproliferative disorder,” refers to antigens that are common to specific hyperproliferative disorders such as cancer. The antigens discussed herein are merely included by way of example. The list is not intended to be exclusive and further examples will be readily apparent to those of skill in the art. Tumor antigens are proteins that are produced by tumor cells that can be targeted by a NKCE of the invention. The selection of the antigen binding moiety of the NKCE of the invention will depend on the particular type of cancer to be treated. Tumor antigens are well known in the art and include, for example, a glioma-associated antigen, carcinoembryonic antigen (CEA), β-human chorionic gonadotropin, alphafetoprotein (AFP), lectin-reactive AFP, thyroglobulin, RAGE-1, MN-CA IX, human telomerase reverse transcriptase, RU1, RU2 (AS), intestinal carboxyl esterase, mut hsp70-2, M-CSF, prostase, prostate-specific antigen (PSA), PAP, NY-ESO-1, LAGE-1a, p53, prostein, PSMA, Her2/neu, survivin and telomerase, prostate-carcinoma tumor antigen-1 (PCTA- 1), MAGE, ELF2M, neutrophil elastase, ephrinB2, CD22, insulin growth factor (IGF)-I, IGF-II, IGF-I receptor and mesothelin. In one embodiment, the tumor antigen comprises one or more antigenic cancer epitopes associated with a malignant tumor. Malignant tumors express a number of proteins that can serve as target antigens for an immune attack. These molecules include but are not limited to tissue-specific antigens such as MART-1, tyrosinase and GP 100 in melanoma and prostatic acid phosphatase (PAP) and prostate-specific antigen (PSA) in prostate cancer. Other target molecules belong to the group of transformation- related molecules such as the oncogene HER-2/Neu/ErbB-2. Yet another group of target antigen are onco-fetal antigens such as carcinoembryonic antigen (CEA). In B-cell lymphoma the tumor-specific idiotype immunoglobulin constitutes a truly tumor-specific immunoglobulin antigen that is unique to the individual tumor. B-cell differentiation antigens such as CD19, CD20 and CD37 are other candidates for target antigens in B-cell lymphoma. Some of these antigens (CEA, HER-2, CD19, CD20, idiotype) have been used as targets for passive immunotherapy with monoclonal antibodies with limited success. The type of tumor antigen referred to in the invention may also be a tumor-specific antigen (TSA) or a tumor-associated antigen (TAA). A TSA is unique to tumor cells and does not occur on other cells in the body. A TAA associated antigen is not unique to a tumor cell and instead is also expressed on a normal cell under conditions that fail to induce a state of immunologic tolerance to the antigen. The expression of the antigen on the tumor may occur under conditions that enable the immune system to respond to the antigen. TAAs may be antigens that are expressed on normal cells during fetal development when the immune system is immature and unable to respond or they may be antigens that are normally present at extremely low levels on normal cells but which are expressed at much higher levels on tumor cells. Non-limiting examples of TSA or TAA antigens include the following: Differentiation antigens such as MART-1/MelanA (MART-I), gp100 (Pmel 17), tyrosinase, TRP-1, TRP-2 and tumor-specific multilineage antigens such as MAGE-1, MAGE-3, BAGE, GAGE-1, GAGE-2, p15; overexpressed embryonic antigens such as CEA; overexpressed oncogenes and mutated tumor-suppressor genes such as p53, Ras, HER-2/neu; unique tumor antigens resulting from chromosomal translocations; such as BCR-ABL, E2A-PRL, H4-RET, IGH-IGK, MYL-RAR; and viral antigens, such as the Epstein Barr virus antigens EBVA and the human papillomavirus (HPV) antigens E6 and E7. Other large, protein-based antigens include TSP-180, MAGE-4, MAGE-5, MAGE-6, RAGE, NY-ESO, p185erbB2, p180erbB-3, c-met, nm-23H1, PSA, TAG-72, CA 19-9, CA 72-4, CAM 17.1, NuMa, K-ras, beta-Catenin, CDK4, Mum-1, p 15, p 16, 43-9F, 5T4, 791Tgp72, alpha-fetoprotein, beta-HCG, BCA225, BTAA, CA 125, CA 15-3\CA 27.29\BCAA, CA 195, CA 242, CA-50, CAM43, CD68\P1, CO-029, FGF-5, G250, Ga733\EpCAM, HTgp-175, M344, MA-50, MG7-Ag, MOV18, NB/70K, NY-CO-1, RCAS1, SDCCAG16, TA-90\Mac-2 binding protein\cyclophilin C-associated protein, TAAL6, TAG72, TLP, and TPS. In one embodiment, the invention provides an anti-siglec7 anti-FSHR NKCE. In one embodiment, the invention provides an anti-siglec7 anti-IL13Ra2 NKCE. Combination Vaccine In one embodiment, the invention relates to the administration of a NKCE of the invention, or nucleic acid molecule encoding the same, in combination with a PD- (L)1 axis inhibitor. The immunogenic composition can be used to increase the immune response against a tumor. In some embodiments, the NKCE of the invention, or nucleic acid molecule encoding the same, is administered simultaneously with administration of the PD-(L)1 axis inhibitory agent. In some embodiments, the NKCE of the invention, or nucleic acid molecule encoding the same, is administered prior to administration of the PD-(L)1 axis inhibitory agent. In some embodiments, the NKCE of the invention, or nucleic acid molecule encoding the same, is administered following administration of the PD-(L)1 axis inhibitory agent. In some embodiments, the NKCE of the invention, or nucleic acid molecule encoding the same, is administered about 1, 2, 5, 10, 30 or 60 minutes or several hours, such as about 2, 4, 6, 10, 12, 24 or 36 hours, or such as about 2, 4, 7, 14, 21, 28, 35, 42, 49, 56 days or more prior to administration of a PD-(L)1 axis inhibitory agent. Therefore, in some embodiments, a PD-(L)1 axis inhibitory agent is administered to a subject who has previously been administered a NKCE of the invention, or nucleic acid molecule encoding the same. In some embodiments, the NKCE of the invention, or nucleic acid molecule encoding the same, is administered about 1, 2, 5, 10, 30 or 60 minutes or several hours, such as about 2, 4, 6, 10, 12, 24 or 36 hours, or such as about 2, 4, 7, 14, 21, 28, 35, 42, 49, 56 days or more following administration of a PD-(L)1 axis inhibitory agent. Therefore, in some embodiments, a Siglec-7 antibody of the invention, or nucleic acid molecule encoding the same, is administered to a subject who has previously been administered a PD-(L)1 axis inhibitory agent. In some embodiments, the combination of the NKCE of the invention, or nucleic acid molecule encoding the same, and PD-(L)1 axis inhibitory agent is administered prior to administration of one or more additional anti-cancer agent. In some embodiments, the combination of the NKCE of the invention, or nucleic acid molecule encoding the same, and PD-(L)1 axis inhibitory agent is administered following administration of one or more additional anti-cancer agent. In some embodiments, the combination of the NKCE of the invention, or nucleic acid molecule encoding the same, and PD-(L)1 axis inhibitory agent is administered simultaneously with administration of one or more additional anti-cancer agent. The length of time between administrations of the NKCE of the invention, or nucleic acid molecule encoding the same, and the PD-(L)1 axis inhibitory agent or one or more additional anti-cancer agent may be a few minutes, such as about 1, 2, 5, 10, 30 or 60 minutes or several hours, such as about 2, 4, 6, 10, 12, 24 or 36 hours, or such as about 2, 4, 7, 14, 21, 28, 35, 42, 49, 56 days or more. One or more of the NKCE of the invention, or nucleic acid molecule encoding the same, the PD-(L)1 axis inhibitory agent or an additional anti-cancer agent may be administered in a pharmaceutically acceptable carrier. "Carrier" refers to a diluent, adjuvant, excipient, or vehicle with which the antibody of the invention is administered. Such vehicles may be liquids, such as water and oils, including those of petroleum, animal, vegetable or synthetic origin, such as peanut oil, soybean oil, mineral oil, sesame oil and the like. For example, 0.4% saline and 0.3% glycine may be used to formulate the bispecific anti-EGFR/c-Met antibody. These solutions are sterile and generally free of particulate matter. They may be sterilized by conventional, well-known sterilization techniques (e.g., filtration). For solid oral preparations, such as powders capsules and tablets, suitable carriers and additives include starches, sugars, diluents, granulating agents, lubricants, binders, disintegrating agents and the like. Solid oral preparations may also be coated with substances such as sugars or be enteric-coated to modulate major site of absorption. For parenteral administration, the carrier may comprise sterile water and other excipients may be added to increase solubility or preservation. Injectable suspensions or solutions may also be prepared utilizing aqueous carriers along with appropriate additives. Suitable vehicles and formulations, inclusive of other human proteins, e.g., human serum albumin, are described, for example, in e.g. Remington: The Science and Practice of Pharmacy, 21st Edition, Troy, D.B. ed., Lipincott Williams and Wilkins, Philadelphia, PA 2006, Part 5, Pharmaceutical Manufacturing pp 691-1092, See especially pp.958-989. The compositions may contain pharmaceutically acceptable auxiliary substances as required to approximate physiological conditions such as pH adjusting and buffering agents, stabilizing, thickening, lubricating and coloring agents, etc. The concentration of the NKCE of the invention, or nucleic acid molecule encoding the same, and the PD-(L)1 axis inhibitory agent in the pharmaceutical formulation may vary, from less than about 0.5%, usually to at least about 1% to as much as 15%, 20%, 30%, 40% or 50% by weight and may be selected primarily based on required dose, fluid volumes, viscosities, etc., according to the particular mode of administration selected. Pharmaceutical compositions comprising solid forms may contain about 0.1 mg to about 2000 mg, such as about 1 mg, about 5 mg, about 10 mg, about 25 mg, about 50 mg, about 100 mg, about 150 mg, about 200 mg, about 300 mg, about 500 mg about 600 mg or about 1000 mg of active ingredient. The therapeutic composition of the present invention can have features required of effective therapeutics such as being safe so the therapeutic composition itself does not cause illness or death; and provides ease of administration, few side effects, biological stability, and low cost per dose. PD-(L)1 axis Inhibitors In some embodiments, the invention provides a combination of a bispecific NKCE of the invention and a PD-(L)1 axis inhibitor. In various embodiments, the composition comprises an inhibitor of one or more gene or protein in the PD-(L)1 axis. In various embodiments, the present invention includes compositions and methods of decreasing the level or activity of one or more gene or protein in the PD-(L)1 axis. It will be understood by one skilled in the art, based upon the disclosure provided herein, that a decrease in the level or activity of one or more gene or protein in the PD-(L)1 axis encompasses the decrease in the expression of the biomarker, including transcription, translation, or both. The skilled artisan will also appreciate, once armed with the teachings of the present invention, that a decrease in the level or activity of one or more gene or protein in the PD-(L)1 axis includes a decrease in the amount of polypeptide, a decrease in the amount of mRNA, a decrease in transcription, a decrease in translation, or a combination thereof; and it also includes decreasing any activity of one or more gene or protein in the PD-(L)1 axis as well. Exemplary inhibitors of the PD-(L)1 axis include, but are not limited to, a small interfering RNA (siRNA), a microRNA, an antisense nucleic acid, a ribozyme, an expression vector encoding a transdominant negative mutant, an antibody, a fragment of an antibody, a fusion protein, an aptamer, a peptide and a small molecule. One skilled in the art will appreciate, based on the disclosure provided herein, that one way to decrease the mRNA and/or protein levels of one or more PD-(L)1 axis protein in a cell is by reducing or inhibiting expression of the nucleic acid encoding the PD-(L)1 axis protein. Thus, the protein level of a PD-(L)1 axis protein in a cell can be decreased using a molecule or compound that inhibits or reduces gene expression such as, for example, siRNA, an antisense molecule or a ribozyme. However, the invention should not be limited to these examples. In one embodiment, RNAi is used to decrease the level or activity of a PD-(L)1 axis protein. RNA interference (RNAi) is a phenomenon in which the introduction of double-stranded RNA (dsRNA) into a diverse range of organisms and cell types causes degradation of the complementary mRNA. In the cell, long dsRNAs are cleaved into short 21-25 nucleotide small interfering RNAs, or siRNAs, by a ribonuclease known as Dicer. The siRNAs subsequently assemble with protein components into an RNA-induced silencing complex (RISC), unwinding in the process. Activated RISC then binds to complementary transcript by base pairing interactions between the siRNA antisense strand and the mRNA. The bound mRNA is cleaved and sequence specific degradation of mRNA results in gene silencing. Chemical modification to siRNAs can aid in intravenous systemic delivery. Optimizing siRNAs involves consideration of overall G/C content, C/T content at the termini, Tm and the nucleotide content of the 3’ overhang. Therefore, the present invention also includes methods of decreasing levels of one or more PD-(L)1 axis protein using RNAi technology. In some embodiments, the invention includes an isolated nucleic acid encoding an inhibitor, such as a protein, an antibody, an siRNA or an antisense molecule operably linked to a nucleic acid comprising a promoter/regulatory sequence such that the nucleic acid is preferably capable of directing expression of the inhibitor encoded by the nucleic acid. Thus, the invention encompasses expression vectors and methods for the introduction of exogenous DNA into cells with concomitant expression of the exogenous DNA in the cells. In order to assess the expression of the inhibitor, the expression vector to be introduced into a cell can also contain either a selectable marker gene or a reporter gene or both to facilitate identification and selection of expressing cells from the population of cells sought to be transfected or infected through viral vectors. In other embodiments, the selectable marker may be carried on a separate piece of DNA and used in a co-transfection procedure. Both selectable markers and reporter genes may be flanked with appropriate regulatory sequences to enable expression in the host cells. Useful selectable markers are known in the art and include, for example, antibiotic- resistance genes, such as neomycin When the inhibitor of the invention is a small molecule, a small molecule antagonist may be obtained using standard methods known to the skilled artisan. Such methods include chemical organic synthesis or biological means. Biological means include purification from a biological source, recombinant synthesis and in vitro translation systems, using methods well known in the art. Combinatorial libraries of molecularly diverse chemical compounds potentially useful in treating a variety of diseases and conditions are well known in the art as are method of making the libraries. The method may use a variety of techniques well- known to the skilled artisan including solid phase synthesis, solution methods, parallel synthesis of single compounds, synthesis of chemical mixtures, rigid core structures, flexible linear sequences, deconvolution strategies, tagging techniques, and generating unbiased molecular landscapes for lead discovery vs. biased structures for lead development. In a general method for small library synthesis, an activated core molecule is condensed with a number of building blocks, resulting in a combinatorial library of covalently linked, core–building block ensembles. The shape and rigidity of the core determines the orientation of the building blocks in shape space. The libraries can be biased by changing the core, linkage, or building blocks to target a characterized biological structure (“focused libraries”) or synthesized with less structural bias using flexible cores. In another aspect of the invention, one or more protein in the PD-(L)1 axis can be inhibited by way of inactivating and/or sequestering the protein(s). As such, inhibiting the effects of one or more protein in the PD-(L)1 axis can be accomplished by using a transdominant negative mutant. In one embodiment, an antibody specific for one or more protein in the PD-(L)1 axis may be used. As will be understood by one skilled in the art, any antibody that can recognize and bind to an antigen of interest is useful in the present invention. Methods of making and using antibodies are well known in the art. For example, polyclonal antibodies useful in the present invention are generated by immunizing rabbits according to standard immunological techniques well-known in the art. Such techniques include immunizing an animal with a chimeric protein comprising a portion of another protein such as a maltose binding protein or glutathione (GSH) tag polypeptide portion, and/or a moiety such that the antigenic protein of interest is rendered immunogenic (e.g., an antigen of interest conjugated with keyhole limpet hemocyanin, KLH) and a portion comprising the respective antigenic protein amino acid residues. The chimeric proteins are produced by cloning the appropriate nucleic acids encoding the marker protein into a plasmid vector suitable for this purpose, such as but not limited to, pMAL-2 or pCMX. Exemplary anti-PD-(L)1 axis antibodies include, but are not limited to, nivolumab (OPDIVO®), pembrolimumab (KEYTRUDA®), sintilimab, cemiplimab (LIBTAYO®), tripolibamab, tislelizumab, spartalizumab, camrelizumab, dostralimab, genolimzumab or cetrelimab, or antibodies that bind PD-L1, such as PD-L1 antibodies are envafolimab, atezolizumab (TECENTRIQ®), durvalumab (IMFINZI®), avelumab (BAVENCIO®), REGN2810, pidilizumab, MEDI0680, PDR001, PF-06801591, BGB- A317, TSR-042, and SHR-1210. Methods of Delivery of the Composition The present invention also relates to a method of delivering the composition to the subject in need thereof. The method of delivery can include, administering the composition to the subject. In some embodiments, the present invention relates to administration of a NKCE of the invention, or a fragment thereof, or a nucleic acid molecule encoding the same. In some embodiments, the nucleic acid molecule is a DNA molecule. In some embodiments, the nucleic acid molecule is an RNA molecule. In some embodiments, the nucleic acid molecule is an mRNA molecule. Administration can include, but is not limited to, intravenous delivery of an antibody, DNA injection, liposome mediated delivery, and nanoparticle facilitated delivery. The mammal receiving delivery of the composition may be human, primate, non-human primate, cow, cattle, sheep, goat, antelope, bison, water buffalo, bison, bovids, deer, hedgehogs, elephants, llama, alpaca, mice, rats, and chicken. The composition may be administered by different routes including orally, parenterally, sublingually, transdermally, rectally, transmucosally, topically, via inhalation, via buccal administration, intrapleurally, intravenous, intraarterial, intraperitoneal, subcutaneous, intramuscular, intranasal, intranasal, intrathecal, and intraarticular or combinations thereof. For veterinary use, the composition may be administered as a suitably acceptable formulation in accordance with normal veterinary practice. The veterinarian can readily determine the dosing regimen and route of administration that is most appropriate for a particular animal. Treatment Methods In one embodiment, the invention provides a method for treatment or prevention of a disease or disorder which would benefit from an increase in NK cell function or activity. Exemplary diseases and disorders that can be treated using the compositions and methods of the invention include, but are not limited to cancer and infectious diseases. The following are non-limiting examples of cancers that can be diagnosed or treated by the disclosed methods and compositions: acute lymphoblastic leukemia, acute myeloid leukemia, adrenocortical carcinoma, appendix cancer, basal cell carcinoma, bile duct cancer, bladder cancer, bone cancer, brain and spinal cord tumors, brain stem glioma, brain tumor, breast cancer, bronchial tumors, burkitt lymphoma, carcinoid tumor, central nervous system atypical teratoid/rhabdoid tumor, central nervous system embryonal tumors, central nervous system lymphoma, cerebellar astrocytoma, cerebral astrocytoma/malignant glioma, cerebral astrocytotna/malignant glioma, cervical cancer, childhood visual pathway tumor, chordoma, chronic lymphocytic leukemia, chronic myelogenous leukemia, chronic myeloproliferative disorders, colon cancer, colorectal cancer, craniopharyngioma, cutaneous cancer, cutaneous t-cell lymphoma, endometrial cancer, ependymoblastoma, ependymoma, esophageal cancer, ewing family of tumors, extracranial cancer, extragonadal germ cell tumor, extrahepatic bile duct cancer, extrahepatic cancer, eye cancer, fungoides, gallbladder cancer, gastric (stomach) cancer, gastrointestinal cancer, gastrointestinal carcinoid tumor, gastrointestinal stromal tumor (gist), germ cell tumor, gestational cancer, gestational trophoblastic tumor, glioblastoma, glioma, hairy cell leukemia, head and neck cancer, hepatocellular (liver) cancer, histiocytosis, hodgkin lymphoma, hypopharyngeal cancer, hypothalamic and visual pathway glioma, hypothalamic tumor, intraocular (eye) cancer, intraocular melanoma, islet cell tumors, kaposi sarcoma, kidney (renal cell) cancer, langerhans cell cancer, langerhans cell histiocytosis, laryngeal cancer, leukemia, lip and oral cavity cancer, liver cancer, lung cancer, lymphoma, macroglobulinemia, malignant fibrous histiocvtoma of bone and osteosarcoma, medulloblastoma, medulloepithelioma, melanoma, merkel cell carcinoma, mesothelioma, metastatic squamous neck cancer with occult primary, mouth cancer, multiple endocrine neoplasia syndrome, multiple myeloma, mycosis, myelodysplastic syndromes, myelodysplastic/myeloproliferative diseases, myelogenous leukemia, myeloid leukemia, myeloma, myeloproliferative disorders, nasal cavity and paranasal sinus cancer, nasopharyngeal cancer, neuroblastoma, non-hodgkin lymphoma, non-small cell lung cancer, oral cancer, oral cavity cancer, oropharyngeal cancer, osteosarcoma and malignant fibrous histiocytoma, osteosarcoma and malignant fibrous histiocytoma of bone, ovarian, ovarian cancer, ovarian epithelial cancer, ovarian germ cell tumor, ovarian low malignant potential tumor, pancreatic cancer, papillomatosis, paraganglioma, parathyroid cancer, penile cancer, pharyngeal cancer, pheochromocytoma, pineal parenchymal tumors of intermediate differentiation, pineoblastoma and supratentorial primitive neuroectodermal tumors, pituitary tumor, plasma cell neoplasm, plasma cell neoplasm/multiple myeloma, pleuropulmonary blastoma, primary central nervous system cancer, primary central nervous system lymphoma, prostate cancer, rectal cancer, renal cell (kidney) cancer, renal pelvis and ureter cancer, respiratory tract carcinoma involving the nut gene on chromosome 15, retinoblastoma, rhabdomyosarcoma, salivary gland cancer, sarcoma, sezary syndrome, skin cancer (melanoma), skin cancer (nonmelanoma), skin carcinoma, small cell lung cancer, small intestine cancer, soft tissue cancer, soft tissue sarcoma, squamous cell carcinoma, squamous neck cancer , stomach (gastric) cancer, supratentorial primitive neuroectodermal tumors, supratentorial primitive neuroectodermal tumors and pineoblastoma, T-cell lymphoma, testicular cancer, throat cancer, thymoma and thymic carcinoma, thyroid cancer, transitional cell cancer, transitional cell cancer of the renal pelvis and ureter, trophoblastic tumor, urethral cancer, uterine cancer, uterine sarcoma, vaginal cancer, visual pathway and hypothalamic glioma, vulvar cancer, waldenstrom macroglobulinemia, and wilms tumor. In one embodiment, the compositions are used to treat cancers having a high level of sialic acid. Cancers associated with high levels of sialic acid include, but are not limited to, ovarian cancer, melanoma, renal cell carcinoma, prostate cancer, colon cancer, breast cancer, head and neck squamous cell carcinoma, and oral cancer. Cancer Therapy In one embodiment, the invention provides methods of treating or preventing cancer, or of treating and preventing growth or metastasis of tumors. Related aspects, illustrated of the invention provide methods of preventing, aiding in the prevention, and/or reducing metastasis of hyperplastic or tumor cells in an individual. In one embodiment, the compositions are used to treat cancers having a high level of sialic acid, including, but not limited to, ovarian cancer, melanoma, renal cell carcinoma, prostate cancer, colon cancer, breast cancer, head and neck squamous cell carcinoma, skin cancer and oral cancer. One aspect of the invention provides a method of inhibiting metastasis in an individual in need thereof, the method comprising administering to the individual an effective amount of a nucleic acid molecule encoding a multivalent antibody of the invention, wherein the multivalent antibody is specific for the cancer to be treated. The invention further provides a method of inhibiting metastasis in an individual in need thereof, the method comprising administering to the individual an effective metastasis- inhibiting amount of a nucleic acid molecule encoding a multivalent antibody of the invention, wherein the multivalent antibody is specific for the cancer to be treated. In some embodiments of treating or preventing cancer, or of treating and preventing metastasis of tumors in an individual in need thereof, a second agent is administered to the individual, such as an antineoplastic agent. In some embodiments, the second agent comprises a second metastasis-inhibiting agent, such as a plasminogen antagonist, or an adenosine deaminase antagonist. In other embodiments, the second agent is an angiogenesis inhibiting agent. The compositions of the invention can be used to prevent, abate, minimize, control, and/or lessen cancer in humans and animals. The compositions of the invention can also be used to slow the rate of primary tumor growth. The compositions of the invention when administered to a subject in need of treatment can be used to stop the spread of cancer cells. As such, an effective amount of a nucleic acid molecule encoding a multivalent antibody of the invention, wherein the multivalent antibody is specific for the cancer to be treated can be administered as part of a combination therapy with one or more drugs or other pharmaceutical agents. When used as part of the combination therapy, the decrease in metastasis and reduction in primary tumor growth afforded by the compositions of the invention allows for a more effective and efficient use of any pharmaceutical or drug therapy being used to treat the patient. In addition, control of metastasis by the compositions of the invention affords the subject a greater ability to concentrate the disease in one location. In one embodiment, the invention provides a method to treat cancer metastasis comprising treating the subject prior to, concurrently with, or subsequently to the treatment with a composition of the invention, with a complementary therapy for the cancer, such as surgery, chemotherapy, chemotherapeutic agent, radiation therapy, or hormonal therapy or a combination thereof. Chemotherapeutic agents include cytotoxic agents (e.g., 5-fluorouracil, cisplatin, carboplatin, methotrexate, daunorubicin, doxorubicin, vincristine, vinblastine, oxorubicin, carmustine (BCNU), lomustine (CCNU), cytarabine USP, cyclophosphamide, estramucine phosphate sodium, altretamine, hydroxyurea, ifosfamide, procarbazine, mitomycin, busulfan, cyclophosphamide, mitoxantrone, carboplatin, cisplatin, interferon alfa-2a recombinant, paclitaxel, teniposide, and streptozoci), cytotoxic alkylating agents (e.g., busulfan, chlorambucil, cyclophosphamide, melphalan, or ethylesulfonic acid), alkylating agents (e.g., asaley, AZQ, BCNU, busulfan, bisulphan, carboxyphthalatoplatinum, CBDCA, CCNU, CHIP, chlorambucil, chlorozotocin, cis- platinum, clomesone, cyanomorpholinodoxorubicin, cyclodisone, cyclophosphamide, dianhydrogalactitol, fluorodopan, hepsulfam, hycanthone, iphosphamide, melphalan, methyl CCNU, mitomycin C, mitozolamide, nitrogen mustard, PCNU, piperazine, piperazinedione, pipobroman, porfiromycin, spirohydantoin mustard, streptozotocin, teroxirone, tetraplatin, thiotepa, triethylenemelamine, uracil nitrogen mustard, and Yoshi- 864), antimitotic agents (e.g., allocolchicine, Halichondrin M, colchicine, colchicine derivatives, dolastatin 10, maytansine, rhizoxin, paclitaxel derivatives, paclitaxel, thiocolchicine, trityl cysteine, vinblastine sulfate, and vincristine sulfate), plant alkaloids (e.g., actinomycin D, bleomycin, L-asparaginase, idarubicin, vinblastine sulfate, vincristine sulfate, mitramycin, mitomycin, daunorubicin, VP-16-213, VM-26, navelbine and taxotere), biologicals (e.g., alpha interferon, BCG, G-CSF, GM-CSF, and interleukin- 2), topoisomerase I inhibitors (e.g., camptothecin, camptothecin derivatives, and morpholinodoxorubicin), topoisomerase II inhibitors (e.g., mitoxantron, amonafide, m- AMSA, anthrapyrazole derivatives, pyrazoloacridine, bisantrene HCL, daunorubicin, deoxydoxorubicin, menogaril, N,N-dibenzyl daunomycin, oxanthrazole, rubidazone, VM-26 and VP-16), and synthetics (e.g., hydroxyurea, procarbazine, o,p'-DDD, dacarbazine, CCNU, BCNU, cis-diamminedichloroplatimun, mitoxantrone, CBDCA, levamisole, hexamethylmelamine, all-trans retinoic acid, gliadel and porfimer sodium). Antiproliferative agents are compounds that decrease the proliferation of cells. Antiproliferative agents include alkylating agents, antimetabolites, enzymes, biological response modifiers, miscellaneous agents, hormones and antagonists, androgen inhibitors (e.g., flutamide and leuprolide acetate), antiestrogens (e.g., tamoxifen citrate and analogs thereof, toremifene, droloxifene and roloxifene), Additional examples of specific antiproliferative agents include, but are not limited to levamisole, gallium nitrate, granisetron, sargramostim strontium-89 chloride, filgrastim, pilocarpine, dexrazoxane, and ondansetron. The compounds of the invention can be administered alone or in combination with other anti-tumor agents, including cytotoxic/antineoplastic agents and anti-angiogenic agents. Cytotoxic/anti-neoplastic agents are defined as agents which attack and kill cancer cells. Some cytotoxic/anti-neoplastic agents are alkylating agents, which alkylate the genetic material in tumor cells, e.g., cis-platin, cyclophosphamide, nitrogen mustard, trimethylene thiophosphoramide, carmustine, busulfan, chlorambucil, belustine, uracil mustard, chlomaphazin, and dacabazine. Other cytotoxic/anti-neoplastic agents are antimetabolites for tumor cells, e.g., cytosine arabinoside, fluorouracil, methotrexate, mercaptopuirine, azathioprime, and procarbazine. Other cytotoxic/anti- neoplastic agents are antibiotics, e.g., doxorubicin, bleomycin, dactinomycin, daunorubicin, mithramycin, mitomycin, mytomycin C, and daunomycin. There are numerous liposomal formulations commercially available for these compounds. Still other cytotoxic/anti-neoplastic agents are mitotic inhibitors (vinca alkaloids). These include vincristine, vinblastine and etoposide. Miscellaneous cytotoxic/anti-neoplastic agents include taxol and its derivatives, L-asparaginase, anti-tumor antibodies, dacarbazine, azacytidine, amsacrine, melphalan, VM-26, ifosfamide, mitoxantrone, and vindesine. Anti-angiogenic agents are well known to those of skill in the art. Suitable anti-angiogenic agents for use in the methods and compositions of the invention include anti-VEGF antibodies, including humanized and chimeric antibodies, anti-VEGF aptamers and antisense oligonucleotides. Other known inhibitors of angiogenesis include angiostatin, endostatin, interferons, interleukin 1 (including alpha and beta) interleukin 12, retinoic acid, and tissue inhibitors of metalloproteinase-1 and -2. (TIMP-1 and -2). Small molecules, including topoisomerases such as razoxane, a topoisomerase II inhibitor with anti-angiogenic activity, can also be used. Other anti-cancer agents that can be used in combination with the compositions of the invention include, but are not limited to: acivicin; aclarubicin; acodazole hydrochloride; acronine; adozelesin; aldesleukin; altretamine; ambomycin; ametantrone acetate; aminoglutethimide; amsacrine; anastrozole; anthramycin; asparaginase; asperlin; azacitidine; azetepa; azotomycin; batimastat; benzodepa; bicalutamide; bisantrene hydrochloride; bisnafide dimesylate; bizelesin; bleomycin sulfate; brequinar sodium; bropirimine; busulfan; cactinomycin; calusterone; caracemide; carbetimer; carboplatin; carmustine; carubicin hydrochloride; carzelesin; cedefingol; chlorambucil; cirolemycin; cisplatin; cladribine; crisnatol mesylate; cyclophosphamide; cytarabine; dacarbazine; dactinomycin; daunorubicin hydrochloride; decitabine; dexormaplatin; dezaguanine; dezaguanine mesylate; diaziquone; docetaxel; doxorubicin; doxorubicin hydrochloride; droloxifene; droloxifene citrate; dromostanolone propionate; duazomycin; edatrexate; eflornithine hydrochloride; elsamitrucin; enloplatin; enpromate; epipropidine; epirubicin hydrochloride; erbulozole; esorubicin hydrochloride; estramustine; estramustine phosphate sodium; etanidazole; etoposide; etoposide phosphate; etoprine; fadrozole hydrochloride; fazarabine; fenretinide; floxuridine; fludarabine phosphate; fluorouracil; fluorocitabine; fosquidone; fostriecin sodium; gemcitabine; gemcitabine hydrochloride; hydroxyurea; idarubicin hydrochloride; ifosfamide; ilmofosine; interleukin II (including recombinant interleukin II, or rIL2), interferon alfa-2a; interferon alfa-2b; interferon alfa-n1; interferon alfa-n3; interferon beta-I a; interferon gamma-I b; iproplatin; irinotecan hydrochloride; lanreotide acetate; letrozole; leuprolide acetate; liarozole hydrochloride; lometrexol sodium; lomustine; losoxantrone hydrochloride; masoprocol; maytansine; mechlorethamine hydrochloride; megestrol acetate; melengestrol acetate; melphalan; menogaril; mercaptopurine; methotrexate; methotrexate sodium; metoprine; meturedepa; mitindomide; mitocarcin; mitocromin; mitogillin; mitomalcin; mitomycin; mitosper; mitotane; mitoxantrone hydrochloride; mycophenolic acid; nocodazole; nogalamycin; ormaplatin; oxisuran; paclitaxel; pegaspargase; peliomycin; pentamustine; peplomycin sulfate; perfosfamide; pipobroman; piposulfan; piroxantrone hydrochloride; plicamycin; plomestane; porfimer sodium; porfiromycin; prednimustine; procarbazine hydrochloride; puromycin; puromycin hydrochloride; pyrazofurin; riboprine; rogletimide; safingol; safingol hydrochloride; semustine; simtrazene; sparfosate sodium; sparsomycin; spirogermanium hydrochloride; spiromustine; spiroplatin; streptonigrin; streptozocin; sulofenur; talisomycin; tecogalan sodium; tegafur; teloxantrone hydrochloride; temoporfin; teniposide; teroxirone; testolactone; thiamiprine; thioguanine; thiotepa; tiazofurin; tirapazamine; toremifene citrate; trestolone acetate; triciribine phosphate; trimetrexate; trimetrexate glucuronate; triptorelin; tubulozole hydrochloride; uracil mustard; uredepa; vapreotide; verteporfin; vinblastine sulfate; vincristine sulfate; vindesine; vindesine sulfate; vinepidine sulfate; vinglycinate sulfate; vinleurosine sulfate; vinorelbine tartrate; vinrosidine sulfate; vinzolidine sulfate; vorozole; zeniplatin; zinostatin; zorubicin hydrochloride. Other anti-cancer drugs include, but are not limited to: 20-epi-1,25 dihydroxyvitamin D3; 5-ethynyluracil; abiraterone; aclarubicin; acylfulvene; adecypenol; adozelesin; aldesleukin; ALL-TK antagonists; altretamine; ambamustine; amidox; amifostine; aminolevulinic acid; amrubicin; amsacrine; anagrelide; anastrozole; andrographolide; angiogenesis inhibitors; antagonist D; antagonist G; antarelix; anti- dorsalizing morphogenetic protein-1; antiandrogen, prostatic carcinoma; antiestrogen; antineoplaston; antisense oligonucleotides; aphidicolin glycinate; apoptosis gene modulators; apoptosis regulators; apurinic acid; ara-CDP-DL-PTBA; arginine deaminase; asulacrine; atamestane; atrimustine; axinastatin 1; axinastatin 2; axinastatin 3; azasetron; azatoxin; azatyrosine; baccatin III derivatives; balanol; batimastat; BCR/ABL antagonists; benzochlorins; benzoylstaurosporine; beta lactam derivatives; beta-alethine; betaclamycin B; betulinic acid; bFGF inhibitor; bicalutamide; bisantrene; bisaziridinylspermine; bisnafide; bistratene A; bizelesin; breflate; bropirimine; budotitane; buthionine sulfoximine; calcipotriol; calphostin C; camptothecin derivatives; canarypox IL-2; capecitabine; carboxamide-amino-triazole; carboxyamidotriazole; CaRest M3; CARN 700; cartilage derived inhibitor; carzelesin; casein kinase inhibitors (ICOS); castanospermine; cecropin B; cetrorelix; chlorins; chloroquinoxaline sulfonamide; cicaprost; cis-porphyrin; cladribine; clomifene analogues; clotrimazole; collismycin A; collismycin B; combretastatin A4; combretastatin analogue; conagenin; crambescidin 816; crisnatol; cryptophycin 8; cryptophycin A derivatives; curacin A; cyclopentanthraquinones; cycloplatam; cypemycin; cytarabine ocfosfate; cytolytic factor; cytostatin; dacliximab; decitabine; dehydrodidemnin B; deslorelin; dexamethasone; dexifosfamide; dexrazoxane; dexverapamil; diaziquone; didemnin B; didox; diethylnorspermine; dihydro-5-azacytidine; dihydrotaxol, 9-; dioxamycin; diphenyl spiromustine; docetaxel; docosanol; dolasetron; doxifluridine; droloxifene; dronabinol; duocarmycin SA; ebselen; ecomustine; edelfosine; edrecolomab; eflornithine; elemene; emitefur; epirubicin; epristeride; estramustine analogue; estrogen agonists; estrogen antagonists; etanidazole; etoposide phosphate; exemestane; fadrozole; fazarabine; fenretinide; filgrastim; finasteride; flavopiridol; flezelastine; fluasterone; fludarabine; fluorodaunorunicin hydrochloride; forfenimex; formestane; fostriecin; fotemustine; gadolinium texaphyrin; gallium nitrate; galocitabine; ganirelix; gelatinase inhibitors; gemcitabine; glutathione inhibitors; hepsulfam; heregulin; hexamethylene bisacetamide; hypericin; ibandronic acid; idarubicin; idoxifene; idramantone; ilmofosine; ilomastat; imidazoacridones; imiquimod; immunostimulant peptides; insulin-like growth factor-1 receptor inhibitor; interferon agonists; interferons; interleukins; iobenguane; iododoxorubicin; ipomeanol, 4-; iroplact; irsogladine; isobengazole; isohomohalicondrin B; itasetron; jasplakinolide; kahalalide F; lamellarin-N triacetate; lanreotide; leinamycin; lenograstim; lentinan sulfate; leptolstatin; letrozole; leukemia inhibiting factor; leukocyte alpha interferon; leuprolide+estrogen+progesterone; leuprorelin; levamisole; liarozole; linear polyamine analogue; lipophilic disaccharide peptide; lipophilic platinum compounds; lissoclinamide 7; lobaplatin; lombricine; lometrexol; lonidamine; losoxantrone; lovastatin; loxoribine; lurtotecan; lutetium texaphyrin; lysofylline; lytic peptides; maitansine; mannostatin A; marimastat; masoprocol; maspin; matrilysin inhibitors; matrix metalloproteinase inhibitors; menogaril; merbarone; meterelin; methioninase; metoclopramide; MIF inhibitor; mifepristone; miltefosine; mirimostim; mismatched double stranded RNA; mitoguazone; mitolactol; mitomycin analogues; mitonafide; mitotoxin fibroblast growth factor-saporin; mitoxantrone; mofarotene; molgramostim; monoclonal antibody, human chorionic gonadotrophin; monophosphoryl lipid A+myobacterium cell wall sk; mopidamol; multiple drug resistance gene inhibitor; multiple tumor suppressor 1-based therapy; mustard anticancer agent; mycaperoxide B; mycobacterial cell wall extract; myriaporone; N-acetyldinaline; N-substituted benzamides; nafarelin; nagrestip; naloxone+pentazocine; napavin; naphterpin; nartograstim; nedaplatin; nemorubicin; neridronic acid; neutral endopeptidase; nilutamide; nisamycin; nitric oxide modulators; nitroxide antioxidant; nitrullyn; O6- benzylguanine; octreotide; okicenone; oligonucleotides; onapristone; ondansetron; ondansetron; oracin; oral cytokine inducer; ormaplatin; osaterone; oxaliplatin; oxaunomycin; paclitaxel; paclitaxel analogues; paclitaxel derivatives; palauamine; palmitoylrhizoxin; pamidronic acid; panaxytriol; panomifene; parabactin; pazelliptine; pegaspargase; peldesine; pentosan polysulfate sodium; pentostatin; pentrozole; perflubron; perfosfamide; perillyl alcohol; phenazinomycin; phenylacetate; phosphatase inhibitors; picibanil; pilocarpine hydrochloride; pirarubicin; piritrexim; placetin A; placetin B; plasminogen activator inhibitor; platinum complex; platinum compounds; platinum-triamine complex; porfimer sodium; porfiromycin; prednisone; propyl bis- acridone; prostaglandin J2; proteasome inhibitors; protein A-based immune modulator; protein kinase C inhibitor; protein kinase C inhibitors, microalgal; protein tyrosine phosphatase inhibitors; purine nucleoside phosphorylase inhibitors; purpurins; pyrazoloacridine; pyridoxylated hemoglobin polyoxyethylene conjugate; raf antagonists; raltitrexed; ramosetron; ras farnesyl protein transferase inhibitors; ras inhibitors; ras-GAP inhibitor; retelliptine demethylated; rhenium Re 186 etidronate; rhizoxin; ribozymes; RII retinamide; rogletimide; rohitukine; romurtide; roquinimex; rubiginone B1; ruboxyl; safingol; saintopin; SarCNU; sarcophytol A; sargramostim; Sdi 1 mimetics; semustine; senescence derived inhibitor 1; sense oligonucleotides; signal transduction inhibitors; signal transduction modulators; single chain antigen binding protein; sizofuran; sobuzoxane; sodium borocaptate; sodium phenylacetate; solverol; somatomedin binding protein; sonermin; sparfosic acid; spicamycin D; spiromustine; splenopentin; spongistatin 1; squalamine; stem cell inhibitor; stem-cell division inhibitors; stipiamide; stromelysin inhibitors; sulfinosine; superactive vasoactive intestinal peptide antagonist; suradista; suramin; swainsonine; synthetic glycosaminoglycans; tallimustine; tamoxifen methiodide; tauromustine; tazarotene; tecogalan sodium; tegafur; tellurapyrylium; telomerase inhibitors; temoporfin; temozolomide; teniposide; tetrachlorodecaoxide; tetrazomine; thaliblastine; thiocoraline; thrombopoietin; thrombopoietin mimetic; thymalfasin; thymopoietin receptor agonist; thymotrinan; thyroid stimulating hormone; tin ethyl etiopurpurin; tirapazamine; titanocene bichloride; topsentin; toremifene; totipotent stem cell factor; translation inhibitors; tretinoin; triacetyluridine; triciribine; trimetrexate; triptorelin; tropisetron; turosteride; tyrosine kinase inhibitors; tyrphostins; UBC inhibitors; ubenimex; urogenital sinus-derived growth inhibitory factor; urokinase receptor antagonists; vapreotide; variolin B; vector system, erythrocyte gene therapy; velaresol; veramine; verdins; verteporfin; vinorelbine; vinxaltine; vitaxin; vorozole; zanoterone; zeniplatin; zilascorb; and zinostatin stimalamer. In one embodiment, the anti- cancer drug is 5-fluorouracil, taxol, or leucovorin. The present invention is further illustrated in the following Examples. It should be understood that these Examples, while indicating exemplary embodiments of the invention, are given by way of illustration only. From the above discussion and these Examples, one skilled in the art can ascertain the essential characteristics of this invention, and without departing from the spirit and scope thereof, can make various changes and modifications of the invention to adapt it to various usages and conditions. Thus, various modifications of the invention in addition to those shown and described herein will be apparent to those skilled in the art from the foregoing description. Such modifications are also intended to fall within the scope of the appended claims. EXPERIMENTAL EXAMPLES The invention is further described in detail by reference to the following experimental examples. These examples are provided for purposes of illustration only and are not intended to be limiting unless otherwise specified. Thus, the invention should in no way be construed as being limited to the following examples, but rather, should be construed to encompass any and all variations which become evident as a result of the teaching provided herein. Without further description, it is believed that one of ordinary skill in the art can, using the preceding description and the following illustrative examples, make and utilize the present invention and practice the claimed methods. The following working examples therefore are not to be construed as limiting in any way the remainder of the disclosure. Example 1: Immunotherapy of Ovarian Cancer Targeting FSHR through Innate and Adaptive Immunity Monoclonal antibodies against FSHR were developed and experiments were designed to focus on the most potent of these reagents. Anti-FSHR antibody bound to multiple FSHR expressing ovarian serous and clear cell adenocarcinoma cells, establishing its specificity. Experiments were designed to utilize this as a tool to develop a bispecific T cell engager targeting FSHR (DDAP TCE) and evaluated this bispecific in therapeutic models for the treatment of ovarian cancer (OC). DDAP TCE in the presence of human PBMCs was highly specific for killing FSHR positive ovarian tumor lines. It is believed that engaging the innate components of the immune system could provide potentially enhanced tumor control. As increasing lines of evidence suggest that OC is receptive to natural killer (NK) cell attack, accordingly antibodies were developed against human Siglec 7, an inhibitory receptor present on human NK cells and demonstrated their binding to NK cells. Experiments were designed to use these to create a novel class of bispecific NK cell engager (NKCE) that simultaneously target both Siglec 7 and FSHR (DDAP NKCE). This NKCE was robust in killing FSHR positive OC targets in the in vitro and in vivo assays. These studies demonstrate for the first time the utility of targeting FSHR for a major subset of OC, that bispecific tools focused on FSHR and CD3 are highly immune potent, in vivo impact by Siglec7 antibodies against OC or human tumors and a new target for NK cell activation by bispecific engagers for a diverse population of OC. Combination studies to engage both T cells and NK cells appear of interest as new tools for therapy of OC. The methods and materials are now described. Cell lines and animals ID8-Defb29/Vegf-a-Fshr, ID8-Defb29/Vegf-a, OVCAR3, CaOV3, TOV- 21G and SKOV3 cells were provided by J.R. Conejo-Garcia (Department of Immunology, Moffitt Cancer Center, Tampa, Florida). OVISE, OVCAR8, OVCAR10, PEO-4 and Kuramochi cells were provided by R. Zhang (The Wistar Institute). HaCaT human keratinocyte cells were provided by M. Herlyn (The Wistar Institute). Human embryonic kidney 293T, Expi293F and murine myeloma cell line Sp2.0/0 were obtained from ATCC.293T cells were transduced retrovirally to express Siglec 7. OVCAR3 and Kuramochi cells were retrovirally transduced with human FSHR to express FSHR as described previously (Perales-Puchalt et al., 2019, JCI Insight 4). K562 and A20 were also purchased from ATCC and retrovirally transduced to express human and murine FSHR respectively. The expression vector pBMN-I-GFP (from Nolan Lab) was purchased from Addgene. Transgenic H2L2 mice were obtained from Harbor Biomed. Balb/c mice were purchased from The Jackson Laboratory. NSG mice were purchased from The Wistar Institute Animal Facility. Mouse immunization, Hybridoma generation, and DNA-encoded mAb generation Human FSHR (Uniprot P23945) was RNA and codon optimized for expression in mouse and cloned into a modified pVax1 vector (Genscript). For the generation of FSHR hybridomas, Balb/c mice were immunized by injecting 25µg of DNA resuspended in 30µl of water into the tibialis anterior muscle followed by electroporation with the CELLECTRA device (Inovio Pharmaceuticals). The murine myeloma cell line Sp2.0/0 was fused with spleen cells using 50% polyethylene glycol 1500 (Roche) to generate hybridomas. Several humanized antibodies against human Siglec 7 were generated in H2L2 mice. These mAbs bound to Siglec 7 and could stain NK cells. These hybridomas were sequenced and used to develop Siglec 7 DNA encoded monoclonal antibodies (DMAbs) as tools for in vitro expression (Patel et al., 2018, Cell Rep 25: 1982-93 e4). Final human IgG1 HC and LC were inserted into a pVax1 plasmid expression vector, under the control of the human cytomegalovirus (hCMV) promoter and bovine growth hormone (BGH) polyA signal as described (Patel et al., 2018, Cell Rep 25: 1982-93 e4). Plasmids were then transfected into Expi293F cells using the Expifectamine 293 Expression Kit (Thermo Fisher Scientific) to produce recombinant antibodies. The purity and apparent molecular weight of the recombinant antibodies were assessed by SDS- PAGE analysis. Design of FSHRxCD3 TCE and FSHRx Siglec 7 NKCE Experiments were set up to design FSHRxCD3 DNA encoded bispecific T cell engager (TCE) by encoding a codon-optimized scFv of FSHR MAb (DDAP) followed by the scFv of a modified UCHT1 anti–human CD3 antibody with the addition of an IgE leader sequence. FSHRxSiglec 7 Natural Killer cell engager (NKCE) was designed by encoding a codon-optimized scFv of Siglec 7 MAb (DB-S7-2) followed by the scFv of FSHR antibody (DDAP) with the addition of an enhancing optimized IgE leader sequence. Both constructs were subcloned into a modified pVax1 expression vector (Perales-Puchalt et al., 2019, Mol Ther 27: 314-25). FSHRxCD3 TCE and FSHRxSiglec7 NKCE are designated as DDAP-TCE and DDAP-NKCE respectively, hereafter. Flow cytometry BD LSRII flow cytometer was used for staining of cells. BD FACS Aria cell sorter (BD Biosciences) was used for the sorting of Siglec 7/FSHR stably expressing cells. Anti-human antibodies used were directly fluorochrome conjugated. The following was used: anti-Siglec7 (F023-420, BD Pharmingen), anti-Siglec 3 (6C5/2, R&D Systems), anti-Siglec 9 (K8, Biolegend). For the non-conjugated primary antibodies, PE- secondary anti-human (H+L) (Invitrogen), PE/AF647- secondary anti-human F(ab’) ₂ (Jackson ImmunoResearch Laboratories Inc) and APC- secondary anti-mouse IgG (Poly4053, BioLegend) were used. Live/Dead Violet viability kit (Invitrogen) was used to exclude dead cells from analysis. Enzyme-linked immunosorbent assay (ELISA) For isotyping DDAP, the ELISA plates were coated with DDAP in PBS overnight. Following, the plate was blocked and added the following HRP conjugated antibodies: anti-mouse IgA, anti-mouse IgM, anti-mouse IgG1, anti-mouse IgG2a, anti- mouse IgG2b, anti-mouse IgG3, anti-mouse kappa light chain (all from Bethyl). For quantification of human IgGs in Siglec 7 DMAb transfected expi293F as well as Siglec 7 DMAb electroporated mice sera, MaxiSorp plates were coated at 4°C overnight with 10 µg/mL of Goat-anti human IgG Fc (Bethyl). Plates were washed and blocked with 5% milk in PBS-T (0.05% Tween 20 in PBS) for 2 h at RT. Plates were washed, and samples diluted in 1% NCS in PBS containing 0.2% Tween 20 were added and incubated at 37°C for 2 h. Plates were again washed and incubated with 1:10,000 dilution of HRP conjugated goat anti-human IgG (H+L) secondary antibody (Bethyl) for 1 h at RT. The plates were developed with SigmaFast OPD for 5-10 min and OD450 signals were measured. Cyclic AMP determination 25,000 K562 or K562-hFSHR cells were plated in 96 well plates. Cells were washed twice with warm PBS then resuspended in 100 µl of serum-free RPMI with 0.5mM IBMX (Cayman chemicals) with or without DDAP antibody. After incubation for 30min at 37ºC FSH (50ng/ml or 1µg/ml) or PBS was added. One hour later, the cells were washed with ice cold PBS, lysed them and performed cyclic AMP determination according to the manufacturer’s instructions (Cell Signaling). Immunoblotting Protein extraction, denaturation and Western blotting were performed as previously described (Tesone et al., 2016). Membranes were blotted with the following antibodies: anti-Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (#9101, Cell Signaling), anti-p44/42 MAPK (Erk1/2) (clone 137F5, Cell Signaling), anti-LHCGR (clone 8G9A2, Abcam) and anti-β-actin (A5441, Sigma-Aldrich). Images were captured with ImageQuantLAS 4000 (GE Healthcare Life Sciences). In vitro cytotoxicity analysis through measurement of luciferase expression 10,000 OVCAR3 cells per well were plated in a 96-well plate and after 18 hours added primary peripheral blood mononuclear cells (PBMC). After a 4 h co- incubation, the cells were stained with 7AAD (Invitrogen), Annexin V (Biolegend) and anti-human CD45 (Biolegend) then performed a flow cytometry-based cytotoxicity assay as described previously (Perales-Puchalt et al., 2017, Clin Cancer Res 23: 441-53). Experiments were conducted to stably transfect K562 and K562-FSHR with firefly luciferase.20,000 K562 and K562-FSHR expressing luciferase were plated in a 96-well plate and co-incubated them for 5 hours with PBMC. Following the incubation, the cells were lysed and luciferase expression was measured using CytoTox Glo (Promega) as previously described (Zhang et al., 2009, Cancer Res 69: 6506-14). Cytotoxicity was calculated as (maximum viability control – individual well)/(maximum viability control – maximum death control)*100 as a percentage or relative to the control (PBMC with mouse IgG2a isotype control C1.18.4). In vitro cytotoxicity analysis using xCELLigence real time cell analyzer In vitro cytotoxicity assay was performed based on impedance using xCELLigence real time cell analyzer equipment (RTCA), Agilent Technologies, USA. The impedance is expressed as arbitrary unit called cell index (Durdagi et al., 2021, Mol Ther 30:963-974). Target cells were seeded into disposable sterile 96-well E-plates of the _{xCELLigence RTCA device at final cell concentration of 1x10} ⁴ _{-2 x10} ⁴ _{cells per well.} The instrument has been placed in a CO ₂ incubator during the experiment and controlled by a cable connected to the control unit. The 96-well E-Plate was placed in the xCELLigence RTCA device and incubated for 18-24 hours. Subsequently, the effector cells (Human PBMCs; E (Effector): T (Target) ratio=5:1/10:1) and treatments (antibodies/TCE/NKCE) were added. Real time analysis was performed for 3-7 days. The electrical conductivity is converted into the unitless cell index (CI) parameter by the xCELLigence device in every 15 minutes and images were captured at the 1 hour intervals. The data generated are normalized as per the time point when the effector cells and antibodies/TCE/NKCE were added to the target cells and were analyzed using RTCA/RTCA Pro Software. Immunohistochemistry and immunocytochemistry Mouse tumors were frozen in OCT (TissueTek) and frozen sections cut. 293T were grown on top of poly-L-lysine-coated cover slides (Sigma) and transfected using a human or murine FSHR expression vector. Slides were then fixed with 4% paraformaldehyde and permeabilized with 0.5% Triton X-100 in PBS. Sections were blocked using 5% normal goat serum followed by staining with DDAP antibody then AF647-conjugated secondary antibodies specific for human or mouse IgG (Invitrogen). Slides were viewed using Leica TCS SP-5 confocal microscope and Leica LAS-X software (immunocytochemistry) or Nikon ECLIPSE 80i microscope and the NIS- Element Imaging (immunohistochemistry). Western blot analysis For validating the in vitro and in vivo expression of Siglec 7 DMAbs, the supernatant collected after transfection of Expi 293F cells with the DNA encoding the antibodies or sera collected from mice after immunizing with the Siglec 7 DMAbs, were heat inactivated, reduced, and loaded with Odyssey Protein Molecule Weight (LI-COR). Following electrophoresis, samples were transferred onto polyvinylidene fluoride (PVDF) membranes via an iBlot-2 system (Thermo Fisher Scientific) and blocked using Odyssey Blocking Buffer (LI-COR). The heavy and light chains were detected using goat anti-human secondary antibody (LI-COR). The expression of Bispecific T and NK cell engagers were detected using goat anti human IgG F(ab’)2 (Jackson ImmunoResearch Laboratories Inc) followed by donkey anti-goat antibody (LICOR). Immunofluorescence (IFA) analysis: Siglec 7 transduced HEK 293T cells were seeded in 2-well chamber slides and allowed the cells to adhere overnight. The cells were permeabilized using 0.5% Triton 100 in PBS followed by blocking using 5 % goat serum. Following this, primary antibodies/bispecific were added and incubated overnight at 4°C. Subsequently, the slides were incubated with goat anti-human H+L (Texas Red conjugated) secondary antibodies. Nuclear staining was done with 4′, 6-diamidino-2-phenylindole (DAPI). The samples were mounted onto glass slides with the help of Fluoroshield mounting medium (Invitrogen) and then observed using a Leica TCS SP8 WLL scanning laser confocal microscope. Cytokine secretion profile analysis: OVCAR3-FSHR (Target) cells were plated at the density of 1X10 ⁴ cells/well. After overnight incubation, PBMCs (Effector cells; E: T=5:1) and DDAP- NKCE or pVax1were added to the target cells. Post 48 hours, the supernatants were collected and analyzed for secreted cytokines by LEGENDplex™ Human CD8/NK Panel (13-plex) multiplex bead-based assay (Biolegend) as per the manufacturer’s protocol Tumor challenges: NOD/SCID-γ (NSG) mice were challenged with OVISE and OVCAR3- FSHR cells.0.8x10 ⁶ OVISE cells (in PBS and Matrigel; 1:1) were injected on the right flank subcutaneously.7 days after tumor implantation, when the tumors were palpable, mice were treated with pVax1 (100 µg), or Siglec 7 DMAbs (50µg HC+50µg LC). The same day when expression vector was given, 7x10 ⁶ PBMCs were injected intraperitoneally into each mouse. The mice were inoculated three times, one week apart. Tumor sizes were monitored periodically via caliper measurements. Mice were euthanized upon developing signs of graft versus host disease (GVHD). Tumor volume (V) was calculated as per the formula V = [(length Xwidth ² )]/2; width is the side with smaller measurement. For OVCAR3-FSHR challenge model, NSG mice were injected with 3x10 ⁶ FSHR expressing OVCAR3 or OVCAR3-FSHR cells on the right flank subcutaneously.3 days after when the tumor became palpable, mice were inoculated with pVax1 (100 µg), or DDAP-TCE (100 µg), or DDAP-NKCE (100 µg). The same day when expression vector was given, 10x10 ⁶ PBMCs were injected intraperitoneally into each mouse. The mice were inoculated twice, one week apart and the same procedure as above was followed henceforth. Animal experiments were approved by the Institutional Animal Care and Use Committee at The Wistar Institute. Human PBMCs from healthy donors were provided by the Human Immunology Core of the University of Pennsylvania. Statistical analysis All statistical analyses were done using Graph Pad Prism. A p-value < 0.05 was considered statistically significant. Differences between the means of experimental groups were calculated using a two-tailed unpaired Student’s t test or one- way ANOVA where more than two quantitative variables were measured. Error bars represent standard error of the mean. Comparisons between tumor size at each time point were done using two-way ANOVA with Fisher’s least significant difference (LSD) test. The results are now described. Generation and flow cytometry screening of anti-human FSHR antibodies The Follicle stimulating hormone receptor (FSHR) is a tumor-associated antigen present in ovarian cancer (Perales-Puchalt et al., 2017, Clin Cancer Res 23: 441- 53), prostate cancer (Mariani et al., 2006, J Urol 175: 2072-7), and the neovessels of 80% of cancers (Radu et al., 2010, N Engl J Med 363: 1621-30). FSHR is a G-coupled protein receptor with seven transmembrane domains (Fan and Hendrickson, 2005, Nature 433: 269-77). This complex structure presents challenges for classical antigen protein approaches. A codon optimized sequence of the human FSHR was generated (Figure 1A) for direct in vivo immunization. The FSHR cDNA was subcloned into the pBMN-I-GFP expression vector (Figure 1B) and used it to inoculate mice by DNA injection followed by in vivo electroporation. Animals were immunized biweekly, and sera were collected a week after each immunization for analysis of antibody levels (Figure 1C). To detect anti-FSHR antibodies that would bind to native FSHR expressed in the cell membrane, stably transduced K562 cells were generated to overexpress human FSHR (K562-FSHR). To validate the correct folding and functionality of the recombinant FSHR, experiments were conducted to test the response of K562-FSHR cells to follicle stimulating hormone (FSH). It was observed that K562-FSHR increased their production of cyclic AMP and ERK phosphorylation upon FSH stimulation, but no response was observed in the parental K562 (Figure 1D & Figure 1E). To monitor the ability of immune sera to bind FSHR, K562 (GFP-) and K562-FSHR (GFP+) cells were combined at equal ratios and added sera diluted up to 1:1000, followed by anti-mouse IgG APC-conjugated secondary antibody (Figure 9A&9B) and determined the fold mean fluorescent intensity (MFI) of K562-FSHR compared to wildtype K562. When a 1:1000 serum dilution exceeded 20-fold MFI, a last immunization was performed 3 weeks from the previous immunization by boosting with FSHR-overexpressing A20 cells. Boosted animals were sacrificed 4 days later for hybridoma generation as described (Bordoloi et al., 2021, ACS Pharmacol Transl Sci 4: 1349-61; Choi et al., 2020, Hum Vaccin Immunother 16: 907-18). Two weeks following the fusion, supernatants from fifteen, 96 well plates were screened using flow cytometry to analyze the potential hybridomas (Figure 9C). The top 20 clones based on fold-MFI were expanded for further analysis (Figure 9D). A highly potent clone was selected based on high binding specificity. Anti-FSHR antibody binds FSHR with high specificity DDAP binds to ovarian cancer cell lines spontaneously expressing FSHR (Perales-Puchalt et al., 2017, Clin Cancer Res 23: 441-53; Zhang et al., 2009, Cancer Res 69: 6506-14). Cell lines (CAOV3, OVCAR3 and TOV-21G) all showed the expected expression of FSHR by DDAP staining (Figure 1F). To further confirm that the signal elicited by DDAP corresponded to FSHR, CRISPR mediated deletion of FSHR in TOV- 21G cell line was performed. Flow cytometric staining with DDAP antibody showed absence of binding to TOV-21G cell line after FSHR knock-out (Figure 1G). This clone was highly specific for FSHR as K562 cells transfected with LHCGR, the homologous protein to FSHR (sequence homology ~46% in the ECD and ~72% in the 7TMD) (Ulloa- Aguirre et al., 2018, Front Endocrinol (Lausanne) 9: 707) did not show cross-reactivity by flow cytometry analysis (Figure 1H). Experiments were performed to further test whether DDAP was also able to bind murine FSHR, as mouse models of disease are important to study the in vivo efficacy and safety of new therapies. Murine FSHR was expressed in mouse tumor lines A20 and ID8-Defb29/Vegf-a and again tested binding of DDAP to transfected and untransfected cells by flow cytometry. It was observed that DDAP successfully bound murine FSHR as it did human FSHR (Figure 1I). Anti-FSHR antibody for detection of FSHR ⁺ Tumor cells Immunohistochemical detection of proteins from biological samples is a common way of determining protein expression from tumors or other specimens to better classify them for prognostic or therapeutic purposes. To explore if DDAP detects FSHR in immunohistochemistry, solid tumors were generated in NSG immunodeficient mice. To generate tumors, 5 million K562, K562-FSHR, OVCAR-3 or TOV-21G were injected in 50% PBS/Matrigel (Corning) into the axillary flank of NSG mice. DDAP detected FHSR from frozen tumor sections (Figure 2A). Additionally, the antibody is useful for staining FSHR in immunocytochemistry analysis. Human or murine FSHR-transduced 293T cells were stained with DDAP. DDAP was able to bind both human and murine FSHR similar to polyclonal anti-human, but not to mock transfected 293T cells confirming this activity (Figure 2B-D). Anti-FSHR antibody induces antibody-dependent cell mediated cytotoxicity (ADCC) To determine the isotype of DDAP, ELISA was performed and found DDAP to be IgG2a (Figure 2E), an isotype that can elicit ADCC (Akiyama et al., 1984, Cancer Res 44: 5127-31). ADCC capacity was tested with K562 with or without FSHR. DDAP was able to increase the cytotoxic activity of PBMC against K562-FSHR but not against K562 (Figure 2F&G). To determine its ability to induce ADCC against unmodified FSHR ⁺ ovarian cancer cell lines, OVCAR3 cells were cocultured with PBMC in the presence of DDAP or an irrelevant IgG2a antibody. It was found that the physiological expression levels of FSHR in the ovarian cancer cells were sufficient to be targeted by DDAP mediated cytotoxicity (Figure 2H) with increasing doses of antibodies. The killing activity in OVCAR3-FSHR cells was also evaluated in the xCelligence assay and was found to induce a dose dependent killing of FSHR overexpressed OVCAR3 cells (Figure 2I). Therefore, DDAP can be used to induce cytotoxicity selectively against target FSHR ⁺ cells, with modest activity. Generation, expression, and cytotoxicity of DDAP-TCE Bispecific T cell engagers represent a recent significant development in the field of monoclonal technology. As DDAP anti-FSHR antibody exhibited initial levels of ADCC, experiments were designed to improve on this potential. An FSHR targeting TCE (DDAP-TCE) was designed (Gary et al., 2021, iScience 24: 102699; Patel et al., 2018, Cell Rep 25: 1982-93 e4; Perales-Puchalt et al., 2019, Mol Ther 27: 314-25). Experiments were designed to genetically optimize and fuse the scFv of the FSHR mAb with the scFv of an optimized sequence encoding anti-CD3 (modified UCHT1) (Figure 3A & B). DDAP-TCE was efficiently expressed in vitro upon transfection of the DNA in Expi293F cells (Figure 3C). This novel bispecific showed no nonspecific binding to K562 cells which do not have natural FSHR expression (Figure 3D) and retained binding to K562-FSHR cells (Figure 3E). Binding to FSHR was further confirmed in CaOV3 (Figure 3F) and OVCAR3-FSHR cells (Figure 3G). CD3 binding of DDAP-TCE bispecific was confirmed with human primary T cells (Figure 3H). To determine the functionality of this novel bispecific expressed in vitro, DDAP-TCE supernatant or media alone with OVCAR3-FSHR OC cells was co-cultured in vitro with human PBMCs and analyzed quantitively using real time xCELLigence based killing assay for tumor cell clearance. Incubation with immune cells + DDAP-TCE led to a highly potent cytotoxic effect on OVCAR3-FSHR cells. No cytotoxicity was found in the absence of DDAP- TCE or effector cells (Figure 3I). Generation and screening of anti-human Siglec 7antibodies Hybridomas which produced mAbs that specifically react with human Siglec 7 expressed in cell lines were produced and screened. Three mAbs targeting Siglec 7 were sequenced and studied in more detail. DB-S7-1, DB-S7-2 and DB-S7-7 showed strong cell binding whereas no binding was observed in case of anti-Siglec 3 (6C5/2, R&D Systems) (Figure 10A). In order to verify the specificity of these three anti-Siglec 7 antibodies, they were checked for binding to Siglec 9 overexpressing 293T cells (293T- Siglec 9). Siglec-9 also belongs to Siglec-3/CD-33 related Siglecs and exhibits homology (84% similarity) to Siglec 7 (Angata and Varki, 2000, J Biol Chem 275: 22127-35). Commercial anti-Siglec 9 antibody (Clone K8, Biolegend) showed binding to 293T- Siglec 9 cells; as expected, whereas no binding was observed for DB-S7-1, DB-S7-2 and DB-S7-7 anti-Siglec 7 ab clones; confirming specificity of the anti-Siglec 7 antibodies. (Figure 10B). To further visualize the binding of anti-Siglec 7 antibodies to human Siglec 7, high resolution confocal imaging of 293T-Siglec 7 fixed cells was performed. Cells were labeled with DAPI (nuclei), GFP (Siglec 7) and Texas Red (Anti-Siglec 7). As shown in Figure 10C, DB-S7-2 showed strong binding to Siglec 7; DB-S7-1 and DB-S7- 7 also exhibited binding to human Siglec 7, whereas no binding was observed with the secondary antibody control alone. Cytotoxicity studies of human anti-Siglec 7 antibodies To determine the ability of anti-Siglec 7 antibodies to induce cytotoxicity by activation of NK cells, in vitro cytotoxicity assay was performed based on impedance using xCELLigence real time cell analyzer. The target cells (A549, HaCaT, GMO5389, OVISE, OVCAR8 and SKOV3) were placed in the xCELLigence RTCA device, incubated for 18-24 hours, and subsequently, human PBMCs and anti-Siglec 7 antibodies were added. The real time analysis for A549 (lung adenocarcinoma cells), HaCaT (Human keratinocyte cells) and GMO5389 (Human fibroblast cells) showed no cytotoxicity induced by the presence of anti-Siglec 7 antibodies: DB-S7-1, DB-S7-2 and DB-S7-7, when cultured up to a period of 3 days after the addition of effector cells and antibodies (Figure 4A, 4C & 4E). The images captured 3 days post addition of effector cells and antibodies to target cells, show no killing in the presence of antibodies when compared to the no antibody control wells (Figure 4B, 4D & 4F). Upon evaluating cytotoxicity in different human OC cells, DB-S7-2 can induce significant tumor cell killing. The killing was observed within 24 hours of treatment with antibodies and effector cells in case of OVISE and SKOV3 cells, whereas for OVCAR8 cells, DB-S7-2 induced killing appears around 30 hours. DB-S7-1 and DB-S7-7 were also able to induce killing in OVISE, OVCAR8 and SKOV3 human ovarian cancer cells, though the killing efficacy with these reagents was not as potent as DB-S7-2 (Figure 4G, 4I & 4K). As shown in the images, post 3 days of addition of effector cells and treatment with DB-S7- 2, no attached tumor cells were observed in the treated wells. In case of the clones, DB- S7-1 and DB-S7-7; killing was observed as well compared to control wells (Figure 4H, 4J & 4L). In vitro expression of Siglec 7 DMAbs and tumor cell killing To rapidly assess the anti-Siglec 7 DMAbs in vivo, expression cassettes was developed as DNA vectors for direct delivery. Experiments were designed to encode codon and RNA-optimized sequences for the heavy and light chains of DB-S7-1, DB-S7- 2 and DB-S7-7 into a pVax1 plasmid expression vector, as dual plasmids (Figure 5A). Antibody expression was tested in vitro by transfecting expi293F cells with the synthetic human Siglec7 DNA vectors by Western blot analysis after 5 days of transfection. Bands corresponding to the heavy and light antibody chains in the human Siglec 7 DMAbs- transfected Expi293F supernatant could be clearly identified but not in the empty factor transfected control wells (Figure 5B). DB-S7-1, DB-S7-2 and DB-S7-7 were expressed at 7.5 µg/ml, 4.297 µg/ml and 7.824 µg/ml respectively in vitro (Figure 5C). The fully human recombinant antibodies generated were then further evaluated for their ability to induce killing in OC cells; OVCAR10 (Figure 5D &E), TOV-21G (Figure 5F), OVISE (Figure 5G) and PEO-4 (Figure 5H) cells. While all the three clones were inducing OC cells’ killing; clone DB-S7-2 exhibited the highest potency. The cell toxicity induced by DB-S7-2 was also evaluated in two additional OC lines; CaOV3 (Figure 5I) and OVCAR3 (Figure 5J) cells. DB-S7-2 retained its ability of effective killing in both the OC cells as well indicating the high potency of this anti-Siglec 7 mAb clone. In vivo expression of Siglec 7 DNA delivered MAbs and impact on tumor progression in ovarian cancer challenged model After confirming in vitro expression, in vivo expression of DMAb clones DB-S7-1, DB-S7-2 and DB-S7-7 were studied. In these studies, 50 µg +50 µg (HC+LC) for each of anti-Siglec 7 clone were injected as described with injection directly of the DNA using EP (Duperret et al., 2018, Cancer Res 78: 6363-70; Patel et al., 2018, Cell Rep 25: 1982-93 e4) to enhance transfection efficiency into the tibialis anterior muscle of mice (Figure 6A). The presence of human IgG in sera from the DB-S7-1, DB-S7-2 and DB-S7-7 Siglec 7 DMAbs’-injected mice but not control (data not shown) or in the pre bled mice sera (Figure 6B, Figure 11) was significant. The DB-S7-1 DMAb exhibited the highest in vivo expression with levels as high as 50 µg/ml in the mice sera (Figure 11). Further, human NK cells were stained with the Day 14 sera (DMAbs exhibited highest expression on Day 14) obtained from mice immunized with DB-S7-1, DB-S7-2 and DB- S7-7 DMAbs along with empty vector control. Day 14 sera from all the three groups positively stained human NK cells whereas the same was not observed in case of pVax1 or irrelevant antibody controls (Figure 6C). To determine the antitumor effects of Siglec 7 DNA delivery in vivo, next NOD/SCID- γ (NSG) mice were challenged with the OVISE human ovarian cancer cell line (0.8x10 ⁶ cells/mouse).50 µg +50 µg (HC+LC) of DB-S7-1 or DB-S7-2 DMAb or pVax1 empty vector was delivered in the muscle by electroporation when tumors reached _{an average size of above 50 mm} ³ _{. (Figure 6D). Notably, the groups receiving DB-S7-1} and DB-S7-2 Siglec 7 (Figure 6E) DMAbs demonstrated a significant decrease in the tumor burden/delay in tumor growth compared to the empty vector control showing the potential of Siglec 7 antibodies to impact ovarian tumor growth in vivo. Fc blocking led to enhanced killing efficacy mediated by anti-Siglec 7 antibody Fc gamma receptors (FcγRs) are largely expressed on lymphoid and myeloid cells such as granulocytes, macrophages and NK cells’ surfaces. However, they are allocated uniquely to each cell type; FcγRIIb is only expressed by B cells, FcγRIIIa is exclusively expressed by NK cells, while combinations of different FcγRs are expressed by various other immune cells allowing for balanced antibody mediated cellular responses (Bournazos et al., 2020, Nat Rev Immunol 20: 633-43; Romain et al., 2014, Blood 124: 3241-9; van der Poel and Carroll, 2017, Nat Immunol 18: 874-5). Similar to native human mAbs, DB-S7-2 anti-Siglec 7 Ab express the variable domains on one end which bind to Siglec 7 present on immune cells, thereby potentially inhibiting the interaction of the antigen with other glycoproteins. However, other end of the antibody bears the constant Fc region that binds to various Fc receptors to engage the innate arms of the immune system (Sanseviero, 2019, J Clin Med 8). The binding of anti-Siglec 7 antibody to immune cells not only through Fab regions but also the Fc region through linkage with FcγRs might interfere with the Siglec 7 mediated cell cytotoxicity and potentially lead to the retargeting of one immune cell by another immune cell (Figure 12). Experiments were designed to evaluate this issue in a preliminary fashion by blocking FcγRs present on immune cells using Fc blocker (Biolegend). As shown in Figure 6F, after blocking of FcγRs on immune cells, there was enhanced killing observed compared to no FcγR blockage. The killing of OVCAR3 cells was observed to occur at earlier time points when FcγR blocking was performed. The images shown in Figure 6G demonstrate enhanced killing upon blocking of FcγR in OVISE cells. FcγR blocking appears to increase both the quality and the quantity of immune cell-mediated antibody- dependent cytotoxicity by endowing more immune cells to participate in cytotoxicity via Siglec 7-mediated signaling to target OC cells. Generation and expression of DDAP-NKCE DNA encoded bispecific NK engager NK cell engagers (NKCEs) have emerged as a promising innate immune modality in the field of immune oncology. Presently, development of single-chain variable fragment (scFv) recombinant reagents with ability of specific targeting CD16 on NK cells and tumor antigens of interest are being evaluated for their use in the clinic (Gleason et al., 2014, Blood 123: 3016-26; Ibarlucea-Benitez et al., 2021, Proc Natl Acad Sci U S A 118). Based on the preliminary data above, the potential engagement of dual activating NKCE which targets Siglec 7 could provide an additional immune tool for tumor targeting and thus could be a promising therapeutic strategy in OC. Therefore, to eliminate any potential Fc mediated effects, engage NK cells more directly, and improve targeting potential, experiments were designed to develop a Siglec 7 based bispecific NKCE. It was constructed as two linked antibody binding fragments (scFvs) so that one engages the targeted tumor antigen; FSHR, while the second engages the innate immune system through binding to Siglec 7, highly expressed on NK cells. The scFv of DB-S7-2 anti-Siglec 7 antibody encoded optimized sequence was fused with the scFv of anti-FSHR (Clone DDAP) encoded optimized sequence (Figure 7A) using a GS (Glycine-Serine) flexible linker (Perales-Puchalt et al., 2019, Mol Ther 27: 314-25). This DDAP-NKCE was efficiently expressed in vitro as studied by transfection of Expi293F cells, as an ~55KDa molecule (Figure 7B). The binding of DDAP-NKCE was confirmed to bind to both cellular targets by flow staining on Siglec 7 or FSHR overexpressing HEK293T (Figure 7C) or K562 (Figure 7D) cells respectively. To visualize the binding of this novel bispecific NKCE to human Siglec 7, high resolution confocal imaging of 293T-Siglec 7 fixed cells was performed. Cells were labeled with DAPI (nuclei), GFP (Siglec 7) and Texas Red (DDAP-NKCE). DDAP- NKCE is observed to exhibit clear surface binding to GFP+ cells which express human Siglec 7 (Figure 7E). Cytokine secretion profile of novel FSHR targeting NK cell engagers Cytokines are involved in promoting the proliferation, survival, differentiation, and activation of lymphocytes (Romain et al., 2014, Blood 124: 3241-9). Experiments were designed to examine the cytokine secretion profile of the new DDAP- NKCE, as cytokine production is a critical component of NK cell function (Gleason et al., 2012, Mol Cancer Ther 11: 2674-84). A recent study conducted by Gauthier and group reported CD20-NK Cell engagers targeting NKp46 and CD16, two other receptors present on human NK cells to induce hardly detectable cytokine release, yet exhibited high anti-tumor potential, demonstrating an important profile for such NKCEs (Gauthier et al., 2019, Cell 177: 1701-13 e16). Increased production of sFas and granulysin in DDAP-NKCE treated group was observed compared to empty vector controls (Figure 7F). DDAP-NKCE; engaging FSHR and mainly NK immune cells exhibited diminished induction of inflammatory cytokines, which may be important in clinical development and these immune profiles which are distinguished from other NKCEs confirm the uniqueness of the Siglec 7 NK bispecific engagement. FSHR targeted novel bispecific T and NK cell engagers induced potent killing in multiple ovarian tumor lines and decreased tumor burden in vivo To determine the functionality of the DDAP-NKCE, xCELLigence real time killing assays were performed, in which the potential of the DDAP-NKCE to induce killing of a panel of human ovarian tumor lines was evaluated. In vivo delivered DDAP- NKCE was compared with DDAP-TCE for induction of tumor killing in vitro. The effector cells (PBMCs/T/NK cells) and TCE/NKCE were added a day after the plating of target OC cells. HEK 293T cells was used as a control; a FSHR-negative cell line (Urbanska et al., 2015, Cancer Immunol Res 3: 1130-7). Notably, nonspecific off target killing in FSHR-negative 293T cells was not observed (Figure 7G & H). DDAP-TCE and DDAP-NKCE effectively killed OVCAR3-FSHR cells in the presence of purified human T cells and NK cells alone respectively (Figure 13A & 13B). Further evaluation of different FSHR expressing ovarian tumor cells demonstrated that DDAP-NKCE was highly efficient in the killing of OVISE (Figure 8A&B), CaOV3 (Figure 8C&D), OVCAR3-FSHR (Figure 8E), PEO-4 cells (Figure 8F) and Kuramochi-FSHR cells (Figure 8G) in the presence of human PBMCs as source of T and NK cells. Importantly, Kuramochi and PEO-4 bear BRCA2 mutations and the later also exhibits resistance to PARP inhibitors (Sakai et al., 2009, Cancer Res 69: 6381-6) but has no escape from DDAP-NKCE killing. Similarly, DDAP-TCE was found to exert potent killing as DDAP- NKCE bispecific. However, the efficacy for both varies in PEO-4 cells. These differences suggest important nuances which may be further developed and potentially complimentary which warrants further investigation. Additionally, non FSHR targeting NKCE (IL13Rα2-NKCE) and TCE (IL13Rα2-TCE) did not induce any toxicity in FSHR expressing OVCAR3 cells (Figure 13C&13D). Further, to validate sFas mediated killing of DDAP-NKCE, the killing efficacy of this novel NKCE was compared in the presence and absence of an anti-Fas antibody. Fas (CD95, apoptosis antigen 1) is a member of death receptor subfamily of the TNF receptor superfamily. Fas/FasL binding is known to induce extrinsic apoptosis pathway. In the presence of anti-Fas antibody, decreased killing of OVCAR3-FSHR cells by DDAP-NKCE was observed. This suggests a novel killing mechanism of DDAP-NKCE through involvement of Fas. To further evaluate the in vivo antitumor efficacy of DDAP-NKCE and DDAP-TCE, NSG mice was challenged with OVCAR3-FSHR cells. NSG mice were administered with OVCAR3-FSHR cells and 4 days after tumor implantation, they were given DDAP-TCE, DDAP-NKCE or empty vector, twice one week apart. On day 4, they were also inoculated with human PBMCs, and tumor volumes were measured periodically (Figure 8H). The treatment with both bispecifics led to significantly decreased tumor burden in OVCAR3-FSHR tumor bearing mice, while no such impact was observed in the control treated group (Figure 8I) supporting potential synergy of this approach (Figure 14). Engineering FSHR to Engage Innate or Adaptive Immunity for Ovarian Cancer Immunotherapy Despite the important advances in the field of OC therapy, recurrent OC still presents extremely poor prognosis and thus portends a highly lethal cancer type (Izar et al., 2020, Nat Med 26: 1271-9; Kurnit et al., 2021, Obstet Gynecol 137: 108-21; Hamanishi et al., 2016, Int Immunol 28: 339-48). Although there are multiple reasons to suppose that OC would respond favorably to treatment with immunotherapy; as the ovarian carcinoma cells express cancer-specific antigens, and these can elicit antitumor immune response after immunotherapy, yet the immunotherapy response rates among OC patients remain fairly modest (Coleman, 2016, Nat Rev Clin Oncol 13: 71-2). Notably, a prime obstacle in the development of targeted therapies is finding targets with specific expression confined to the surface of tumor cells, but not the healthy tissues (Perales- Puchalt et al., 2017, Clin Cancer Res 23: 441-53). FSHR is one such target with selective expression on ovarian granulosa cells (Perales-Puchalt et al., 2017, Clin Cancer Res 23: 441-53) and thus experiments were designed to study its consideration as a potential target in OC. Follicle stimulating hormone is a critical ovarian epithelial cell growth- inducing factor, which functions through binding to FSHR. Overexpression of FSHR is responsible for upregulation of oncogenic pathways and increased EOC proliferation. Hence FSHR could be utilized as an important therapeutic target for directing T cells against OC (Perales-Puchalt et al., 2017, Clin Cancer Res 23: 441-53). It was recently reported the potential for tumor impact, tolerability and safety of targeting FSHR by immunization in an immunocompetent mouse model (Perales-Puchalt et al., 2019, JCI Insight 4). Injection of optimized DNA sequences followed by electroporation confers overexpression of the protein in its native conformation capable of eliciting potent immune cellular and humoral responses (Tebas et al., 2017, N Engl J Med; Yan et al., 2013, Cancer Immunol Res 1: 179-89). Here experiments were extended to generate of anti-FSHR monoclonal antibodies and use this reagent to develop novel biologics. The results presented herein demonstrate the generation and characterization of a potent anti- FSHR antibody and its application as a tool for immunotherapy of OC. Several individual clones, among them clone DDAP was selected for additional study based on its potency and reactivity. The MAb supports detection of FSHR expression in samples by multiple methods, including flow cytometry, ELISA and immunocytochemistry. This extends its potential impact into the clinic where it may aid in determining the FSHR status of patient samples for personalized medicine approaches. An important recent tool in the field of antibody technology for cancer therapy is the bispecific T cell engager approach. While most of these are in preclinical and early clinical study, there is a single approved cancer bispecific product, Blincynto (blinatumomab) which is used as a therapy for acute lymphoblastic leukemia (ALL) that targets CD19 on B cells and engages T cells through linked anti-CD3 binding (Sheridan, 2021, Nat Biotechnol 39: 251-4). Bispecific T cell engagers can redirect both CD4 as well as CD8 T cells for the killing of tumor cells and are independent of intrinsic antigen specific TCR recognition by the T cells (Dao et al., 2015, Nat Biotechnol 33: 1079-86). Despite exhibiting high anti-tumor efficacy, the advancement rate of these tools is slower than desired due to several factors including tumor antigen specificity, off tumor activity, specific cytokine release issues and short half-lives (Perales-Puchalt et al., 2019, Mol Ther 27: 314-25). Based on the specificity of the DDAP anti-FSHR clone, it was reasoned this could be an important target for study. Direct DNA in vivo delivery was used to rapidly evaluate these new potential tools in OC models. The DDAP-TCE showed binding to both FSHR and CD3 ends with potent killing observed at nanogram levels (7.81 ng/ml) in the presence of human PBMCs. This DDAP-TCE was significantly more potent in specific tumor killing than the DDAP parental antibody. Some aggressive OC types such as HGSOC and OCS, referred to as “Cold” tumors are associated with restricted treatment approaches and low TIL infiltration causes them to be less responsive and highly lethal (Wu et al., 2021, Front Immunol 12: 672502). Thus, T cell approaches as well as innate effector cells such as NK may be important tools for study. (Hoogstad-van Evert et al., 2020, Gynecol Oncol 157: 810-6). NK cells serve as the first line of defense in tumor immunosurveillance (Wiernik et al., 2013, Clin Cancer Res 19: 3844-55). Recent limited data suggests that OC may be responsive to NK cell attack (Hoogstad-van Evert et al., 2020, Gynecol Oncol 157: 810- 6). Early NK bispecific work has focused on NK cell related receptors. NK cells find their immune targets through involvement of NKG2D and natural cytotoxicity receptors, which are associated with the regulation of natural cytotoxicity. Additionally, the activating receptor CD16 (FcγRIII), which binds potently to specific Ig isotypes facilitates NK driven ADCC (Wiernik et al., 2013, Clin Cancer Res 19: 3844-55) as consequences of antibodies trafficked to the local tumor environment. Thus, the immune response elicited by the NK cells is dependent on interactions between the receptors present on NK cells, direct recognition of tumor at the site, or the host humoral response to the target cell ligands which engage the NK cells (Wiernik et al., 2013, Clin Cancer Res 19: 3844-55). Although, NK cells are capable of lysing tumor cells as described, and thus play role in tumor immune surveillance; tumor cells often utilize immune evasion strategies to escape this immune function. An area of recent importance linked to immune escape is through tumors displaying increased sialic acid glycosylation on their surface as immune static decoys for NK attack. NK cells display Siglec 7, which when engaged on the surface of human NK cells through tumor association can inhibit NK-mediated target killing (Prescher et al., 2017, J Med Chem 60: 941-56). Siglecs have recently been designated as glyco-immune checkpoints but much of this work is early. Through their interactions with sialylated glycan ligands which are overexpressed on cancer cells, inhibitory Siglecs may impact protective anti-tumor immunity (Hong et al., 2021, ACS Cent Sci 7: 1338-46). Thus, targeting Siglec 7 represents a promising therapeutic strategy to augment antitumor immune responses in OC (Ibarlucea-Benitez et al., 2021, Proc Natl Acad Sci U S A 118). To accomplish this, several human like antibodies against Siglec 7 using a transgenic humanized mouse (Bordoloi et al., 2021, ACS Pharmacol Transl Sci 4: 1349-61; Perales-Puchalt et al., 2019, Mol Ther 27: 314-25) which provide advantages for study and rapid translation due to their V regions being derived from human V gene lineages (Tu and Zheng, 2016, Methods Mol Biol 1371: 157-76). Several important clones were developed, and experiments were designed to move forward with the three highly potent clones (DB-S7-1, DB-S7-2 and DB-S7-7) with high binding to recombinant human Siglec 7, Siglec 7 expressed in cells and human NK cells. It was observed that the antibodies can drive NK cell function in the presence of tumor target cells facilitating specific killing of target OC cells without nonspecific killing of cell targets. These are important tools for further evaluation. Further characterization of DDAP-NKCE is presented herein. It is believed that this is the first report of a Siglec 7 based bispecific NK cell engager. The sequence of DB-S7-2, which showed highest potency, was used for the design of this novel bispecific human NKCE and linked it with anti-FSHR. This DDAP-NKCE was highly potent in tumor specific cell killing, as evaluated using a panel of human ovarian tumor cells. Targets included cell lines harboring mutation in BRCA gene and also the ones exhibiting resistance to chemotherapy or Poly-ADP-ribose polymerase inhibitors (PARPis). Despite demonstrating impressive activity in case of sporadic high grade serous OC as well as BRCA-related OC, unfortunately, as with classical chemotherapy, many patients are eventually reported to acquire resistance to PARPi treatment (Franzese et al., 2019, Cancer Treat Rev 73: 1-9; Liu et al., 2014, Gynecol Oncol 133: 362-9; McMullen et al., 2020, Cancers (Basel) 12; Yang et al., 2020, Front Immunol 11: 577869), supporting new approaches targeting such OC tumors are important. The high potency displayed by both DDAP-TCE and DDAP-NKCE; bispecific T and NK engagers using FSHR targeting is encouraging. Notably, it was observed that both NK and T cells engagers targeting FSHR were found to have equal potency in attenuating tumor burden/tumor progression in vivo in ovarian tumor bearing mice models. Differences between both DDAP-TCE and DDAP-NKCE were observed; the FSHR targeted bispecifics. Both are highly potent approaches to impact tumor in vitro and in vivo. DDAP-NKCE exhibits potent killing with reduced cytokine elaboration phenotype. These studies demonstrate for the first time the utility of targeting FSHR for a major subset of OC, that bispecific tools focused on FSHR and CD3 are highly immune potent, that Siglec 7 mAbs engage and activate NK cells and finally that Siglec 7 NKCE are potent tools for targeting OC, which can impact tumor growth in vivo and that a combination of these two approaches may have additional benefits. It is believed that the results presented herein show the first time a new target for NK cell activation by bispecific engagers, a diverse population of OC are potentially of interest for these therapies. These can have a direct application in OC research and diagnosis. Additional efforts are warranted to further investigate these important tools for translational advancement of these approaches for ovarian and other cancers expressing FSHR. Siglec NKCE should be further studied in relevance to other solid and liquid tumor targets. Example 2: Designed IL13Ra2 and Siglec7 targeting bispecific NK cell engager (IL13Ra2-NKCE). Figure 17 shows a schematic of designed IL13Ra2 and Siglec7 targeting bispecific NK cell engager (IL13Ra2-NKCE). IL13Ra2-NKCE showed potent activity for killing antigen positive melanoma cells (Figure 20). Example 3: Siglec-7 glyco-immune checkpoint MAbs and NK cell engager biologics induce potent antitumor immunity against ovarian cancers Aggressive OC types such as HGSC and ovarian carcinosarcoma (OCS), are referred to as “Cold” tumors as they exhibit low tissue infiltrating lymphocyte (TIL) infiltration and are associated with poor treatment responses (Wu et al., 2021, Front Immunol 12, 672502, Hoogstad-van Evert et al., 2020, Gynecol Oncol 157, 810-816). Thus, engaging immune responses by additional means is very important for immune targeting of cold tumors (Pugh-Toole et al., 2022, Curr Treat Options Oncol 23, 210- 226). The innate immune effector system is significant to consider as NK cells serve as a first line of defense in tumor immunosurveillance (Wiernik et al., 2013, Clin Cancer Res 19, 3844-3855). Tumors evade the T cell responses through multiple mechanisms such as MHC downmodulation and upregulation of T cell exhaustion programs (Vinay et al., 2015, Semin Cancer Biol 35 Suppl, S185-S198). Similarly, cancers can utilize host systems to bypass the surveillance function of NK cells though immune evasion strategies including shedding soluble ligands for NK activating receptors, release of inhibitory cytokines, upregulation of HLA molecules and thus escape NK immune function (Sabry et al., 2013, Front Immunol 4, 408), but NK non-responsiveness is also likely mediated by additional NK regulatory pathways. Recent studies have identified that many tumors display increased levels of sialic acid on their surface, which likely functions as a negative signal to NK cells allowing the tumor to avoid NK immune surveillance (Dobie et al., 2021, Br J Cancer 124, 76-90). One effort in the approach to strengthen NK activation against such hypersialylated tumors is the desialylation of target cells expressing ligands of Siglec-7 (Jandus et al., 2014, J Clin Invest 124, 1810-1820). As NK cells display Siglec-7, a receptor / sensor for distinct sialoglycan determinants, which when engaged on the surface of human NK cells through tumor association can serve to inhibit NKmediated target killing (Prescher et al., 2017, J Med Chem 60, 941- 956; Fong et al., 2018, Proc Natl Acad Sci U S A 115, 10410-10415; Meril et al., 2020, Mol Carcinog 59, 713-723) These may exhibit regulatory negative signals by a sialoglycan tumor shield. Very recent studies suggest that some Siglecs could function as a glyco-immune checkpoint molecules that inhibit NK mediated anti-tumor immunity in an MHC independent manner (Hong et al., 2021, ACS Cent Sci 7, 1338-1346). In this study, the use of monoclonal antibodies and derivatives that target Siglec-7 for tumor immune modulation was examined to confirm and perhaps overcome such glyco-CPI function to improve the ability to impact tumor control. Anti-tumor immune responses for an aggressive difficult to treat phenotype of human OC (19) were the focus of these studies. The group developed several antibodies (Bordoloi et al., 2022, JCI Insight 7; Perales-Puchalt et al., 2019, JCI Insight 4; Bordoloi et al., 2021, Genes Cancer 12, 51-64) against Siglec-7 using a transgenic humanized mouse model. In this study, three highly potent Siglec-7 binding clones were focused on. These antibodies were engineered as human IgG1, and their immune cell binding was studied. Strong staining of anti-Siglec-7 antibody on NK cells was observed including both bright and dim NK subsets suggesting its ability to bind bulk effector NK population. In addition, expression can activate NK cells and when these now activated cells are in the presence of several tumor lines, NK mediated killing can occur against previously refractory OC targets. These human Siglec-7 antibodies drive NK immune function in the presence of diverse OC tumor target cells facilitating specific killing of target OC cells. Importantly this approach should be relatively agnostic to tumor mutations. OC lines were tested with multiple genetic mutations including BRCA1, BRCA2, AKT2, TP53, SPOP, STAT3, MTOR, MEK1, MEK2, BRAF, among others (Table 1), and it was observed that all mutations were targeted by anti-Siglec-7 antibodies activation of NK cell targets. Table 1: Studied ovarian cancer cell types, cancer driver mutations in them and drug resistance These Mab were studied in combination with PD-1 CPI. It was found that the dual treatment was synergistic. However, it was observed that the potency of the Siglec-7 antibody was 10 times greater than the anti-PD1 antibody, Pembrolizumab, which was studied, suggesting the potential value of this combined NK T cell anti exhaustion panel. Next a humanized NSG mouse model engrafted with human PBMCs was utilized and it was observed that a single dose of DNA encoded DB7.2 Siglec-7 MAb demonstrated significant tumor control and increase in median survival of mice bearing OVISE human ovarian tumor. Due to a limitation of the NSG model in that it will develop graft vs host disease (Wunderlich et al., 2014, Blood 123, e134-144) over a few months, only single dose of anti-Siglec-7 was administered, yet it was still highly effective. It suggests that multiple doses over time, as current CPIs (Hirsch et al., 2022, Nat Med 28, 2236-2237) are utilized would be likely to provide additional benefit. Of note, this is the first demonstration of the impact of Siglec-7 targeting MAb alone as well as in combination with anti-PD1 (NK and T cell CPIs) for targeting OC or any human tumor and suggests more study of the potential added value to such combination, or CPI refractory tumors should be considered. These studies have important implications for tumor therapy supporting a novel non-T cell CPI potential approach to possibly augment current immune therapy strategies. Next the potency of Siglec-7 binding and activation of NK cells for targeted OC therapy was evaluated. Without being bound by theory, it was hypothesized that binding to Siglec-7 could directly engage NK cells and draw them to a cell target in an efficient manner. A new type of NKcell engager was developed by creating a bispecific fusion between FSHR targeting MAb and a potent anti-Siglec- 7 MAb. NKCEs have emerged as an interesting innate immune concept in the field of immune oncology. Presently, there is one such bispecific which has been advanced into the clinic; GTB- 3550 engaging CD16a-IL-15/CD33 for AML and CD33+ malignancies (Gleason et al., et al., 2014, Blood 123, 3016-3026; Ibarlucea-Benitez et al., 2021, Proc Natl Acad Sci U S A 118; Demaria et al., 2021, Eur J Immunol 51, 1934-1942). Other NK targets being studied preclinically include NKG2D, NKp30, and NKp46. The phenotype shown for the anti-Siglec-7 MAbs of binding and activation of NK cells that would otherwise be negatively impacted by a tumor sialoglycan cloak, suggest Siglec-7 could provide a unique immune tool for specific tumor-NK activation and engagement. The bispecific developed here, DB7.2xD2AP1, exhibited potent binding to both NK cells as well as ovarian cancer cells. It displays killing (pM level) against diverse OC phenotypes. This is the first report of a development of a member of the Siglec family as an immune engager or using such an approach for development of a Siglec-7 bispecific NK cell engager. This NKCE was specific for its target cells, and potent in tumor cell killing, as evaluated using a panel of different human ovarian tumor lines. FSHR expression on targets was a requirement for NK killing activity, as FSHR negative cells were not killed. Interestingly, DB7.2xD2AP11 led to fewer cytokine and cytotoxic molecules’ production, which suggests it important to study for a killing tool with a potential limited risk of cytokine release syndrome (CRS) (Pinto et al., 2022, Trends Immunol 43, 932-946). During these studies the focus was on OC cells that express mutations that are particularly problematic for OC therapies. This included PARPi resistant OC cells and OC displaying resistance against diverse drug targets, specifically HDAC (Dacinostat, Entinostat, Belinostat), PI3K (Dactolisib, Buparlisib), mTORC (Omipalisib), Wee1(CHEK1), TOP1(Gallibiscoquinazole, Mitoxantrone, Irinotecan), DNA alkylating agents (Oxaliplatin, Cisplatin) and microtubule stabilizer (Docetaxel) (Table 1) (Ai et al., 2021, Oncogene 40, 2496-2508; Diaz Osterman et al., 2019, Elife 8; Estep et al., 2007, PLoS One 2, e1279; Kapoor et al., 2018, Biochim Biophys Acta Mol Cell Res 1865, 392- 405; Ayestaran et al., 2020, Patterns (N Y) 1, 100065). The studies included OC lines containing BRCA (BRCA1 & 2) mutations as these are a major risk in OC cancer patient cohorts. Around 50% of HGSCs exhibit disrupted BRCA pathway either via germline or somatic mutation, or through epigenetic silencing of pathway members (Vaughan et al., 2011, Nat Rev Cancer 11, 719-725). PARP inhibition represents an important pathway for DNA damage repair and therefore PARPi hold great promise for the treatment of tumors with disruptive mutations in BRCA1/2. However, resistance to PARPi has been reported to be a problem for treating resistant OC patients (Noordermeer et al., 2019, Trends Cell Biol 29, 820-834). The potency and consistency for killing FSHR + tumors using both the Siglec-7 MAb as a NK CPI, as well as the bispecific Siglec -7 NK engager in vitro and in vivo is encouraging for potentially bringing additional tools to treat poorly responding OCs. In summary, the study describes potent Siglec-7 MAbs that engage and activate NK cells and can further complement PD-1 immunotherapy against OC representing a potential additional class of CPI in this case for NK cells. Furthermore, the data show that Siglec-7 can be used to build novel a NKCE and function as a potent tool for targeting receptor positive OC driving significant antitumor responses in vitro and in vivo. While these studies are important for designing additional tools for OC, other studies are warranted to examine the utility of such biologics against additional difficult cancers. The materials and methods are now described: Cells and animals Cell lines used in the experiments include OVCAR3, CaOV3, TOV-21G, OVISE, OVCAR10, PEO-4, Kuramochi cells, HaCaT human keratinocytes, WM3743 melanoma cells, human embryonic kidney 293T, Expi293F, AGS gastric cancer, and GM05389 human fibroblast cells.293T cells were transduced retrovirally to express Siglec-7. OVCAR3, OVISE and Kuramochi cells were retrovirally transduced with human FSHR to express FSHR as described previously (46). K562 cells were purchased from ATCC and retrovirally transduced to express FSHR. DNA-encoded MAb generation Several humanized antibodies were generated against human Siglec-7. These MAbs bound to Siglec-7 and could stain NK cells. Here these hybridomas were sequences and used to develop Siglec-7 DNA encoded monoclonal antibodies (DMAbs) as tools for in vitro expression (Patel et al., 2018, Cell Rep 25, 1982-1993 e1984). Final human IgG1 HC and LC were inserted into a pVax1 plasmid expression vector, under the control of the human cytomegalovirus (hCMV) promoter and bovine growth hormone (BGH) polyA signal as described (Patel et al., 2018, Cell Rep 25, 1982-1993 e1984). Plasmids were then transfected into Expi293F cells using the Expifectamine 293 Expression Kit (Thermo Fisher Scientific) to produce recombinant antibodies. The purity and apparent molecular weight of the recombinant antibodies were assessed by SDS- PAGE analysis. Design of FSHRx Siglec-7 NKCE FSHRxSiglec-7 Natural Killer cell engager (NKCE) was designed by encoding a codon-optimized scFv of Siglec-7 MAb (DB-S7-2) followed by the scFv of FSHR antibody (D2AP11) with the addition of an enhancing optimized IgE leader sequence. Both constructs were subcloned into a modified pVax1 expression vector (Perales-Puchalt et al., 2019, JCI Insight 4). FSHRxSiglec-7 NKCE is designated as DB7.2xD2AP11. Flow cytometry A BD LSRII flow cytometer was used for staining of cells. BD FACS Aria cell sorter (BD Biosciences) was used for the sorting of Siglec-7/FSHR stably expressing cells. Anti-human antibodies used were directly fluorochrome conjugated. Antibodies used: anti-Siglec-7 (F023-420, BD Pharmingen), anti-Siglec 3 (6C5/2, R&D Systems). For the non-conjugated primary antibodies, PE- secondary anti-human (H+L) (Invitrogen) and PE/AF647- secondary anti-human F(ab’)2 (Jackson ImmunoResearch Laboratories Inc) were used. Live/Dead Violet viability kit (Invitrogen) was used to exclude dead cells from analysis. For Fluorescence cytometry staining on PBMCs, the following antibodies were used: CD69 PE-Cy5 (clone FN50), PD-1 BV421 (clone EH12.2H7), CCR7 APC-Cy7 (G043H7), CD19 BV785 (clone HIB19), CD27 BV650 (clone 0323), CD56 BV570 (clone HCD56), CD16 BV711 (clone 3G8), CD21 PE-Cy7 (clone BU32) and Siglec-7 (clone 6-434) from Biolegend; CD11c BUV395 (clone B- ly6), CXCR5 BV750 (clone RF8B2), CD3 BUV805 (UCHT1), CD45 AF700 (clone HI30), CD127 PE-CF594 (clone HIL-7RM21), CD25 BUV737 (clone 2A3), CD8 BUV496 (clone RPA-T8), HLA-DR BV605 (clone G46- 6), CD38 BUV661 (clone HIT2), CD14 BV480 (clone MP9), CD45RA BUV563 (HI100), CD4 BB790 (clone SK3), CD15 FITC (clone HI98), CD103 BB700 (clone Ber-ACT8), CD161 APC (clone DX12) from BD Biosciences. Briefly, cryopreserved PBMC were thawed and rested for 2 hours at 37C and 5% CO2 in complete R10 media (RPMI supplemented with 10% FBS, 2 mM Lglutamine, 100 U/ml penicillin and 100 mg/ml streptomycin) with 10 U/ml DNAse I (Roche Life Sciences). Cells were washed with PBS and incubated with 0, 1 or 10 ug/ml of DB7.2 Siglec-7 antibody diluted in fluorescence-activated cell sorting (FACS) buffer for 20 minutes. After washing with FACS buffer, cells were incubated with mouse anti-human IgG Fab secondary antibody PE (Invitrogen) diluted in FACS buffer for 20 minutes. Cells were washed with FACS buffer, resuspended in PBS and prestained for chemokine receptor CCR7 and CXCR5 for 10 min at 37C 5% CO2. Then, cells were stained for viability exclusion using Live/Dead Fixable Aqua (Invitrogen) for 10 minutes, followed by a 20-minute incubation with a panel of directly conjugated monoclonal antibodies and Human Trustain FcX (Biolegend), diluted in equal parts of fluorescence-activated cell sorting (FACS) buffer (PBS containing 0.1% sodium azide and 1% bovine serum albumin) and brilliant stain buffer (BD Biosciences). Stained cells were washed and fixed in PBS containing 1% paraformaldehyde (Sigma- Aldrich). Samples were acquired using a FACS Symphony A5 cytometer and analysis was performed by Flowjo software 10.8.1 (Tree Star Inc.). Enzyme-linked immunosorbent assay (ELISA) For quantification of human IgGs in Siglec-7 MAbs as well as Siglec-7 DMAb electroporated mice sera, MaxiSorp plates were coated at 4°C overnight with 10 μg/mL of Goat-anti human IgG Fc (Bethyl). Plates were washed and blocked with 5% milk in PBS-T (0.05% Tween 20 in PBS) for 2 h at RT. Plates were washed, and samples diluted in 1% NCS in PBS containing 0.2% Tween 20 were added and incubated at 37°C for 2 h. Plates were again washed and incubated with 1:10,000 dilution of HRP conjugated goat anti-human IgG (H+L) secondary antibody (Bethyl) for 1 h at RT. The plates were developed with SigmaFast OPD for 5-10 min and OD450 signals were measured. In vitro cytotoxicity analysis using xCELLigence real time cell analyzer In vitro cytotoxicity assay was performed based on impedance using xCELLigence real time cell analyzer equipment (RTCA), Agilent Technologies, USA. The impedance is expressed as arbitrary unit called cell index. Target cells were seeded into disposable sterile 96 well E-plates of the xCELLigence RTCA device at final cell concentration of 1x10 ⁴ -2 x10 ⁴ cells per well. The instrument has been placed in a CO2 incubator during the experiment and controlled by a cable connected to the control unit. The 96-well E-Plate was placed in the xCELLigence RTCA device and incubated for 18- 24 hours. Subsequently, the effector cells (Human PBMCs/NKs; E (Effector): T (Target) ratio=5:1/10:1) and treatments (Siglec-7 MAbs/ NKCE) were added. Real time analysis was performed for 3-7 days. The electrical conductivity is converted into the unitless cell index (CI) parameter by the xCELLigence device in every 15 minutes and images were captured at the 1-hour intervals. The data generated are normalized as per the time point when the effector cells and MAbs/NKCE were added to the target cells and were analyzed using RTCA/RTCA Pro Software. Western blot analysis For validating the in vitro and in vivo expression of Siglec-7 MAbs, the supernatant collected after transfection of Expi 293F cells with the DNA encoding the antibodies or sera collected from mice after immunizing with the Siglec-7 DMAbs, were heat inactivated, reduced, and loaded with Odyssey Protein Molecule Weight (LI-COR). Following electrophoresis, samples were transferred onto polyvinylidene fluoride (PVDF) membranes via an iBlot-2 system (Thermo Fisher Scientific) and blocked using Odyssey Blocking Buffer (LI-COR). The heavy and light chains were detected using goat anti-human secondary antibody (LI-COR). The expression of Bispecific T and NK cell engagers were detected using goat anti human IgG F(ab’)2 (Jackson ImmunoResearch Laboratories Inc) followed by donkey anti-goat antibody (LICOR). Immunofluorescence (IFA) analysis Siglec-7 transduced HEK 293T cells were seeded in 2-well chamber slides and allowed the cells to adhere overnight. The cells were permeabilized using 0.5% Triton 100 in PBS followed by blocking using 5 % goat serum. Following this, bispecific NKCE was added and incubated overnight at 4°C. Subsequently, the slides were incubated with goat anti-human H+L (Texas Red conjugated) secondary antibodies. Nuclear staining was done with 4′, 6-diamidino-2-phenylindole (DAPI). The samples were mounted onto glass slides with the help of Fluoroshield mounting medium (Invitrogen) and then observed using a Leica TCS SP8 WLL scanning laser confocal microscope. Tumor challenges NOD/SCID-γ (NSG) mice were challenged with OVCAR3-FSHR cells. NSG mice were injected with 3x10 ⁶ FSHR expressing OVCAR3 or OVCAR3-FSHR cells on the right flank subcutaneously. After 3 days, when the tumor became palpable, mice were inoculated with pVax1 (100 μg), or DDAP-NKCE (100 μg). The same day when expression vector was given, 10x10 ⁶ PBMCs were injected intraperitoneally into each mouse. The mice were inoculated with DNA twice, one week apart and tumor sizes were monitored periodically. Mice were euthanized upon developing signs of graft versus host disease (GVHD). Tumor volume (V) was calculated as per the formula V = [(length Xwidth2)]/2; width is the side with smaller measurement. For Siglec-7 DMAb challenge, NOD/SCID-γ (NSG) mice were challenged with OVISE cells (0.8 x10 ⁶ ). After 10 days, when the tumor became palpable, mice were inoculated with DB7.2 DMAb (50 μg +50 μg; HC+LC), or pVax1 (100 μg) followed by intraperitoneal injection of 10x10 ⁶ PBMCs into each mouse. The same procedure was followed henceforth. Animal experiments were approved by the Institutional Animal Care and Use Committee at The Wistar Institute. Statistical analysis All statistical analyses were done using Graph Pad Prism. A p-value < 0.05 was considered statistically significant. Differences between the means of experimental groups were calculated using a two-tailed unpaired Student’s t test or one- way ANOVA where more than two quantitative variables were measured. Error bars represent standard error of the mean. Comparisons between tumor size at each time point were done using two-way ANOVA with Fisher’s least significant difference (LSD) test. The Experimental Results are now described. In vitro expression of Siglec-7 MAbs and specificity evaluation To assess the potential for Siglec-7 blockade as an NK cell activation strategy, MAbs specific against human Siglec-7 were recently generated and their biological activity was studied in vitro. Here, codon and RNA optimized antibody expression cassettes of potent Siglec-7 binders were generated and assembled into DNA vectors optimized for expression of human IgG1. These HC & LC individual combinations are designated as DB7.1 (DB-S7-1), DB7.2 (DB-S7-2) and DB7.7 (DB-S7- 7) respectively (Figure 21A). Expression was studied in vitro by transfecting expi293F cells with the synthetic human Siglec-7 DNA vectors by Western blot analysis. These studies identify bands corresponding to the heavy and light antibody chains of the expressed antibodies in the transfected Expi293F supernatant but not in the empty vector transfected control wells (Figure 21B). The in vitro expression of DB7.1, DB7.2 and DB7.7 was further confirmed by ELISA quantification (Figure 21C). DB7.1, DB7.2 and DB7.7 Siglec-7 MAbs showed specific and dose dependent binding to recombinant human Siglec-7 analyzed by ELISA (Figure 22A). HEK293T cells were stably transduced for Siglec-7 expression and those cells (HEK293T-Siglec7 cells) were used for evaluation of binding by Siglec-7 MAbs. As shown in Figure 22B, DB7.1, DB7.2 and DB7.7 showed specific binding to HEK293T-Siglec-7 cells. The most potent binder DB7.2 was further analyzed for binding in PBMCs from multiple donors (n=4) (Figure 23). DB7.2 bound predominantly to human NK cells (~90%) whereas lower levels of binding were observed in case of CD8+ T and CD4+ T cells (Figure 22C&D). Binding of DB7.2 to innate lymphoid cells (ILCs) (~9%) was observed which may be considered as the innate counterparts of CD4+ T helper 1 (TH1), TH2, and TH17 cells (Eberl et al., 2015, Science 348, aaa6566). Additionally, DB7.2 showed >25% binding to mucosal- associated invariant T (MAIT) cells, which play important role in the immune defense against microbial infections in mucosal barriers and serve as innate sensors of inflammation and viral infection (Parrot et al., 2020, Sci Immunol 5; Legoux et al., 2020, Immunity 53, 710-723). Additional study of the minor T cell populations that express Siglec-7 are important for further study. Interestingly, DB7.2 MAb stained both CD56dim and CD56bright NK cell subsets suggesting its ability to bind the bulk of human NK populations (Figure 22E). DB7.2 also demonstrated strong binding to human Siglec-7 protein in Western blot (Figure 24A) as well as analyzed their binding in surface plasmon resonance (SPR) analysis. DB7.2 anti-Siglec-7 antibody exhibited a KD value of 44 pM as determined using a titration of indicated concentrations of anti-Siglec-7 and a maximum point on the sensorgram signifying saturation of the recombinant human Siglec-7 protein. Besides high affinity, high specificity of DB7.2 (Koff: 10-M) was also observed in the Surface Plasmon Resonance (SPR) assay (Figure 24B-D). Siglec-7 MAbs induced potent and specific killing of target ovarian cancer cells in vitro To evaluate the Siglec-7 genetically optimized MAbs ability to activate human peripheral blood NK cells against human cancer lines, a diverse panel of human ovarian cancer cells was assembled (Table 1)( Bordoloi et al., 2022, JCI Insight 7), using HaCaT (human Keratinocyte cells) as a Siglec-7 negative control. Importantly, DB7.1, DB7.2 and DB7.7 did not induce killing of HaCaT cells (Figure 25 A&B). Next the ability of the MAbs to drive killing of defined human OC cells (OVISE, TOV-21G, OVCAR3, CaOV3, OVCAR10 and PEO-4) was examined with different disease phenotypes and mutations (Table 1) in the presence of human PBMC/NK cells. While all the three clones induced killing of all four OC targets (Figure 25C-G), clone DB7.2 exhibited the highest potency in these assays. DB7.2 displayed enhanced killing induction against two additional OC lines, CaOV3 (Figure 25H) and OVCAR3 (Figure 25I) cells. To confirm Siglec-7 MAb activity independence of Fc receptor binding it was found that (Figure 26A) DB7.2 potency was maintained in the presence of Fc blockade (Figure 26 B&C). Next, residue modification of the Fc of antibody was performed to eliminate Fc engagement and potential off target effects. A variant of DB7.2 was designed which contain multiple residue modifications (“TM”; L234F/ L235E/ P331S) in the Fc domain to ablate FcR and complement (C1q) binding (Oganesyan et al., 2008, Acta Crystallogr D Biol Crystallogr 64, 700-704; Parzych et al., 2022, Nat Commun 13, 5886), designated as DB7.2_TM Mod. The killing efficacy of DB7.2_TM Mod was maintained in OVISE cells (Figure 27A). Post-24 h addition of DB7.2_TM Mod to OVISE cells in presence of human PBMCs resulted in potent killing of target cells, but not against the control (Figure 27B) cell targets. DB7.2 and DB7.2_TM Mod exhibited comparable IC50 values of; 82.67 and 192 nM respectively in OVISE cells (Figure 27 C&D). Together, these studies illustrate the Siglec-7 MAbs’ specificity for activating immune killing and its ability to target OC cells. Combination of anti PD-1 with DB7.2 MAbs demonstrate enhancement of OC killing using xCELLigence assays OC is one of the subsets of cancers with modest responses to the existing immune checkpoint blockade therapy with objective response rate (ORR) of ~8–9%. OC patients receiving checkpoint inhibitors (CPIs) reported infrequent durable responses and there are no FDA approved CPIs for the management of OC so far (Farkkila et al., 2020, Nat Commun 11, 2543). However, evidence suggests that combinatorial methods might prove important to optimize EOC patient response to immunotherapy. Without being bound by theory, it was hypothesized that the combination of T cell activating PD-1 with activation of NK cells by Siglec-7 MAb’s could synergistically target tumors more efficiently. To test this hypothesis for simultaneous targeting of PD-1 for T cells and for engaging NK immune pathways; antibody combinations of DB7.2 and anti-PD1 (Pembrolizumab) were studied in xCELLigence assays targeting OC tumors. DB7.2 showed the ability to simulate killing against both BRCA2 mutated and PARPi resistant PEO4 cells with an EC5068.87 nM (Figure 27E&G), whereas anti-PD1 targeted PEO4 cells with an 10x lower EC50680 nM (Figure 27F&H) in xCELLigence based in vitro killing assays. The combination of anti PD-1 with DB7.2 showed further enhancement of PEO4 cell killing in the presence of human PBMCs (Figure 27I). These data illustrate that the combination of Siglec-7 MAb and anti-PD1 (NK and T cell CPIs) enhances anti- tumor immunity. In vivo expression of Siglec-7 MAbs reduces tumor progression in an ovarian cancer challenge model Next, the in vivo expression of the Siglec-7 MAb clones was examined using a DNA delivery in vivo approach. To that end mice were injected with DNA expression cassettes for the MAb (Patel et al., 2018, Cell Rep 25, 1982-1993 e1984) at a dose of 50 μg + 50 μg (HC+LC) in a two-plasmid system for each anti-Siglec-7 clone (DB7.1, DB7.2 and DB7.7) along with empty vector control (pVax1) allowing for biologic antibody production of mAb in vivo. Injections were performed into the tibialis anterior muscle of mice on Day 0 as previously described (Parzych et al., 2022, Nat Commun 13, 5886; Patel et al., 2018, Cell Rep 25, 1982-1993 e1984) (Figure 28A). The presence of human IgG in sera from the DB7.1, DB7.2 and DB7.7 Siglec-7 MAbs’- injected mice was observed, and no expression was detected in control animals or in the pre bled mice sera. To confirm the specificity of the inivo generated antibodies, human NK cells were stained using Day 14 sera obtained from mice inoculated with either DB7.1, DB7.2, and DB7.7 vs sera from empty vector control delivered animals. Day 14 sera from all the three groups positively stained human NK cells, whereas staining was not observed in case of pVax1 or irrelevant antibody controls (Figure 28B). To examine the potential anti-tumor potency of Siglec-7 MAb delivery in animals, an NSG-K (NOD/SCID- γ-MHC I/II double knockout mutant) mouse tumor challenge model was employed in which OVISE human ovarian cancer cells (0.8x10 ⁶ cells/mouse) were injected and tumor growth was monitored prospectively. When tumors reached an average size of >50 mm3, 50 μg + 50 μg (HC+LC) of DB7.2 or pVax1 vector control was delivered in the muscle as described (Parzych et al., 2022, Nat Commun 13, 5886; Patel et al., 2018, Cell Rep 25, 1982-1993 e1984) together with 10 million human PBMCs per each mouse (Figure 28C). Mice receiving DB7.2 Siglec-7 MAb exhibited a significant decrease in the tumor burden/delay in tumor growth compared to the vector control (Figure 28D, Figure 29). Notably, The Siglec-7 MAb significantly enhanced the median survival of tumor bearing mice (Figure 28E). These data provide the first in vivo data demonstrating the potential of Siglec-7 antibodies for direct treatment of human ovarian cancers. Generation and expression of DB7.2xD2AP11 DNA encoded bispecific NK cell engager NK engagers are an important new focus for targeting tumor cells (Gleason et al., et al., 2014, Blood 123, 3016-3026; Ibarlucea-Benitez et al., 2021, Proc Natl Acad Sci U S A 118; Demaria et al., 2021, Eur J Immunol 51, 1934-1942). Based on the potency of the anti Siglec-7 MAbs to enhance NK activity against OC, as described above, the potential of this target was considered as new targeted NKCE approach. Without being bound by theory, it was hypothesized that this approach would not only allow for specific targeting of NK cells, but also prevent their receiving negative TME signals, resulting in a novel NKCE. Therefore, to enhance targeting tumors using NK cell specific Siglec-7 engagement, a NKCE was constructed in the format of two linked antibody binding fragment (scFVs) arranged to bind to the OC antigen FSHR as recently described (Bordoloi et al., 2022, JCI Insight 7) linked to anti Siglec-7 FV. An NKCE fusion sequence was designed encoding the scFV of DB7.2 anti-Siglec-7 antibody with the scFV of anti-FSHR (Clone D2AP11)( Bordoloi et al., 2022, JCI Insight 7) (Figure 30A) incorporating a GS (Glycine-Serine) flexible linker (Perales-Puchalt et al., 2019, JCI Insight 4; Pratik et al., 2022, Molecular therapy Oncolytics). In vitro analysis showed the DB7.2xD2AP11 NKCE was efficiently expressed as through transfection of Expi293F cells, production of an expected ~55 KDa molecule was observed (Figure 30B). This NKCE binds to both cellular targets by flow staining on Siglec-7 or FSHR overexpressing HEK293T (Figure 30C) or K562 (Figure 30D) cells, respectively. To visualize the binding to human Siglec-7, high resolution confocal imaging of 293T- Siglec-7 fixed cells were performed. Cells were labeled with DAPI (nuclei), GFP (Siglec- 7) and Texas Red (DB7.2xD2AP11). DB7.2xD2AP11 NKCE demonstrated clear surface binding to GFP+ cells expressing human Siglec-7, but not in the secondary antibody control (Figure 30E). FSHR targeted novel NK cell engager induces potent killing in multiple ovarian tumor lines and decreased tumor burden in vivo Next, the DB7.2xD2AP11 NK cell engager (NKCE) was evaluated for induction of tumor killing in vitro using the xCelligence RTCA assay format. The effector cells include testing of PBMC as well as NK cells directly. The NKCE were added a day after the plating of target OC cells. As controls, four FSHR negative cell lines were studied, including HEK 293T cells (Urbanska et al., 2015, Cancer Immunol Res 3, 1130-1137), AGS human gastric cancer cells, GM05389 human fibroblast cells and WM3743 human melanoma cells. Off target killing was not observed against these FSHR-negative cells (Figure 30 F-K) including irrelevant cancer cells. As shown in Figure 30G&J, HEK293T and AGS cells remained healthy and adherent through 3 days of treatment with DB7.2xD2AP11 NKCE in the presence of human PMBCs. In contrast, multiple FSHR expressing ovarian tumor lines OVISE, OVCAR3-FSHR, CaOV3, Kuramochi-FSHR and PEO-4 (Figure 31A-G) were efficiently killed by human PBMCs in the presence of DB7.2xD2AP11 NKCE. As an additional specificity control, purified human NK cells were directly used as effector cells. DB7.2xD2AP11 NKCE co- incubated with human NK cells also effectively killed OVCAR3-FSHR cells (Figure 32A). The specificity of this bispecific engaging approach was confirmed on FSHR negative AGS cells; here anti-Siglec-7 antibody mediated killing of AGS cells (Figure 32B), but not the DB7.2xD2AP11 NKCE (Figure 30I). As a further specificity control, a non FSHR targeting NKCE (IL13Rα2-NKCE) was developed and it was observed that it did not drive toxicity in FSHR overexpressing OVCAR3 or against OVISE cells (Figure 32C&D). DB7.2xD2AP11 NKCE induced concentration dependent cytolysis in both OVISE-FSHR (in separate experiments using PBMCs from 3 different human donors) and OVCAR3 cells showing EC50 values of 142.87 pM and 236.6 pM respectively, supporting the significant potency of this engager tool for targeting pathogenic cells as a novel NKCE (Figure 31H&I; Figure 33 and Figure 34). The cytokine/cytotoxic molecule secretion profile of the OC – NKCE was examined. Coculture of OVCAR3-FSHR cells and human PBMCs and DB7.2xD2AP11 NKCE (Figure 35A) generated enhanced production of soluble Fas (sFas) and Granzyme A as part of the specific immune activation, with decreased levels of IL-10 observed, compared to No Ab control or empty vector control groups (Figure 35B), supporting a more effector-based activation. To directly evaluate the in vivo antitumor effects of DB7.2xD2AP11 NKCE, NSGK mice were challenged with OVCAR3-FSHR cells. NSG-K mice were administered 3 million OVCAR3-FSHR cells and 7 days after tumor implantation, they were treated for in vivo expression using nucleic acid encoded DB7.2xD2AP11(100 μg) or empty vector; pVax1 (100 μg), twice at two weeks apart. On day 7, they were also inoculated with 10 million human PBMCs, and tumor volumes were measured periodically (Figure 35C). Therapy with the NKCE led to the significantly decreased tumor burden in OVCAR3-FSHR tumor bearing mice, while no such impact was observed in the control treated group (Figure 35D). Further, DB7.2xD2AP11 NKCE treatment enhanced survival (Figure 35E), supporting further studies of this approach. Example 4: Siglec 7 antibody clones’ sequences (CDR sequences underlined) DB-S7-1 Heavy chain DB-S7-1 Heavy chain DB-S7-1 Light chain DB-S7-1 Light chain DB-S7-2 Heavy chain DB-S7-2 Heavy chain DB-S7-2 Light chain DB-S7-2 Light chain DB-S7-3 Heavy chain DB-S7-3 Heavy chain DB-S7-3 Light chain DB-S7-3 Light chain DB-S7-6 Heavy chain DB-S7-6 Heavy chain DB-S7-6 Light chain DB-S7-6 Light chain DB-S7-7 Heavy chain DB-S7-7 Heavy chain DB-S7-7 Light chain DB-S7-7 Light chain DB-S7-8 Heavy chain DB-S7-8 Heavy chain DB-S7-8 Light chain DB-S7-8 Light chain

DDAP-NKCE (Nucleotide Sequence) SEQ ID NO: 97

DDAP-NKCE (Protein Sequence) SEQ ID NO: 98 IL13Ra2-Siglec 7 NK cell engager (Nucleic Acid Sequence) (No his tag) SEQ ID NO: 99

IL13Ra2-Siglec 7 NK cell engager (Protein Sequence) (No His tag) SEQ ID NO: 100 IL13Ra2-Siglec 7 NK cell engager (Nucleic Acid Sequence) (His tag) SEQ ID NO: 101 IL13Ra2-Siglec 7 NK cell engager (Protein Sequence) (His tag) SEQ ID NO: 102 The disclosures of each and every patent, patent application, and publication cited herein are hereby incorporated herein by reference in their entirety. While this invention has been disclosed with reference to specific embodiments, it is apparent that other embodiments and variations of this invention may be devised by others skilled in the art without departing from the true spirit and scope of the invention. The appended claims are intended to be construed to include all such embodiments and equivalent variations.