Targeted nanoparticles and their uses in cancer

Abstract

Provided herein are cancer-targeted nanoparticles for the treatment or prevention of cancer.

Description

[0001]PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) TARGETED NANOPARTICLES AND THEIR USES IN CANCER CROSS-REFERENCE TO RELATED APPLICATIONS This application claims the benefit of U.S. Provisional Application No. 63 / 568,712, filed March 22, 2024, and U.S. Provisional Application No.63 / 677,199, filed July 30, 2024. The above-listed applications are hereby incorporated herein by this reference in their entireties. STATEMENT REGARDING FEDERALLY FUNDED RESEARCH This invention was made with government support under grant number AI62989 awarded by the National Institutes of Health. The government has certain rights in the invention. BACKGROUND Cancer is the leading cause of death around the globe accounting for about 15% of all deaths in 2020. In the U.S. ~600,000 people die of cancer every year (CDC). In 2024, the United States is facing an alarming rise in cancer incidence, set to surpass 2 million new cases. Prostate, breast, endometrial, pancreatic, kidney, and melanoma cancers contribute to this surge. SUMMARY Provided herein are cancer-targeting nanoparticles for the treatment or prevention of cancer. In some embodiments, the nanoparticles comprise a C-type lectin receptor or a fragment thereof that is coupled to the surface of the nanoparticle, wherein the C-type lectin receptor or a fragment thereof binds an antigen expressed by a cancer cell. In some embodiments, the anticancer agent is encapsulated in the nanoparticle. In some embodiments, the C-type lectin receptor or fragment thereof is coupled to the surface of the nanoparticle by inserting the C-type lectin receptor or fragment thereof into the surface of the nanoparticle. In some embodiments, the C-type lectin receptor or fragment thereof is coupled to the surface of the nanoparticle by attaching the C-type lectin receptor or fragment thereof to the surface of the nanoparticle. In some embodiments, the C-type lectin receptor or fragment thereof is selected from the group consisting of Dectin-1 or a fragment PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) thereof, Dectin-2 or a fragment thereof, Dectin-3 or a fragment thereof, and DC-SIGN or a fragment thereof. In some embodiments, the C-type lectin receptor or a fragment thereof is a soluble C- type lectin receptor or a fragment thereof. In some embodiments, the soluble C-type lectin receptor or a fragment thereof is a soluble human Dectin-1 comprising an amino acid sequence having at least 85%, 90%, 95%, or 99% identity to SEQ ID NO: 1, or a fragment thereof and is not a full-length Dectin-1 protein. In some embodiments, the soluble human Dectin-1 comprises SEQ ID NO: 1 or a fragment thereof and is not a full-length Dectin-1 protein. In some embodiments, the soluble C-type lectin receptor or a fragment thereof is a soluble human Dectin-2 comprising an amino acid sequence having at least 85%, 90%, 95%, or 99% identity to SEQ ID NO: 2, or a fragment thereof and is not a full-length Dectin-2 protein. In some embodiments, the soluble human Dectin-2 comprises SEQ ID NO: 2 or a fragment thereof and is not a full-length Dectin-2 protein. In some embodiments, the soluble C-type lectin receptor or a fragment thereof is a soluble human Dectin-3 comprising an amino acid sequence having at least 85%, 90%, 95%, or 99% identity to SEQ ID NO: 3, or a fragment thereof and is not a full-length Dectin-3 protein. In some embodiments, the soluble human Dectin-3 comprises SEQ ID NO: 3 or a fragment thereof and is not a full-length Dectin-3 protein. In some embodiments, the C-type lectin receptor fragment is a soluble C-type lectin receptor fragment, wherein the soluble C-type lectin receptor fragment is not a full-length C- type lectin receptor, and wherein the C-type lectin receptor fragment comprises an amino acid sequence having at least 65%, 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 10, SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 16, SEQ ID NO: 18, SEQ ID NO: 41, SEQ ID NO: 42, SEQ ID NO: 43, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46, SEQ ID NO: 47 or SEQ ID NO: 48. In some embodiments, the C-type lectin receptor comprises a Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Non-integrin (DC-SIGN) polypeptide or a fragment thereof. In some embodiments, the DC-SIGN polypeptide is not a full-length DC- SIGN polypeptide. In some embodiments, the C-type lectin receptor fragment comprises a carbohydrate recognition domain (CRD). In some embodiments, the DC-SIGN polypeptide comprises a DC-SIGN CRD (SEQ ID NO: 21) and one or more neck regions of DC-SIGN selected from the group consisting of (NR1) SEQ ID NO: 22, (NR2) SEQ ID NO: 23, (NR3) SEQ ID NO: 24, (NR4) SEQ ID NO: 25, (NR5) SEQ ID NO: 26, (NR6) SEQ ID NO: 27, PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) (NR7) SEQ ID NO: 28 and (NR8) SEQ ID NO: 29. In some embodiments, the DC-SIGN polypeptide comprises a DC-SIGN CRD (SEQ ID NO: 21), NR1 (SEQ ID NO: 22) and NR2 (SEQ ID NO: 23). In some embodiments, the DC-SIGN polypeptide has at least 90% identity to SEQ ID NO: 32. In some embodiments, the DC-SIGN polypeptide comprises a DC-SIGN CRD (SEQ ID NO: 21), NR7 (SEQ ID NO: 28) and NR8 (SEQ ID NO: 29). In some embodiments, the DC-SIGN polypeptide has at least 90% identity to SEQ ID NO: 30. In some embodiments, the DC-SIGN CRD (SEQ ID NO: 21) and the one or more neck regions are joined with one or more linkers. In some cancer-targeting nanoparticles, the concentration of the anticancer agent is reduced as compared to the concentration of the anticancer agent in a nanoparticle that does not comprise a C-type lectin receptor or a fragment thereof coupled to the surface of the nanoparticle. In some embodiments, the antigen is a tumor-specific antigen. In some embodiments, the tumor-specific antigen is solid tumor antigen. In some embodiments, the solid tumor antigen is a breast tumor antigen, a prostrate tumor antigen or a lung tumor antigen. In some embodiments, the tumor-specific antigen is a glycan. In some embodiments, the cancer-targeting nanoparticle is a liposome. Further provided is a nanoparticle comprising: (a) a C-type lectin receptor or fragment thereof that binds an antigen on a cancer cell; and (b) a signal-generating molecule, wherein the C-type lectin receptor or fragment thereof is coupled to the surface of the nanoparticle and the signal-generating molecule generates a signal when the C-type lectin receptor or fragment thereof binds the antigen on the cancer cell. In some embodiments, the C-type lectin receptor or fragment thereof is selected from the group consisting of Dectin-1 or a fragment thereof, Dectin-2 or a fragment thereof, Dectin- 3, and DC-SIGN or a fragment thereof. In some embodiments, the signal-generating molecule is linked to the C-type lectin receptor or fragment thereof. In some embodiments, the C-type lectin receptor or a fragment thereof is a soluble C-type lectin receptor or a fragment thereof. In some embodiments, the soluble C-type lectin receptor or a fragment thereof is a human Dectin-1 comprising an amino acid sequence having at least 85%, 90%, 95%, or 99% identity to SEQ ID NO: 1, or a fragment thereof. In some embodiments, the soluble human Dectin-1 comprises SEQ ID NO: 1 or a fragment thereof. In some embodiments, the soluble C-type lectin receptor or a fragment thereof is a soluble human Dectin-2 comprising an amino acid sequence having at least 85%, 90%, 95%, or 99% identity to SEQ ID NO: 2, or a fragment thereof. In some embodiments, the soluble human Dectin-2 comprises SEQ ID NO: 2 or a PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) fragment thereof. In some embodiments, the soluble C-type lectin receptor or a fragment thereof is a soluble human Dectin-3 comprising an amino acid sequence having at least 85%, 90%, 95%, or 99% identity to SEQ ID NO: 3, or a fragment thereof. In some embodiments, the soluble human Dectin-3 comprises SEQ ID NO: 3 or a fragment thereof. In some embodiments, the C-type lectin receptor comprises a Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Non-integrin (DC-SIGN) polypeptide or a fragment thereof. In some embodiments, the DC-SIGN polypeptide comprises a DC-SIGN CRD (SEQ ID NO: 21) and one or more neck regions of DC-SIGN selected from the group consisting of (NR1) SEQ ID NO: 22, (NR2) SEQ ID NO: 23, (NR3) SEQ ID NO: 24, (NR4) SEQ ID NO: 25, (NR5) SEQ ID NO: 26, (NR6) SEQ ID NO: 27, (NR7) SEQ ID NO: 28 and (NR8) SEQ ID NO: 29. In some embodiments, the DC-SIGN polypeptide comprises a DC- SIGN CRD (SEQ ID NO: 21), NR1 (SEQ ID NO: 22) and NR2 (SEQ ID NO: 23). In some embodiments, the DC-SIGN polypeptide has at least 90% identity to SEQ ID NO: 32. In some embodiments, the DC-SIGN polypeptide comprises a DC-SIGN CRD (SEQ ID NO: 21), NR7 (SEQ ID NO: 28) and NR8 (SEQ ID NO: 29). In some embodiments, the DC-SIGN polypeptide has at least 90% identity to SEQ ID NO: 30. In some embodiments, the DC-SIGN CRD (SEQ ID NO: 21) and the one or more neck regions are joined with one or more linkers. In some embodiments, the signal-generating molecule is incorporated into or attached to the surface of the nanoparticle. In some embodiments, the signal-generating molecule is a fluorescent dye or fluorescent polypeptide. In some embodiments, the C-type lectin receptor or fragment thereof is linked to the C-terminal and / or an N-terminal fragment of a fluorescent protein, an antibody or a fragment thereof or an enzyme. In some embodiments the cancer-targeting nanoparticles described herein are cancer- targeting liposomes. In some embodiments, the liposome comprises from about 40 to about 70 mole percent phosphatidylcholine relative to total lipid content. In some embodiments, the phosphatidylcholine is fully hydrogenated soy phosphatidylcholine (18:0-18:1 PC, 1-stearoyl- 2-oleoyl-sn-glycero-3-phosphocholine). In some embodiments, the liposome comprises about 20% to 50% mole percent cholesterol relative to total lipid content. In some embodiments, the liposome comprises about 1 to about 6 mole percent polyethylene glycol (PEG) relative to total lipid content. In some embodiments, the PEG is mPEG-2000-DSPE (18:0 PEG2000 PE) (sodium;[(2R)-2,3-di(octadecanoyloxy)propyl] 2-(2-methoxyethoxycarbonylamino)ethyl phosphate). In some embodiments, the liposome comprises about 5 to 25 mole percent anti- cancer agent relative to total lipid content. In some embodiments, the liposome comprises about PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) 0.3 to about 1.2 mole percent C-type lectin receptor or a fragment thereof relative to total lipid content. Also provided are pluralities of any of the cancer-targeting nanoparticles described herein. Further provided is a pharmaceutical composition comprising any of the pluralities of nanoparticles described herein. Uses of the pharmaceutical compositions for the treatment of cancer are also provided. Also provided is a method of treating or preventing cancer in a subject comprising administering to the subject having cancer or at risk of developing cancer an effective amount of a plurality of cancer-targeting nanoparticles described herein. Further provided is a method of treating or preventing cancer in a subject comprising administering to the subject having cancer or at risk of developing cancer, any of the pharmaceutical compositions described herein. In some embodiments, the subject has breast cancer, prostate cancer or lung cancer. In some methods, a second therapeutic agent or therapy is administered to the subject. In some methods, the second therapy is surgery, a second anticancer agent, and / or radiation. In some methods, the second therapeutic agent is a second anticancer agent. In some embodiments, the anticancer agent is a drug, a peptide or an antibody. In some embodiments, the drug is a chemotherapeutic drug. In some embodiments, the chemotherapeutic drug is doxorubicin. Also provided is a method for detecting cancer in a subject or a sample from a subject comprising: (a) contacting the subject or a sample from the subject with the plurality of any of the nanoparticles comprising a C-type lectin receptor or fragment thereof that binds an antigen on a cancer cell; and a signal-generating molecule, and (b) detecting a signal, wherein a signal indicates the presence of cancer. In some embodiments, the signal is a fluorescent signal. In some embodiments, the signal is directly or indirectly detected. DESCRIPTION OF THE FIGURES The present application includes the following figures. The figures are intended to illustrate certain embodiments and / or features of the compositions and methods, and to supplement any description(s) of the compositions and methods. The figures do not limit the scope of the compositions and methods, unless the written description expressly indicates that such is the case. FIG.1 is a schematic of a Dectin-2 (DEC2)-targeted doxorubicin (DOX) loaded lipid nanoparticle, DEC2-DOX-LL, shown binding to a cognate glycoprotein ligand on the surface of a HR-negative breast cancer cell. In this exemplary liposome, a DOX-loaded liposome is PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) coated with the glycan recognition domain and stalk region of Dectin-2. The Dectin-2 monomers (purple) are tethered to the liposome via the DSPE moiety of a DEC2-PEG-DSPE conjugate. They float freely on the liposomal membrane and form dimers as they bind cognate ligands. The liposomes are also coated with red fluorescent rhodamine B (red star) via a DHPE moiety to monitor their binding to cells. The crystal structure of DOX (also red) is shown inside of the liposome. In one proposed iteration, the mole percent ratios of liposomal lipid:Dectin- 2:rhodamine B:DOX are 100:1:2:16, respectively. FIGS. 2A-H shows that exemplary Dectin-1, -2 and -3 coated liposomes (DEC1-Ls, DEC2-Ls and DEC3-Ls, respectively) bound specifically and quantitatively to triple negative breast cancer cell line MDA-MB-231, while untargeted control liposomes did not. A. In this experiment, DCSIGN DCS12-Ls did not bind significantly. However, this was likely due to a defective preparation because, in subsequent replicate experiments with a different preparation, the DCS12-Ls did bind to these cells. B, C, & D. Representative images show the strong binding of red fluorescent DEC1-Ls, DEC2-Ls and DEC3-Ls to MBA-MB-231. E & F. No significant binding was detected for two untargeted liposome controls. The liposomal protein concentration during staining for the five protein coated liposomes was 1 ug / 200 uL. A-F.10X magnification. G. A scatter bar plot quantifies the area of red fluorescent liposome binding. Fold increases and P values relative to BSA-Ls are indicated. N=10 randomly selected images were quantified for each bar. Zero pixel values for some images were set to 5 pixels so these values could be plotted on a log scale and p values estimated. H. At higher magnification surface patches DEC2-L binding are revealed. Cell nuclei were stained with Hoechst and images show combined blue and red fluorescence. FIGS. 3A-G show that exemplary Dectin-2, Dectin-2 and Dectin-3 coated liposomes DEC1-Ls, DEC2-Ls and DEC3-Ls bind efficiently to the prostate cancer cell line PC3, which was derived from a prostate bone marrow adenocarcinoma. Representative images reveal CTL targeted liposome bound to in vitro grown cells. A. In this experiment, DCSIGN DCS12-Ls did not bind. B, C, D. DEC1-Ls, DEC2-Ls and DEC3-Ls bound very efficiently. E & F. No binding was detected for two untargeted liposome controls, BSA-Ls or uncoated Ls. The liposomal protein concentration during staining for the five protein coated liposomes was 1 ug / 200 uL. G. A scatter bar plot quantifies the area of red fluorescent liposome binding in pixels and p values relative to the BSA-L controls are indicated. N=10 randomly photographed images quantified for each bar. Photographs were taken at 10X magnification, combining phase & red fluorescence. Zero red pixel values were set to 5 pixels to allow log10plotting of data. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) FIGS.4A-G shows that exemplary DEC1-Ls, DEC2-Ls and DEC3-Ls bound efficiently to the lung cancer cell line A549 cell line, which was derived from a lung carcinoma. A,B,C,D. Representative images of CTL targeted liposome binding in vitro. A. in this experiment, DCSIGN DCS12-Ls did not bind. B, C, D. DEC1-Ls, DEC2-Ls and DEC3-Ls bound efficiently. E & F. No significant binding was detected for two untargeted liposome controls, BSA-Ls or uncoated Ls. The liposomal protein concentration during staining for the five protein coated liposomes was 1 ug / 200 uL. G. A scatter bar plot quantifies the area of red fluorescent liposome binding in pixels and p values relative to the BSA-L controls are indicated. N=10 randomly photographed images quantified for each bar. Cell nuclei were stained with Hoechst. Photographs were taken at 10X magnification, combining blue & red fluorescence. Zero red pixel values were set to 5 to allow p-value estimates and log10plotting of data. FIGS. 5A-G show that binding to artificially immortalized human kidney embryonic HEK293T control cells was relatively weak and of low statistical significance. A,B,C,D. Representative images of Dectin and DC-SIGN targeted liposome binding in vitro. A. In this experiment, DCSIGN DCS12-Ls did not bind significantly. B, C, D. DEC1-Ls, DEC2-Ls and DEC3-Ls bound inefficiently and with little or no statistical significance, when compared to BSA-Ls. E & F. Little binding was detected for two untargeted liposome controls, BSA-Ls or uncoated Ls. The liposomal protein concentration during staining for the five protein coated liposomes was 1 ug / 200 uL. Zero red pixel values set to 5 pixels to allow the data to be plotted on a log scale and p values estimated. G. A scatter bar plot quantifies the area of red fluorescent liposome binding in pixels and p values relative to the BSA-L controls are indicated. N=10 randomly photographed images quantified for each bar. Photographs were taken at 10X magnification, combining bright field & red fluorescence. A biological replicate produced a similar result. FIGS.6A-G show that exemplary DEC1-Ls, DEC2-Ls and DEC3-Ls bound efficiently and strongly to the triple positive breast cancer cell line MCF7. A,B,C,D. Representative images of CTL targeted liposome binding in vitro. A. In this experiment, DCSIGN DCS12-Ls did not bind significantly. B, C, D. DEC1-Ls, DEC2-Ls and DEC3-Ls bound efficiently and significantly when compared to BSA-Ls. E & F. Little binding was detected for two untargeted liposome controls, BSA-Ls or uncoated Ls. The liposomal protein concentration during staining for the five protein coated liposomes was 1 ug / 100 uL. G. A scatter bar plot quantifies the area of red fluorescent liposome binding in pixels and p values relative to the BSA-L PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) controls are indicated. N=10 randomly photographed images quantified for each bar using data from the red channel. Photographs were taken at 10X magnification, combining blue & red fluorescence. Zero red pixel values in some images were set to 5 to enable p-value estimates and log10 plotting. A biological replicate produced a similar result. Cell nuclei were stained with Hoechst. FIGS. 7A-C show cell killing of triple negative breast cancer cells by C-type lectin receptor targeted liposomes and DOX in the nucleus. MDA-MB-231 cells were treated with DOXIL® and DOXIL targeted by four different C-type lectin receptor polypeptides (CTLs) and assayed for metabolic activity after three days treatment. Liposomes delivered 10 μM (A) and 5 μM (B) Doxorubicin. Targeting with all four CTLs significantly improved the efficacy of DOXIL at killing cells showing that all four CTLS bind to and kill MDA-MB-231 cells. Scatter bar plots show the distribution of N=8 data points. Fold differences from DOXIL®treated samples and PMW(Mann Whitney) P values indicate the statistical significance. C. DOX’s intrinsic fluorescence was observed in the nucleus only 2 hr after one treatment with DEC1-DOXIL. FIGS. 8A-E show human DCIS-H samples in a BrCaProg3 tissue array stained with DEC2-DOX-LLs, DOX-LLs, and H&E. (A) DEC2-DOX-LL staining of DCIS-H tissue. (B) DOX-LL staining of DCIS-H tissue. (C) DEC2-DOX-LL staining of non-cancerous breast tissue with ductal morphology (NB-NC). The top row contains the merged red fluorescent liposome and blue, fluorescent DAPI stained images. The bottom row shows the red fluorescent liposome channel alone. Exposures in the red channel were at 100% light intensity for 220 msec and in the blue channel were at 22% light intensity for 5 msec. (D) H&E staining. A 100- micron size bar indicates the degree of magnification for all seven images. (E) Quantification of liposome binding. FIGS.9A-D show HuCAT292 patient TNBC tumor sections stained with DEC2-DOX- LLs, DOX-LLs, and H&E. (A) DEC2-DOX-LL staining of FFPE section of HuCAT292 tumor. (B) DOX-LL staining of HuCAT292 same tumor. (C) H&E staining of an adjacent section from the same tumor. The top row of A & B contains the merged red fluorescent liposome and blue, fluorescent DAPI stained images. The bottom row shows the red fluorescent liposome channel alone. (C) H&E staining. Imaging details are the same as in FIG. 8D. The quantification of the area of red fluorescent liposome staining. (N=9 to 10). Fold difference, P value, and bars showing standard errors are indicated. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) FIGS.10A-B show that DEC2-DOX-LLs labeled the metastatic triple negative breast cancer (TNBC) cell line MDA-MB-468 far more efficiently than untargeted DOX-LLs. Cells were grown in a 24-well plastic plate, washed, fixed with 4% formalin, washed in PBS and stored with azide at 4oC. Cells were washed, blocked, stained with liposomes and DAPI, and washed extensively in a liposome dilution buffer 4 (LDB4) (25 mM MES, 150 mM NaCl, 2.5 mM CaCl2, 0.1% BSA, ~ 1 mM fresh BME adjusted to pH 5.7 with NaOH + 1% BSA, (Feinberg et al. (2017), JBC, 292, 13402-13414)). Images were taken bottom up with a Revolve 20 PLAN Fluorite LWD LL Phase Ph1 N.A.0.45 lens WD 6.6 to 7.8 mm. Exposures were set at the level where some background fluorescence could be detected in cells of the DOX-LL- stained sample. Exposures were set with bright field light at 6% intensity and 10 msec exposure, TXRED red fluorescence channel at 100% intensity and 1,000 msec exposure, DAPI blue fluorescence channel at 22% and 50 msec exposure. These staining and photographic conditions allowed improved imaging of Dectin-2 targeted liposomes binding to cancer cells. FIGS.11A-B show that DEC2-DOX-LLs labeled the metastatic triple negative breast cancer (TNBC) cell line MDA-MB-231 far more efficiently than untargeted DOX-LLs. Staining and photographic conditions are provided in the legend for FIGS 10A-B. FIGS.12A-B show that DEC2-DOX-LLs labeled the metastatic HER2 overexpressing breast cancer cell line SKBR3 far more efficiently than untargeted DOX-LLs. Staining and photographic conditions are provided in the legend for FIGS 10A-B. FIGS. 13A-B show that DEC2-DOX-LLs labeled the metastatic non-small cell lung carcinoma (NSCLC) cell line A549 far more efficiently than untargeted DOX-LLs. Staining and photographic conditions are provided in the legend for FIGS 10A-B. FIGS. 14A-B show that DEC2-DOX-LLs label TNBC tissue within a TNBC patient tumor FFPE breast tissue section HuCAT292 far more efficiently than untargeted DOX-LLs. Formalin Fixed Paraffin Embedded HuCAT292 human female TNBC tumors sections mounted on a glass microscope slide were obtained from TissueArray. Tissue was deparaffinized by standard protocols and stored for no more than a day in PBS. TNBC morphology tissue cells stain with DEC2-DOX-LLs, but not with DOX-LLs. Cells were washed, blocked, stained with liposomes and DAPI, and washed extentively in a liposome dilution buffer 2 (LDB2) (pH 8.020 mM HEPES, 10 mM Triethanolamine, 150 mM NaCl, 10 mM CaCl2, pH 8.0) + 5% BSA + freshly added 1 mM beta-mercaptoethanol (BME) with 1% BSA). Images were top down through a coverslip with a Revolve 20 PLAN Apo N.A.0.8 short working distance WD 0.6 mm lens). Exposures were set with bright field light at 12% intensity PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) and 5 msec exposure, TXRED red fluorescence channel at 100% intensity and 250 msec exposure, DAPI blue fluorescence channel at 28% and 80 msec exposure. DETAILED DESCRIPTION The following description recites various aspects and embodiments of the present compositions and methods. No particular embodiment is intended to define the scope of the compositions and methods. Rather, the embodiments merely provide non-limiting examples that are at least included within the scope of the disclosed compositions and methods. The description is to be read from the perspective of one of ordinary skill in the art; therefore, information well known to the skilled artisan is not necessarily included. Articles “a” and “an” are used herein to refer to one or to more than one (i.e. at least one) of the grammatical object of the article. By way of example, “an element” means at least one element and can include more than one element. “About” is used to provide flexibility to a numerical range endpoint by providing that a given value may be “slightly above” or “slightly below” the endpoint without affecting the desired result. The use herein of the terms "including," "comprising," or "having," and variations thereof, is meant to encompass the elements listed thereafter and equivalents thereof as well as additional elements. Embodiments recited as "including," "comprising,” or "having" certain elements are also contemplated as "consisting essentially of and "consisting of those certain elements. As used herein, “and / or” refers to and encompasses any and all possible combinations of one or more of the associated listed items, as well as the lack of combinations were interpreted in the alternative (“or”). As used herein, the transitional phrase "consisting essentially of" (and grammatical variants) is to be interpreted as encompassing the recited materials or steps "and those that do not materially affect the basic and novel characteristic(s)" of the claimed invention. See, In re Herz, 537 F.2d 549, 551-52, 190 U.S.P.Q.461, 463 (CCPA 1976) (emphasis in the original); see also MPEP §2111.03. Thus, the term "consisting essentially of" as used herein should not be interpreted as equivalent to "comprising." Recitation of ranges of values herein are merely intended to serve as a shorthand method of referring individually to each separate value falling within the range, unless otherwise-Indicated herein, and each separate value is incorporated into the specification as if it were individually recited herein. For example, if a concentration range is stated as 1% to PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) 50%, it is intended that values such as 2% to 40%, 10% to 30%, or 1% to 3%, etc., are expressly enumerated in this specification. These are only examples of what is specifically intended, and all possible combinations of numerical values between and including the lowest value and the highest value enumerated are to be considered to be expressly stated in this disclosure. Nanoparticle Delivery of Anti-Cancer Agents Although nanoparticles have emerged as a technology for delivering therapeutic agents to cells, and some have been approved for clinical use, the translation of nanotechnology for targeting and treating cancer in human patients has been limited. As of 2023, less than twenty nanoparticle formulations have advanced for treating human patients with cancer, and most nanoparticle formulations were approved based on the altered toxicological profile of the therapeutic agent rather than their enhanced therapeutic efficacy (He et al., Acc Chem Res. 2019;52(9):2445–2461). In fact, poor delivery efficiency is one of the problems for translating nanomedicines (Chan “Principles of Nanoparticle Delivery to Solid Tumors,” BME Front 4: 0016 (2023). Wilhelm et al. (Nature Review Materials 16014(2016)) showed that less than 0.7% of administered nanoparticles are delivered to solid tumors. Most nanoparticles become trapped in nontumor organs, resulting in an insufficient drug dose delivered to the targeted site to elicit an effective response. In preclinical animal models, low delivery efficiency can be addressed by administering more nanoparticles to induce a therapeutic effect. However, this strategy could lead to adverse side effects in humans. The present disclosure provides cancer-targeted nanoparticles that overcome longstanding difficulties in cancer drug delivery. The cancer- targeted nanoparticles described herein can be used to specifically deliver an anti-cancer agent to cancer cells in a subject and / or enhance accumulation of the anti-cancer agent in the targeted cancer cells (e.g., in or on a tumor), while reducing side effects in the subject. By targeting nanoparticle drugs on or in tumor cells the drug is concentrated where needed while reducing exposure to non-target cells that may suffer unwanted toxicity from the drug. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) Nanoparticles Provided herein are nanoparticles for the diagnosis, treatment or prevention of cancer. As used throughout, nanoparticles can be, but are not limited to, lipid nanoparticles, for example, liposomes or non-liposomal lipid nanoparticles (for example, lipid nanoparticles with a non-aqueous core (LNPs)), dendrimers, polymeric micelles, nanocapsules or nanospheres, to name a few. In some embodiments, the nanoparticles described herein comprise a cancer- targeting molecule, for example, a polypeptide or a fragment thereof, that targets the nanoparticle to an antigen expressed on cancer cells. In some embodiments, the nanoparticle is a cancer-targeting nanoparticle comprising a C-type lectin receptor or a fragment thereof that is coupled to the surface of the nanoparticle, wherein the C-type lectin receptor or a fragment thereof targets an antigen expressed by a cancer cell. In some embodiments, the cancer-targeting molecule targets the antigen on a cancer cell by specifically or selectively binding to the antigen. As used herein, the terms specifically bind or selectively binds mean binding that is measurably different from a non-specific or non- selective interaction. Specific binding can be measured, for example, by determining binding of a molecule to a target antigen compared to binding of a control molecule. Specific binding can be determined by competition with a control molecule that is similar to the target antigen, such as an excess of non-labeled target antigen. In that case, specific binding is indicated if the binding of the labeled target to a probe is competitively inhibited by the excess unlabeled target antigen. In some embodiments, the target antigen is a cell surface antigen, for example, a tumor- specific antigen (e.g., a tumor-specific protein or a tumor-specific glycan). In some embodiments, the tumor-specific protein or tumor-specific glycan is a solid tumor antigen, for example, and not to be limiting, a breast tumor antigen, a prostrate tumor antigen or a lung tumor antigen. As used herein, a tumor specific antigen is a protein or other molecule (for example, a glycan) that is found only on cancer cells and not found to any appreciable extent on normal cells. In some embodiments, the tumor specific antigen is involved in neoblastic transformation of cells. As used throughout, by “coupling” is meant that a cancer-targeting molecule, for example, a C-type lectin receptor or a fragment thereof, is incorporated into the outer surface of the nanoparticle or attached to the nanoparticle. For example, a C-type lectin receptor or fragment thereof can be incorporated into the surface (e.g., the outer bilayer) of a liposome or attached to a liposome. Incorporation can occur by insertion or intercalation of the cancer- PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) targeting molecule, e.g., a C-type lectin receptor or a fragment thereof, into the lipid bilayer. Attachment to a liposome can occur, for example, by affinity to a molecule incorporated into the outer lipid bilayer of the liposome. In some cases, the liposome can be coated with biotin (for example, DSPE-PEG-biotin inserted into the lipid bilayer) and the C-type lectin receptor or a fragment thereof linked to streptavidin. In other embodiments, the C-type lectin receptor or a fragment thereof can be linked or conjugated to a lipid carrier (e.g., DSPE-PEG) prior to insertion of the C-type lectin receptor or a fragment thereof, via the DSPE lipid moiety, into the outer surface of the liposome. A C-type lectin receptor or a fragment thereof can also be conjugated to a nanoparticle by a number of methods known in the art (e.g., Arruebo et al. “Antibody-Conjugated Nanoparticles for Biomedical Applications,” Journal of Nanomaterials vol. 2009, Article ID 439389 (2009)). Liposomes can also be conjugated to cancer-targeting molecules via a streptavidin / biotin bond, thiol / maleimide chemistry, azide / alkyne chemistry, tetrazine / cyclooctyne chemistry, and other click chemistries. These chemical handles are prepared either during phosphoramidite synthesis or post-synthesis. As used herein, the term click chemistry refers to biocompatible reactions intended primarily to join substrates of choice with specific biomolecules. Click chemistry reactions are not disturbed by water, generate minimal and non-toxic byproducts, and are characterized by a high thermodynamic driving force that drives it quickly and irreversibly to high yield of a single reaction product, with high reaction specificity. Exemplary human C-Type Lectin receptor polypeptides that can target nanoparticles to cancer cells, for example, by binding an antigen(s) on cancer cells include, but are not limited to, Dectin-1, Dectin-2, Dectin-3, and DC-SIGN. In some embodiments, the C-Type Lectin polypeptide or a fragment thereof comprises a carbohydrate recognition domain (CRD) and is not a full-length C-type lectin receptor (e.g., not a full-length Dectin-1, Dectin-2, Dectin-3 or DC-SIGN polypeptide). Fragments of Dectin-1, Dectin-2, Dectin-3, or DC-SIGN, for example fragments comprising a CRD, can also be coupled to the surface of any of the nanoparticles described herein. Table 1 sets forth the corresponding UniProt Nos. for the amino acid sequences of these exemplary C-type Lectin polypeptides. The amino acid sequences set forth in the Uniprot Nos of Table 1 are incorporated herein by reference. Amino acid sequences having at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, or at least 95% sequence identity with the amino acids sequences set forth in the Uniprot Nos of Table 1 are PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) also provided. In some embodiments, the amino acid sequence is a cancer cell binding protein sequence that has at least 75%, at least 80%, at least 85%, at least 90%, or at least 95% sequence identity with the amino acids sequences set forth in the Uniprot Nos of Table 1. Fragments of any of the polypeptides described herein are also provided. Table 1 – C-type Lectins Exemplary C-type lectin polypeptides that bind to cancer cells include but are not limited to soluble human Dectin-1, Dectin-2 and Dectin-3 polypeptides comprising SEQ ID NO: 1, 2, and 3, respectively. Other exemplary targeting molecules include but are not limited to soluble mouse Dectin-1, Dectin-2 and Dectin-3 polypeptides comprising SEQ ID NO: 4, 5, 6, respectively. Fragments of SEQ ID NOs: 1, 2, 3, 4, 5, or 6, for example, fragments comprising a deletion of 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 or more amino acids from the C-terminal and / or N-terminal end of a polypeptide comprising or consisting of SEQ ID NOs: 1, 2, 3, 4, 5, PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) or 6, are also provided and can be used in any of the nanoparticles (e.g. liposomes), polypeptides or compositions described herein. Other exemplary constructs that can be used in any of the nanoparticles described herein are set forth as follows. SEQ ID NO: 7, shown below, is a nucleic acid sequence encoding an exemplary codon optimized soluble mouse Dectin-1 (sDectin-1). A vector pET-45b+ sequence of 9 codons is boxed with the start codon underlined. Sites for cloning into pET-45B+ KpnI (GGTACC)(SEQ ID NO: 23) and PacI (TTAATTAA) (SEQ ID NO: 36), respectively, are underlined. Codons for Gly Ser (G,S) flexible linker residues are shown in bold and codons for reactive lys (K) residues (AAG) are shown in bold, with lysine codons in italic). The mouse sDectin-1 sequence (CLEC7A, GenBank No. AAS37670.1) is shown in plain text; an Ala codon GCT and stop codons TAA and TTA are underlined, with stop codons in bold. Alternative gene name MmsDectin1lyshis. The length of the nucleotide sequence is 604 base pairs, with 597 base pairs encoding a protein of 199 amino acids in length. ATG GCA CAT CAC CAC CAC CAT CAC GTG GGT ACC GGC AGC GGC AAG GGC AAG GGC AGC GGC AGC GGT TTT TGG CGTCACAACAGCGGTCGTAACCCGGAGGAGAAAGACAACTTCCTGAGCCGTAAC AAGGAGAACCACAAACCGACCGAGAGCAGCCTGGACGAAAAGGTTGCGCCGAG CAAAGCGAGCCAGACCACCGGTGGCTTCAGCCAACCGTGCCTGCCGAACTGGAT CATGCACGGCAAGAGCTGCTACCTGTTCAGCTTTAGCGGTAACAGCTGGTATGGC AGCAAACGTCATTGCAGCCAGCTGGGTGCGCACCTGCTGAAGATCGACAACAGC AAAGAGTTCGAATTTATTGAGAGCCAGACCAGCAGCCACCGTATCAACGCGTTTT GGATTGGTCTGAGCCGTAACCAAAGCGAGGGTCCGTGGTTCTGGGAAGATGGCA GCGCGTTCTTTCCGAACAGCTTTCAAGTGCGTAACACCGCGCCGCAAGAAAGCCT GCTGCACAACTGCGTTTGGATTCACGGCAGCGAGGTTTACAATCAAATCTGCAAT ACCAGCAGCTACAGCATCTGCGAGAAG GAA CTG GCT TAA TTA A (SEQ ID NO: 7) SEQ ID NO: 8 is an amino acid sequence encoded by SEQ ID NO: 7. This is a polypeptide comprising a mouse sDectin-1 polypeptide. The N-terminal amino acid sequence and (His)6(HHHHHH) (SEQ ID NO: 37) affinity tag is boxed. The Gly Ser (GS) flexible linker residues and reactive lys (K) residues appear in bold with lysines in italic. Mouse sDectin-1 amino acid residues appear in plain text, ending in a C-terminal Ala residue (A) in bold, the PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) codon for which was used to put stop codons and a PacI site in frame. It is understood that, optionally, a stop codon in any of the polypeptide sequences disclosed herein, if not part of the native polypeptide from which the polypeptide is derived, can be removed, to produce a polypeptide that does not include one or more stop codons. The protein comprising the mouse sDectin-1 polypeptide is 199 amino acids in length, with a molecular weight (MW) of 22,389.66 g / mole. The theoretical pI is 7.74. It is understood that any protein described herein comprising an affinity tag, for example, a (His)6 affinity tag, can be modified to remove the His tag. Therefore, polypeptides (i.e. any C-type lectin receptor or fragment thereof or DC- SIGN polypeptide or fragment thereof) that do not comprise a histidine tag are provided herein. In some examples, any nucleotide sequence described herein can further comprise a protease cleavage site for post-translational and / or post-purification removal of the affinity tag. In some examples, the soluble mouse Dectin-1 polypeptide comprises amino acids 23-198 of SEQ ID NO: 8 or amino acids 23-199 of SEQ ID NO: 8. MAHHHHHHV GT GSG KGK GSGSG FWRHNSGRNPEEKDSFLSRNKENHKPTESSLDEKVAPSKASQTTGGFSQSCLPNWIM HGKSCYLFSFSGNSWYGSKRHCSQLGAHLLKIDNSKEFEFIESQTSSHRINAFWIGLSR NQSEGPWFWEDGSAFFPNSFQVRNAVPQESLLHNCVWIHGSEVYNQICNTSSYSICE KELA (SEQ ID NO: 8) In some embodiments, the soluble mouse Dectin-1 polypeptide comprises SEQ ID NO: 46 MAHHHHHHYGTGSGKGKGSGSGFWRHNSGRNPEEKDSFLSRNKENHKPTESSLDE KVAPSKASQTTGGFSQSCLPNWIMHGKSCYLFSFSGNSWYGSKRHCSQLGAHLLKID NSKEFEFIESQTSSHRINAFWIGLSRNQSEGPWFWEDGSAFFPNSFQVRNAVPQESLL HNCVWIHGSEVYNQICNTSSYSICEKELA (SEQ ID NO: 46) SEQ ID NO: 9 is a nucleic acid sequence encoding an exemplary codon optimized soluble mouse Dectin-2 (sDectin-2) (SEQ ID NO: 10). The vector pET-45b+ sequence of 9 codons is boxed with the start codon underlined. Sites for cloning into pET-45B+ KpnI (GGTACC)(SEQ ID NO: 38) and PacI (TTAATTAA) (SEQ ID NO: 36), respectively, are underlined. Codons for Gly Ser (G,S) flexible linker residues appear in bold and the codons for reactive lys (K) residues (AAG) appear in bold, with lysine codons in italic. Codon optimized sDectin-2 from the CLEC6A mouse Dectin 2 gene appears in plain text, with an Ala codon (GCT) and stop codons, TAA and TTA, underlined and stop codons in bold. The alternative gene name is MmsDectin2lyshis. The length of the nucleic acid sequence is 574 base pairs, PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) with 567 base pairs encoding a protein that is 190 amino acids in length. The nucleic acid encoding the codon-optimized mouse sDectin-2 exemplary was cloned into pET-45B+. ATG GCA CAT CAC CAC CAC CAT CAC GTG GGT ACC GGC AGC GGC AAG GGC AAG GGC AGC GGC AGC GGT ATA ATG GAT CAA CCC TCA AGA AGG CTA TAT GAG CTG CAC ACG TAC CAC AGC TCC CTC ACG TGC TTT TCT GAG GGT ACT ATG GTG TCC GAG AAA ATG TGG GGC TGC TGC CCG AAT CAT TGG AAA TCT TTT GGT AGC AGC TGT TAT CTG ATC AGC ACC AAA GAG AAC TTC TGG AGT ACC AGC GAG CAA AAC TGC GTC CAG ATG GGC GCA CAC CTG GTT GTG ATT AAC ACC GAA GCG GAA CAG AAC TTC ATC ACC CAG CAA TTA AAT GAA AGC TTG TCT TAC TTC CTG GGT CTG TCG GAT CCG CAG GGC AAC GGC AAG TGG CAG TGG ATT GAC GAC ACC CCG TTC TCC CAA AAC GTG CGC TTT TGG CAT CCG CAT GAA CCG AAT CTG CCG GAA GAA CGT TGT GTA AGC ATT GTT TAT TGG AAT CCA AGC AAG TGG GGT TGG AAC GAC GTT TTT TGT GAT AGC AAG CAC AAC TCG ATC TGC GAG ATG AAA AAG ATC TAC TTG GCT TAA TTA A (SEQ ID NO: 9) SEQ ID NO 10 is an amino acid sequence encoded by SEQ ID NO: 9. This polypeptide comprises a mouse sDectin-2 protein. The N terminal amino acid and (His)6(HHHHHH)(SEQ ID NO: 37) affinity tag from pET-45B+ is boxed. The Gly Ser (GS) flexible linker residues and reactive lys (K) residues appear in bold, with lysines in italic. Mouse sDectin-2 amino acid residues appear in plain text ending in a C-terminal Ala residue (A) (bold), the codon for which was used to put stop codons and PacI site in frame. The polypeptide comprising the mouse sDectin-2 that is produced has 189 amino acids, with a MW of 21,699.25 g / mole and a theoretical pI of 6.33. In some examples, the soluble mouse Dectin-2 polypeptide comprises amino acids 23-188 of SEQ ID NO: 10, or amino acids 23-189 of SEQ ID NO: 10. MAHHHHHHV GT GSG KGK GSGSG IMDQPSRRLYELHTYHSSLTCFSEGTMVSEKMWGCCPNHWKSFGSSCYLISTKENFW STSEQNCVQMGAHLVVINTEAEQNFITQQLNESLSYFLGLSDPQGNGKWQWIDDTPF SQNVRFWHPHEPNLPEERCVSIVYWNPSKWGWNDVFCDSKHNSICEMKKIYLA (SEQ ID NO: 10) In some embodiments, the soluble mouse Dectin-2 polypeptide comprises SEQ ID NO: 47 MAHHHHHHYGTGSGKGKGSGSGIMDQPSRRLYELHTYHSSLTCFSEGTMVSEKMW GCCPNHWKSFGSSCYLISTKENFWSTSEQNCVQMGAHLVVINTEAEQNFITQQLNES LSYFLGLSDPQGNGKWQWIDDTPFSQNVRFWHPHEPNLPEERCVSIVYWNPSKWG WNDVFCDSKHNSICEMKKIYLA (SEQ ID NO: 47) SEQ ID NO: 11 is a nucleic acid sequence encoding an exemplary codon optimized soluble mouse Dectin-3 (sDectin-3) (SEQ ID NO: 12). The vector pET-45b+ sequence of 9 PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) codons is boxed with the start codon underlined. Sites for cloning into pET-45b+ KpnI (GGTACC) (SEQ ID NO: 38) and PacI (TTAATTAA) (SEQ ID NO: 36), respectively, are underlined. Codons for Gly Ser (G,S) flexible linker residues are shown in bold. Reactive lys (K) codons (AAG) are shown in bold, with lysines in italic. Codon optimized sDectin-3 from the CLEC4D mouse Dectin-3 gene (GenBank Accesion No. NP_034949.3) is shown in plain text, with an Ala codon (GCT) and stop codons TAA and TTA underlined. Stop codons are shown in bold. The alternative gene name is MmsDectin3lyshis. The length of the nucleotide sequence is 604 base pairs, with 597 base pairs encoding a protein that is 199 amino acids in length. The nucleic acid encoding the exemplary codon-optimized mouse sDectin-3 was cloned into pET-45B+. ATG GCT CAC CAT CAC CAC CAC CAT TAT GGT ACC GGT TCC GGC AAA GGC AAG GGC TCC GGC TCT GGT CAC TATTTCCTGCGTTGGACCCGCGGTTCCGTGGTGAAACTGAGCGACTACCAT ACGCGCGTGACTTGCATTCGTGAAGAGCCGCAGCCGGGCGCAACCGGCGGTACA TGGACG TGCTGCCCGGTTAGCTGGCGTGCGTTCCAGTCTAACTGTTATTTCCCACTGAATG ACAAC CAAACGTGGCATGAGAGCGAACGTAACTGCAGCGGCATGAGCAGTCACCTGGTT ACCATT AACACCGAGGCGGAGCAAAACTTTGTGACCCAATTGCTCGACAAGCGCTTCAGC TACTTC CTGGGTTTGGCCGATGAAAATGTTGAGGGTCAGTGGCAGTGGGTAGATAAGACC CCGTTT AATCCGCACACCGTCTTTTGGGAAAAGGGTGAGTCGAACGACTTCATGGAAGAA GATTGT GTTGTTCTGGTGCACGTGCACGAGAAGTGGGTTTGGAATGATTTCCCGTGTCATT TTGAA GTCAGACGTATCTGCAAATTACCGGGTATCACCTTTAACTGGAAACCGAGCAAA GCT TAA TTA A (SEQ ID NO: 11) SEQ ID NO: 12 is an amino acid sequence encoded by SEQ ID NO: 11. This polypeptide comprises a mouse sDectin-3 protein. The N terminal amino acid and (His)6(HHHHHH)(SEQ ID NO: 37) affinity tag from pET-45B+ is boxed. Gly Ser (GS)flexible linker residues and reactive lys (K) residues are shown in bold, with lysines in italic. Mouse sDectin-3 amino acid residues are shown in plain text (amino acids 23-199 of SEQ ID NO: 12), ending in a C-terminal Ala residue (A) in bold, the codon for which was used to put stop codons and PacI site in frame. The polypeptide is 199 amino acids in length with a MW of 23,023.72 g / mole and a theoretical pI or 6.52. In some examples, the soluble mouse Dectin-3 polypeptide comprises amino acids 23-198 of SEQ ID NO: 12 or amino acids 23-199 of SEQ ID NO: 12. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) DNQTWHESERNCSGMSSHLVTINTEAEQNFVTQLLDKRFSYFLGLADENVEGQWQ WVDKTPFNPHTVFWEKGESNDFMEEDCVVLVHVHEKWVWNDFPCHFEVRRICKLP GITFNWKPSK A (SEQ ID NO: 12) In some embodiments, the soluble mouse Dectin-3 polypeptide comprises SEQ ID NO: 48 MAHHHHHHYGTGSGKGKGSGSGHYFLRWTRGSVVKLSDYHTRVTCIREEPQPGAT GGTWTCCPVSWRAFQSNCYFPLNDNQTWHESERNCSGMSSHLVTINTEAEQNFVTQ LLDKRFSYFLGLADENVEGQWQWVDKTPFNPHTVFWEKGESNDFMEEDCVVLVHV HEKWVWNDFPCHFEVRRICKLPGITFNWKPSKA (SEQ ID NO: 48) SEQ ID NO: 13 is a nucleic acid sequence encoding an exemplary codon optimized soluble human Dectin-1 (sDectin-1) (SEQ ID NO: 14). The human sDectin-1 DNA sequence is expressed from vector pET-45B+. The vector pET-45b+ sequence and His tag of 9 codons is boxed with the start codon underlined. Cloning sites BamHI (GGATCC)(SEQ ID NO: 38) and PacI (TTAATTAA)(SEQ ID NO: 36), respectively, are underlined. Codons for enterokinase processing site in lower case font, Codons for Gly Ser (G,S) flexible linker residues and reactive lys (K) residues (AAA and AAG) are shown in bold with lysine codons in italic. The human sDectin-1 sequence (CLEC7A, GenBank Accession No. NM_197947) is shown in plain text, codon optimized for expression. An Ala codon GCT and stop codons TAA and TTA underlined, with stop codons in bold. An alternate name for this sequence is HssDectin1lyshis. The nucleotide sequence encoding human sDectin-1 has a length of 649 base pairs, encoding a polypeptide that is 214 amino acids in length. The nucleic acid encoding the exemplary codon-optimized human sDectin-1 was cloned into pET-45B+. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) SEQ ID NO: 14 is an amino acid sequence encoded by SEQ ID NO: 13. This is a polypeptide comprising a human sDectin-1 protein. The N-terminal amino acid and (His)6 (HHHHHH)(SEQ ID NO: 37) affinity tag from pET-45B+ is boxed. The enterokinase processing site in lower case font. The Gly Ser (GS)flexible linker residues and reactive lys (K) residues are shown in bold, with lysines in italic. Human sDectin-1 amino acid residues are shown in plain text, ending in a C-terminal Ala residue (A) in bold, the codon for which was used to put stop codons and PacI site in frame. The polypeptide is 214 amino acids in length, with a MW of 23,703.20 g / mole and a theoretical pI of 6.22. In some examples, the soluble human Dectin-1 polypeptide fragment comprises amino acids 35-213 of SEQ ID NO: 14 or amino acids 35-214 of SEQ ID NO: 14. MAHHHHHHYGT GSN ddddk SPDP GSG KGK GSGSG IWRSNSGSNTLENGYFLSRNKENHSQPTQSSLEDSVTPTKAVKTTGVLSSPCPPNWII YEKSCYLFSMSLNSWDGSKRQCWQLGSNLLKIDSSNELGFIVKQVSSQPDNSFWIGL SRPQTEVPWLWEDGSTFSSNLFQIRTTATQENPSPNCVWIHVSVIYDQLCSVPSYSICE KKFSM A (SEQ ID NO: 14) In some embodiments, a polypeptide comprising a human sDectin-1 protein comprises SEQ ID NO: 40 or a fragment thereof (for example, amino acids 23-201 of SEQ ID NO: 40, or amino acids 23-202 of SEQ ID NO: 40). MAHHHHHHYGTGSGKGKGSGSGIWRSNSGSNTLENGYFLSRNKENHSQPTQSSLED SVTPTKAVKTTGVLSSPCPPNWIIYEKSCYLFSMSLNSWDGSKRQCWQLGSNLLKID SSNELGFIVKQVSSQPDNSFWIGLSRPQTEVPWLWEDGSTFSSNLFQIRTTATQENPSP NCVWIHVSVIYDQLCSVPSYSICEKKFSMA (SEQ ID NO: 40) In some embodiments, a polypeptide comprising a human sDectin-1 protein comprises SEQ ID NO: 43 or a fragment thereof. The membrane spanning and / or stalk region of human Dectin-1 is underlined. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) MEYHPDLENLDEDGYTQLHFDSQSNTRIAVVSEKGSCAASPPWRLIAVILGILCLVIL VIAVVLGTMAIWRSNSGSNTLENGYFLSRNKENHSQPTQSSLEDSVTPTKAVKTTGV LSSPCPPNWIIYEKSCYLFSMSLNSWDGSKRQCWQLGSNLLKIDSSNELGFIVKQVSS QPDNSFWIGLSRPQTEVPWLWEDGSTFSSNLFQIRTTATQENPSPNCVWIHVSVIYDQ LCSVPSYSICEKKFSM (SEQ ID ON: 43) SEQ ID NO: 15 is a nucleic acid sequence encoding an exemplary codon optimized soluble human Dectin-2 (sDectin-2) (SEQ ID NO: 16). The human sDectin-2 nucleotide sequence is expressed from vector pET-45B+. The length of the nucleotide sequence is about 616 base pairs with 580 base pairs encoding a protein of 203 amino acids in length. The vector pET-45b+ sequence of 9 codons including the His tag is boxed with the start codon underlined. Cloning sites BamHI (GGATCC)(SEQ ID NO: 38) and PacI (TTAATTAA)(SEQ ID NO: 36), respectively, are underlined. Codons for enterokinase processing site in lower case font. Codons for Gly Ser (G,S) flexible linker residues are shown in bold, and reactive lys (K) residues (AAG) are shown in bold, with lysines in italic. Codon optimized sDectin-2 from the CLEC6A human Dectin 2 gene (cDNA GenBank Accession No. NM_001317999) is shown in plain text. An Ala codon (GCT) and stop codons, TAA and TTA, are underlined, with stop codons shown in bold. The alternative gene name is HssDectin2lyshis. The nucleic acid encoding the codon-optimized human sDectin-2 exemplary was cloned into pET-45B+. ATG GCA CAT CAC CAC CAC CAT CAC GTG GGT ACC GGT TCG AAT gat gac gac gac aag AGT CCG GAT CCC GGG TCT GGA AAA GGC AAG GGA AGT GGT TCA ATCACTCCTCTCTGACGTGCTTTAGCGAGGGTACTAAAGTGCCAGCGTGGGGTTG TTGTCCGGCGAGCTGGAAGTCGTTCGGCAGCAGCTGCTATTTCATCAGCTCGGAG GAAAAAGTTTGGAGCAAGAGCGAGCAAAACTGCGTGGAAATG GGTGCACATTTGGTTGTCTTCAACACCGAAGCGGAGCAAAACTTTATCGTGCAGC AGCTGAACGAAAGCTTCTCCTACTTCCTGGGTCTGTCCGACCCGCAGGGTAATAA CAACTGGCAGTGGATTGATAAAACCCCGTATGAAAAGAACGTGCGCTTTTGGCA TTTGGGCGAGCCGAATCATTCTGCCGAACAATGTGCGAGCATTGTTTTCTGGAAG CCGACCGGCTGGGGTTGGAATGACGTTATTTGCGAGACGCGTCGTAACAGCATCT GCGAGATGAATAAAATCTACCTG GCT TAA TTA A (SEQ ID NO: 15) SEQ ID NO: 16 is the amino acid sequence encoded by SEQ ID NO: 15. This polypeptide comprises a human sDectin-2 protein. The N-terminal amino acid and (His)6(HHHHHH)(SEQ ID NO: 37) affinity tag from pET-45B+ are boxed. The enterokinase processing site is in lower case font. Gly Ser (GS) flexible linker residues and reactive lys (K) PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) residues are shown in bold, with lysines in italic. Human sDectin-2 amino acid residues are shown in plain text (GenBank Accession No. NP_001007034.1) (amino acids 36-203 of SEQ ID NO: 10), ending in a C-terminal Ala residue (A) in bold, the codon for which was used to put stop codons and PacI site in frame. The polypeptide is 203 amino acids in length, with a MW of 22,969 g / mole and a theoretical pI of 5.91. In some examples, the soluble human Dectin-2 polypeptide fragment comprises amino acids 35-202 of SEQ ID NO: 16 or amino acids 35-203 of SEQ ID NO: 16. MAHHHHHHV GT GSN ddddk SPDP GSG KGK GSGSG TYHFTYGETGKRLSELHSYHSSLTCFSEGTKVPAWGCCPASWKSFGSSCYFISSEEKV WSKSEQNCVEMGAHLVVFNTEAEQNFIVQQLNESFSYFLGLSDPQGNNNWQWIDKT PYEKNVRFWHLGEPNHSAEQCASIVFWKPTGWGWNDVICETRRNSICEMNKIYL A (SEQ ID NO: 16) In some embodiments, a polypeptide comprising a human sDectin-2 protein comprises SEQ ID NO: 41 or a fragment thereof (for example, amino acids 23-186 of SEQ ID NO: 41, or amino acids 23-187 of SEQ ID NO: 41). MAHHHHHHVGTGSGKGKGSGSGTYGETGKRLSELHSYHSSLTCFSEGTKVPAWGC CPASWKSFGSSCYFISSEEKVWSKSEQNCVEMGAHLVVFNTEAEQNFIVQQLNESFS YFLGLSDPQGNNNWQWIDKTPYEKNVRFWHLGEPNHSAEQCASIVFWKPTGWGW NDVICETRRNSICEMNKIYLA SEQ ID NO: 41) In some embodiments, a polypeptide comprising a human sDectin-2 protein comprises SEQ ID NO: 44 or a fragment thereof. The membrane spanning and / or stalk region of human Dectin-2 is underlined. MMQEQQPQSTVTYHFTYGETGKRLSELHSYHSSLTCFSEGTKVPAWGCCPASWKSF GSSCYFISSEEKVWSKSEQNCVEMGAHLVVFNTEAEQNFIVQQLNESFSYFLGLSDPQ GNNNWQWIDKTPYEKNVRFWHLGEPNHSAEQCASIVFWKPTGWGWNDVICETRRN SICEMNKIYL (SEQ ID NO: 44) SEQ ID NO: 17 is a nucleic acid sequence encoding an exemplary codon optimized soluble human Dectin-3 (sDectin-3) (SEQ ID NO: 18). The human sDectin-3 DNA sequence is expressed from vector pET-45B+ in E. coli. The vector pET-45b+ sequence of 9 codons with hist tag is boxed, with the start codon underlined. Sites for cloning into pET-45b+ BamHI (GGATCC)(SEQ ID NO: 39) and PacI (TTAATTAA)(SEQ ID NO: 36), respectively, are underlined. Codons for enterokinase processing site are in lower case font. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) Codons for Gly Ser (G,S) flexible linker residues are shown in bold and reactive lys (K) residues (AAG) are shown in bold, with lysines in italic. Codon optimized sDectin-3 from the CLEC4D human Dectin-3 gene,(GenBank Accession NM_080387) is shown in plain text. An Ala codon (GCT) and stop codons, TAA and TTA, are underlined, with stop codons in bold. The alternative gene name is HssDectin3lyshis. The nucleotide sequence has a length of 628 base pairs, encoding a polypeptide of 207 amino acids in length. The nucleic acid encoding the exemplary codon-optimized human sDectin-3 was cloned into pET-45B+. ATG GCT CAC CAT CAC CAC CAC CAT TAT GGT ACC GGT TCG AAT gat gac gac gac aag AGT CCG GAT CCC GGG TCT GGA AAA GGC AAG GGA AGT GGT TCA GGC CACAACTTCAGCCGTTGTAAGCGCGGTACGGGCGTGCATAAGTTGGAGCACCAC GCCAAGCTCAAGTGCATCAAAGAAAAATCCGAGCTGAAATCTGCTGAGGGCAGC ACCTGGAACTGCTGCCCGATTGATTGGCGTGCGTTTCAAAGCAATTGCTACTTCC CGCTGACCGATAACAAAACCTGGGCGGAAAGCGAGCGCAACTGCAGCGGTATGG GTGCACATCTGATGACCATTTCGACCGAAGCGGAGCAGAATTTCATCATCCAATT TTTGGACCGCCGTCTGTCCTACTTCCTGGGTCTGCGTGATGAAAATGCAAAAGGC CAATGGCGTTGGGTTGACCAGACCCCGTTTAACCCGCGTCGTGTTTTTTGGCATA AGAACGAACCAGACAACAGCCAGGGTGAAAACTGCGTCGTGTTAGTTTATAACC AGGATAAATGGGCGTGGAACGACGTGCCGTGTAATTTCGAGGCTTCTCGCATTTG TAAGATCCCGGGTACGACTCTGAAT GCT TAA TTA A (SEQ ID NO: 17) SEQ ID NO: 18 is an amino acid sequence encoded by SEQ ID NO: 17. This polypeptide comprises the human Dectin-3 protein. The N-terminal amino acid and (His)6 (HHHHHH)(SEQ ID NO: 37) affinity tag from pET-45B+ is boxed. The enterokinase processing site is in lower case font. The Gly Ser (GS)flexible linker residues and reactive lys (K) residues are shown in bold, with lysines in italic. The human sDectin-3 amino acid residues (GenBank Accession No. NP_525126) are shown in plain text (amino acids 35-207 of SEQ ID NO: 12), ending in a C-terminal Ala residue (A) in bold, the codon for which was used to put stop codons and a PacI site in frame. The protein is 207 amino acids in length with a MW of 23,662 g / mole and a theoretical pI of 7.64. In some examples, the soluble human Dectin-3 polypeptide fragment comprises amino acids 35-206 of SEQ ID NO: 18. MAHHHHHHV GT GSN ddddk SPDP GSG KGK GSGSG HNFSRCKRGTGVHKLEHHAKLKCIKEKSELKSAEGSTWNCCPIDWRAFQSNCYFPLT DNKTWAESERNCSGMGAHLMTISTEAEQNFIIQFLDRRLSYFLGLRDENAKGQWRW VDQTPFNPRRVFWHKNEPDNSQGENCVVLVYNQDKWAWNDVPCNFEASRICKIPG TTLN A (SEQ ID NO: 18) PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) In some embodiments, a polypeptide comprising a human sDectin-3 protein comprises SEQ ID NO: 42 or a fragment thereof (for example, amino acids 23-194 of SEQ ID NO: 42, or amino acids 23-195 of SEQ ID NO: 42). MAHHHHHHVGTGSGKGKGSGSGHNFSRCKRGTGVHKLEHHAKLKCIKEKSELKSA EGSTWNCCPIDWRAFQSNCYFPLTDNKTWAESERNCSGMGAHLMTISTEAEQNFIIQ FLDRRLSYFLGLRDENAKGQWRWVDQTPFNPRRVFWHKNEPDNSQGENCVVLVYN QDKWAWNDVPCNFEASRICKIPGTTLNA (SEQ ID NO: 42) In some embodiments, a polypeptide comprising a human sDectin-3 protein comprises SEQ ID NO: 45 or a fragment thereof. The membrane spanning and / or stalk region of human Dectin-3 is underlined. MGLEKPQSKLEGGMHPQLIPSVIAVVFILLLSVCFIASCLVTHHNFSRCKRGTGVHKL EHHAKLKCIKEKSELKSAEGSTWNCCPIDWRAFQSNCYFPLTDNKTWAESERNCSG MGAHLMTISTEAEQNFIIQFLDRRLSYFLGLRDENAKGQWRWVDQTPFNPRRVFWH KNEPDNSQGENCVVLVYNQDKWAWNDVPCNFEASRICKIPGTTLN (SEQ ID ON: 45) In some nanoparticles, the targeting molecule is a Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Non-integrin (DC-SIGN) polypeptide or a fragment thereof comprising a carbohydrate recognition domain (CRD), and wherein the targeting molecule is incorporated into the outer surface of the nanoparticle. Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Non-integrin (DC- SIGN or CD209) is a type II membrane protein, with a single CRD, expressed on the surface of immature dendritic cells (DCs), involved in initiation of the primary immune response. Human DC-SIGN is a 404 amino acid residue polypeptide that comprises an N-terminal cytoplasmic tail, a transmembrane domain, and an extracellular domain comprising eight neck regions (NR1-NR8) and a carbohydrate recognition domain (CRD). The full-length sequence of DC-SIGN is set forth under UniProtKB No. Q9NNX6, and set forth herein as SEQ ID NO: 19. Amino acids 1-70 of SEQ ID NO: 19 comprise the signal sequence and transmembrane domain of DC-SIGN (SEQ ID NO: 20). It is understood that polypeptide sequences comprising a polypeptide fragment of DC-SIGN that does not include the signal sequence and / or transmembrane domain are also provided herein. For example, fragment of amino acids 71- 404 are provided herein, including fragments with N-terminal and / or C-terminal deletions of 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids. In some nanoparticles, the DC-SIGN polypeptide is not a full-length DC-SIGN polypeptide In some nanoparticles, the DC-SIGN polypeptide fragment comprises a CRD PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) (SEQ ID NO: 21) and one or more neck regions of DC-SIGN selected from the group consisting of (NR1) SEQ ID NO: 22, (NR2) SEQ ID NO: 23, (NR3) SEQ ID NO: 24, (NR4) SEQ ID NO: 25, (NR5) SEQ ID NO: 26, (NR6) SEQ ID NO: 27, (NR7) SEQ ID NO: 28 and (NR8) SEQ ID NO: 29. It is understood that the CDR and one or more neck regions of DC-SIGN can be joined with or without a linker having about 2, 3, 4, 5, 6, 7, 8, 9, 10 or more amino acids. Examples of linkers include but are not limited to GSGnwherein n is an integer, and GSGSG (SEQ ID NO: 49). Any of the DC-SIGN polypeptides provided herein can also be linked to a tag, for example, a histidine tag, as described below. In some nanoparticles, the DC-SIGN polypeptide fragment comprises, consists essentially of, or consists of, a DC-SIGN CRD (SEQ ID NO: 21), NR7 (SEQ ID NO: 28) and NR8 (SEQ ID NO: 29). An example of this construct is described herein as DSC78. In some liposomes, the fragment comprises, consists essentially of, or consists of SEQ ID NO: 30 (DCS78 construct) set forth below. N terminal amino acid and (His)6 (HHHHHH) (SEQ ID NO: 37) affinity tag from a pET-45B+ vector is boxed. Gly Ser (GS)flexible linker residues and reactive lys (K) residues for linking to lipid carrier are in bold with lysines in italic. Human DC-SIGN amino acid residues appear in plain text and includes 2x23 a.a. neck repeats 7 and 8 and all 153 a.a. of CDR (total of 201 a.a. from Hs DC-SIGN), ending in a C-terminal Ala residue (A) in bold, the codon for which was used to put stop codons and PacI site in frame. It is understood that fragments of SEQ ID NO: 30 that do not comprise the His tag (boxed), the linker sequence (bold) and / or the C-terminal Ala residue of SEQ ID NO: 30 are also provided. SEQ ID NO: 30 is an exemplary sequence comprising a DC-SIGN CRD (SEQ ID NO: 21), NR7 (SEQ ID NO: 28) and NR8 (SEQ ID NO: 29). Fragments of SEQ ID NO: 30 are also provided. SEQ ID NO: 31 encodes the amino acid sequence of SEQ ID NO: 30. MAHHHHHHYGT GSG KGK GSGSG GELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTQLKAAVERLCHPCPWEW TFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWM GLSDLNQEGTWQWVDGSPLLPSFKQYWNRGEPNNVGEEDCAEFSGNGWNDDKCN LAKFWICKKSAASCSRDEEQFLSPAPATPNPPPA (SEQ ID NO: 30) In some nanoparticles, the fragment comprises, consists essentially of, or consists of, a DC-SIGN (CRD) SEQ ID NO: 21, NR1 (SEQ ID NO: 22) and NR2 (SEQ ID NO: 23). An example of this construct is described herein as DCS12. In some liposomes, the fragment comprises, consists essentially of, or consists of, SEQ ID NO: 32 (DSC12 construct) as set PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) forth below. An N terminal amino acid and (His)6 (HHHHHH) (SEQ ID NO: 37) affinity tag from a pET-45B+ vector is boxed. Gly Ser (GS)flexible linker residues and reactive lys (K) residues for linking to lipid carrier are in bold with lysines in italic. Human DC-SIGN amino acid residues appear in plain text and includes 2x23 a.a. neck repeats 1 and 2 (underlined) and all 153 a.a. of CDR (total of 201 a.a. from Hs DC-SIGN splice variant 2d (Serrano Gomez et al., Journal of Biological Chemistry 283, 3889-3903 (2008)), ending in a C-terminal Ala residue (A) in bold, the codon for which was used to put stop codons and PacI site in frame. It is understood that fragments of SEQ ID NO: 32 that do not comprise the His tag (boxed) the linker sequence (bold) and / or the C-terminal Ala residue are also provided. SEQ ID NO: 32 is another exemplary sequence comprising a DC-SIGN (CRD) SEQ ID NO: 1, NR1 (SEQ ID NO: 2) and NR2 (SEQ ID NO: 3). Fragments of SEQ ID NO: 32 are also provided. SEQ ID NO: 33 encodes SEQ ID NO: 32. MAHHHHHHYGTGSGKGKGSGSGQSRQDAIYQNLTQLKAAVGELSEKSKLQEIYQE LTQLKAAVERLCHPCPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSA EEQNFLQLQSSRSNRFTWMGLSDLNQEGTWQWVDGSPLLPSFKQYWNRGEPNNVG EEDCAEFSGNGWNDDKCNLAKFWICKKSAASCSRDEEQFLSPAPATPNPPPA (SEQ ID NO: 32) Other examples of DC-SIGN polypeptides include, but are not limited to: • a polypeptide comprising, consisting essentially of, or consisting of a DC-SIGN CRD (SEQ ID NO: 21), (NR1) SEQ ID NO: 22, (NR2) SEQ ID NO: 23, (NR3) SEQ ID NO: 24, (NR4) SEQ ID NO: 25, (NR5) SEQ ID NO: 26, (NR6) SEQ ID NO: 27, (NR7) SEQ ID NO: 28 and (NR8) SEQ ID NO: 29 (See, for example, SEQ ID NO: 34, encoded by SEQ ID NO: 35) • a polypeptide comprising, consisting essentially of, or consisting of a DC-SIGN CRD (SEQ ID NO: 1), (NR1) SEQ ID NO: 2, (NR6) SEQ ID NO: 7, (NR7) SEQ ID NO: 8 and (NR8) SEQ ID NO: 9 • polypeptide comprising, consisting essentially of, or consisting of a DC-SIGN CRD (SEQ ID NO: 21), (NR1) SEQ ID NO: 22, (NR2) SEQ ID NO: 23, (NR3) SEQ ID NO: 24, and (NR8) SEQ ID NO: 29 • a polypeptide comprising, consisting essentially of, or consisting of a DC-SIGN CRD (SEQ ID NO: 21), (NR1) SEQ ID NO: 22, (NR2) SEQ ID NO: 23, (NR7) SEQ ID NO: 28 and (NR8) SEQ ID NO: 29 PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) • a polypeptide comprising, consisting essentially of, or consisting of a DC-SIGN CRD (SEQ ID NO: 21) and (NR1) SEQ ID NO: 22, (NR2) • a polypeptide comprising, consisting essentially of, or consisting of a DC-SIGN CRD (SEQ ID NO: 21), (NR1) SEQ ID NO: 22, (NR2) SEQ ID NO: 23, (NR3) SEQ ID NO: 24, (NR4) SEQ ID NO: 25, (NR5) SEQ ID NO: 26, (NR7) SEQ ID NO: 28 and (NR8) SEQ ID NO: 29 • a polypeptide comprising, consisting essentially of, or consisting of a DC-SIGN CRD (SEQ ID NO: 21), (NR1) SEQ ID NO: 22, (NR2) SEQ ID NO: 23, (NR3) SEQ ID NO: 24, (NR4) SEQ ID NO: 25, (NR7) SEQ ID NO: 28 and (NR8) SEQ ID NO:29 • a polypeptide comprising, consisting essentially of, or consisting of a DC-SIGN CRD (SEQ ID NO: 21), (NR1) SEQ ID NO: 22, (NR3) SEQ ID NO: 24, (NR4) SEQ ID NO: 25, (NR7) SEQ ID NO: 28 and (NR8) SEQ ID NO: 29 As used throughout, polypeptide, protein and peptide are used interchangeably herein to refer to a polymer of amino acid residues. As used herein, the terms encompass amino acid chains of any length, including full-length proteins and fragments thereof, wherein the amino acid residues are linked by covalent peptide bonds. As used throughout, the term nucleic acid refers to deoxyribonucleic acids (DNA) or ribonucleic acids (RNA) and polymers thereof in either single- or double-stranded form. Unless specifically limited, the term encompasses nucleic acids containing known analogues of natural nucleotides that have similar binding properties as the reference nucleic acid and are metabolized in a manner similar to naturally occurring nucleotides. Unless otherwise indicated, a particular nucleic acid sequence also implicitly encompasses conservatively modified variants thereof (e.g., degenerate codon substitutions), alleles, orthologs, SNPs, and complementary sequences as well as the sequence explicitly indicated. Specifically, degenerate codon substitutions may be achieved by generating sequences in which the third position of one or more selected (or all) codons is substituted with mixed-base and / or deoxyinosine residues (Batzer et al., Nucleic Acid Res. 19:5081 (1991); Ohtsuka et al., J. Biol. Chem. 260:2605-2608 (1985); and Rossolini et al., Mol. Cell. Probes 8:91-98 (1994)). In each case, where specific nucleic acid or polypeptide sequences are recited, embodiments comprising a sequence having at least 70% (e.g., 70%, 75%,80%, 85%. 90%, 95%, 99%) identity to the recited sequence are also provided. Identity or similarity with respect PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) to a sequence is defined as the percentage of amino acid residues in the candidate sequence that are identical (i.e., same residue) with the starting amino acid residues, after aligning the sequences and introducing gaps, if necessary, to achieve the maximum percent sequence identity. For example, polypeptide and nucleic acid sequences having at least 70% (e.g., 70%, 75%, 80%, 85%. 90%, 95%, 99%) identity to SEQ ID NOs: 1-45 are provided herein. Polypeptides and nucleic acid sequences that do not include the histidine tag and / or linker sequences set forth in SEQ ID NOs: 1-35 are also provided. Polypeptides and nucleic acid sequences having at least 60% (e.g. 60%, 65%, 70%, 75%, 80%, 85%. 90%, 95%, 99%) identity to polypeptides and nucleic acid sequences that do not include the histidine tag and / or linker sequences set forth in SEQ ID NOs: 1-48 are also provided herein. It is understood that sequences having at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity to any one of SEQ ID NOs: 1-48 can be used in any of the nanoparticles (for example, liposomes) described herein. Nucleic acids encoding the polypeptides described herein are also provided. Methods of alignment of sequences for comparison are well known in the art. Optimal alignment of sequences for comparison can be conducted, for example, by the local homology algorithm of Smith and Waterman (Adv. Appl. Math.2:482, 1970), by the homology alignment algorithm of Needleman and Wunsch (J. Mol. Biol.48:443, 1970), by the search for similarity method of Pearson and Lipman (Proc. Natl. Acad. Sci. USA 85:2444, 1988), by computerized implementations of these algorithms (e.g., GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin Genetics Software Package, Genetics Computer Group, 575 Science Dr., Madison, Wis.), or by manual alignment and visual inspection (see, e.g., Ausubel et al., Current Protocols in Molecular Biology (1995 supplement)). Any of the polypeptides disclosed herein can comprise one or more conservative amino acid substitutions. As a non-limiting example, the list below summarizes possible substitutions often likely to be carried out without resulting in a significant modification of the biological activity of the corresponding variant: 1) Alanine (A), Serine (S), Threonine (T), Valine (V), Glycine (G), and Proline (P); 2) Aspartic acid (D), Glutamic acid (E); 3) Asparagine (N), Glutamine (Q); 4) Arginine (R), Lysine (K), Histidine (H); 5) Isoleucine (I), Leucine (L), Methionine (M), Valine (V) and 6) Phenylalanine (F), Tyrosine (Y), Tryptophan (W). See also, Creighton, Proteins, W.H. Freeman and Co. (1984). PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) In making such changes / substitutions, the hydropathic index of amino acids may also be considered. The importance of the hydropathic amino acid index in conferring interactive biologic function on a protein is generally understood in the art (Kyte and Doolittle; (1982) J Mol Biol. 157(1):105-32). It is accepted that the relative hydropathic character of the amino acid contributes to the secondary structure of the resultant protein, which in turn defines the interaction of the protein with other molecules, for example, enzymes, substrates, receptors, DNA, antibodies, antigens and the like. As set forth above, in some embodiments, the C-type lectin receptor polypeptide or fragment thereof is coupled to a liposome. As used herein, the term liposome refers to an aqueous or aqueous-buffered compartment enclosed by at least one lipid bilayer. Optionally, liposomes can carry aqueous solutions, compounds, drugs or other substances in the compartment, i.e., internal cavity or space, enclosed by at least one lipid bilayer. Liposomes can vary in size, i.e., diameter. For example, a liposome can have a size of about 1000 nanometers (nm) or less. For example, a liposome can have a size of about 50 nm to about 1000 nm, about 50 nm to about 900 nm, about 50 nm to about 800 nm, about 50 nm to about 700 nm, about 50 nm to about 600 nm, about 50 nm to about 500 nm, about 50 nm to about 400 nm, about 50 nm to about 300 nm, about 50 nm to about 200 nm, or about 50 nm to about 100 nm. Also provided are pluralities or populations of liposomes, wherein the liposomes in the plurality have an average size of about 1000 nanometers (nm) or less. For example, the liposomes in the plurality can have an average size of about 50 nm to about 1000 nm, about 50 nm to about 900 nm, about 50 nm to about 800 nm, about 50 nm to about 700 nm, about 50 nm to about 600 nm, about 50 nm to about 500 nm, about 50 nm to about 400 nm, about 50 nm to about 300 nm, about 50 nm to about 200 nm, or about 50 nm to about 100 nm. In some embodiments, the liposomes in the plurality can have an average size of about 75 nm to 120 nm, about 75 nm to about 110 nm, or about 75 nm to about 100 nm. In some embodiments, the liposomes in the plurality can have am average size of about 50 nm to about 100 nm, about 50 nm to 95 nm, about 50 nm to about 90 nm, about 50 nm to about 85 nm, 50 nm to about 80 nm, about 50 nm to 75 nm, about 70 nm to about 90 nm, or about 50 nm to about 75 nm. In some embodiments, the liposomes cross the blood brain barrier, for example, smaller liposomes of about 50 nm to about 120 nm, of about 50 nm to about 100 nm , or about 50 nm to about 75 nm in size. Liposomes that cross the blood brain barrier can be used to treat brain cancer. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) The liposomes described herein include liposomes comprising a compartment for encapsulation of an agent, for example, an anticancer drug or antineoplastic agent. An encapsulated anticancer drug or antineoplastic agent is an anticancer drug or antineoplastic agent that is completely or partially located in the interior space of the liposome. For example, in any of the liposomes described herein, at least about 75%, 80%, 85%, 90%, 95% or 99% of the anticancer drug or antineoplastic agent is incorporated into the interior space of the liposome or into the lipid bilayer of the liposome. The anticancer or antineoplastic agent can be, but is not limited to a drug, an antisense oligonucleotide, a shRNA, a siRNA, a mRNA, a peptide, an aptamer, a drug, or a small molecule, to name a few. In some embodiments, the nanoparticle is a diagnostic nanoparticle, wherein an imaging agent, for example radiolabeled nuclei, are encapsulated in the nanoparticle. Any of the cancer-targeting nanoparticles described herein, for example, liposomes, can be made by any suitable method known to or later discovered by one of skill in the art, including the methods set forth in the Examples. In general, liposomes can be prepared by a thin film hydration technique followed by a few freeze-thaw cycles. Liposomal suspensions can also be prepared according to methods known to those skilled in the art. Exemplary methods for the preparation of liposomes are described in Akbarzadeh et al. (“Liposome: classification, preparation and applications,” Nanoscale Res. Lett. 8(1): 102 (2013); Vemuri and Rhodes, “Preparation and characterization of liposomes as therapeutic delivery systems: a review;” Pharmaceutica Acta Helvetiae 70(2): 95-111 (1995)), which are hereby incorporated by reference in their entireties. In some embodiments, drug loaded liposomes, for example, DOX- loaded liposomes, can be made by using a transmembrane ammonium sulfate pH gradient. For example, newly formed dehydrated liposomes can be hydrated in a highly pH basic 250 mM solution of (NH4)2SO4, such that this basic ammonium salt is both in the liposomal lumen and in the media surrounding the liposomes. The solution around the liposomes is then replaced with 20 mM (NH4)2SO4, at pH 6.5. Doxorubicin is added to this medium. Because doxorubicin is a weak base and positively charged at pH 6.5, it moves into the liposomes and is exchanged for ammonium ion as it moves out into the media (Haran et al., Biochim Biophys Acta, 1151, 201-15 (1993); Mayer et al., Cancer Lett, 53, 183-90 (1990)). Doxorubicin crystalizes as it is concentrated in the lumen of the liposomes, removing it from the equilibrium formula, which further enhances uptake. In some embodiments, liposomes with high concentrations of luminal PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) doxorubicin can be made using this method (e.g., about 16 mol % relative to moles of liposomal lipid). In general, a variety of lipid components can be used to make liposomes. These include neutral lipids that exist either in an uncharged or neutral zwitterionic form at physiological pH. Such lipids include, for example, diacylphosphatidylcholine, diacylphosphatidylethanolamine, ceramide, sphingomyelin, dihydrosphingomyelin, cephalin, and cerebrosides. In some embodiments, the liposomes comprise phosphatidylcholine or a derivative thereof (e.g., a phosphatidyl choline having an acyl group having 6 to 22 carbon atoms, a diacylphosphatidylcholine, and / or diacylphosphatidylethanolamine). Synthetic derivatives of any of the lipids described herein can also be used to make lipid nanoparticles. Lipid nanoparticles can also comprise a sterol, for example, cholesterol. Lipid nanoparticles can also comprise a cationic lipid which carries a net positive charge at about physiological pH. Such cationic lipids include, but are not limited to, N,N-dioleyl-N,N-dimethylammonium chloride (DODAC); N-(2,3-dioleyloxy)propyl-N,N-N-triethylammonium chloride (DOTMA); N,N- distearyl-N,N-dimethylammonium bromide (DDAB); N-(2,3-dioleoyloxy)propyl)-N,N,N- trimethylammonium chloride (DOTAP); 1,2-Dioleyloxy-3-trimethylaminopropane chloride salt (DOTAP.Cl); 3.beta.-(N--(N',N'-dimethylaminoethane)-carbamoyl)cholesterol ("DC- Chol"), N-(1-(2,3-dioleyloxy)propyl)-N-2-(sperminecarboxamido)ethyl)-N,N-dimethyl- ammonium trifluoroacetate ("DOSPA"), dioctadecylamidoglycyl carboxyspermine (DOGS), 1,2-dileoyl-sn-3-phosphoethanolamine (DOPE), 1,2-dioleoyl-3-dimethylammonium propane (DODAP), N,N-dimethyl-2,3-dioleyloxy)propylamine (DODMA), and N-(1,2- dimyristyloxyprop-3-yl)-N,N-dimethyl-N-hydroxyethyl ammonium bromide (DMRIE). Anionic lipids are also suitable for use in lipid nanoparticles described herein. These include, but are not limited to, phosphatidylglycerol, cardiolipin, diacylphosphatidylserine, diacylphosphatidic acid, N-dodecanoyl phosphatidylethanoloamine, N-succinyl phosphatidylethanolamine, N-glutaryl phosphatidylethanolamine, lysyl phosphatidylglycerol, and other anionic modifying groups joined to neutral lipids. In some examples, the liposome comprises phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, phosphatidylinositol, phosphatidic acid, phosphatidylglycerol, palmitoyloleoyl phosphatidylcholine, lysophosphatidylcholine, lysophosphatidylethanolamine, dimyristoylphosphatidylcholine (DMPC), dipalmitoylphosphatidylcholine (DPPC), dioleoylphosphatidylcholine, distearoylphosphatidylcholine (DSPC), dilinoleoylphosphatidylcholine, a 1,2-distearoyl-sn- PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) glycero-3-phosphoethanolamine (DSPE) conjugated polyethylene glycol (DSPE-PEG), a sphingomyelin, cholesterol, or any combination thereof. In some embodiments, PEG can be PEG-molecular weight (MW500) to PEG-MW20000. In addition to being components of the liposomes described herein, any of the lipids described herein can be attached or conjugated to a C-type lectin receptor polypeptide or a fragment thereof that binds a target antigen. In some embodiments, a lipid can be functionalized with a reactive group such as, for example, N-hydroxysuccinimide (NHS). In some examples, pegylated versions of any of the lipids described herein can be conjugated to a C-type lectin receptor polypeptide or a fragment thereof that binds a target antigen on a cancer cell, or an antigen expressed on a cancer cell. In some examples the targeted antigen is a ligand of any of the C-type lectin receptor polypeptides or a fragments thereof described herein. In some examples, the C-type lectin receptor polypeptide or a fragment thereof binds to a glycan on the surface of the cancer cell. In some embodiments, the the C-type lectin receptor polypeptide or a fragment thereof specifically binds to a tumor-associated glycan. In some embodiments, the nanoparticle, for example, a liposome, comprises about 40 to 70, 45 to 70, 50 to 70, 55 to 70, 60 to 70, or 65 to 70, 40 to 60, 45 to 60, 50 to 60, or 55 to 60 moles percent phosphatidylcholine lipid (e.g., fully hydrogenated soy phosphatidylcholine (18:0-18:1 PC, 1-stearoyl-2-oleoyl-sn-glycero-3-phosphocholine) (HSPC) or 18:10 (n10)- 16:00 PC, 15:0-18:1 PC). In some embodiments, the nanoparticles, for example, a liposome, comprise about 40, 45, 50, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, or 70 mole percent phosphatidylcholine lipid (e.g., fully hydrogenated soy phosphatidylcholine (18:0-18:1 PC, 1-stearoyl-2-oleoyl-sn-glycero-3-phosphocholine) (HSPC) or 18:10 (n10)-16:00 PC, 15:0- 18:1 PC) relative to total lipid content. In some embodiments, the nanoparticle, for example, a liposome, comprises about 20 to about 50, about 25 to about 50, about 30 to about 50, about 35 to about 50, about 40 to about 50, about 45 to about 50, about 20 to about 40, about 25 to about 40, about 30 to about 40, or about 35 to about 40 mole percent cholesterol (e.g., CAS 57-88-0). In some embodiments, the nanoparticle, for example, a liposome, comprises about 20, 25, 30, 35, 40, 45, or 50 mole percent cholesterol relative to total lipid content. In some embodiments, the nanoparticle, for example, a liposome, comprises about 1 to about 6 , about 2 to about 6, about 3 to about 6, about 4 to about 6 or about 5 to about 6 mole percent polyethylene glycol (e.g., methyl PEG-2000-DSPE (18:0 PEG2000 PE) PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) (sodium;[(2R)-2,3-di(octadecanoyloxy)propyl] 2-(2-methoxyethoxycarbonylamino)ethyl phosphate) (CAS 147867-65-0)) relative to total lipid. In some embodiments, the liposome comprises 18:1 PEG2000 PE, 16:0 PEG2000 PE, or 14:0 PEG2000 PE instead of 18:0 PEG2000 PE relative to total lipid content. In addition to lipid components any of the nanoparticles described herein, for example, liposomes, can contain about 0.2 to about 25 mole percent anticancer agents. For example, the nanoparticle can contain about 0.2, 0.3, 0.4, 0.5, 0.6, 0.7, 0.8, 0.9, 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 moles percent or greater of an anticancer agent or imaging agent relative to total lipid content of the liposome. In other words, the nanoparticles can comprise about 0.2:100, 0.3:100, 0.4:100, 0.5:100, 0.6:100, 0.7:100, 0.8:100, 0.9:100, 1:100, 2:100, 3:100, 4:100, 5:100, 6:100, 7:100, 8:100, 9:100, 10:100, 11:100, 12:100, 13:100, 14:100, 15:100, 16:100, 17:100, 18:100, 19:100, 20:100 mole ratio or greater of anticancer agent or imaging agent relative to total lipid content. In some embodiments, the nanoparticle, for example, a liposome can contain about 5 to about 10 mole percent, about 5 to about 15 mole percent, about 5 to about 20 mole percent, or about 5 to about 25 mole percent of an anticancer agent or imaging agent relative to lipid. In other words, the nanoparticles can comprise about 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, or 25 mole percent of an anticancer agent or imaging agent relative to lipid. In some embodiments, the nanoparticles comprise about 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, or 25 mole percent of an anticancer agent relative to lipid, wherein the anticancer agent is selected from the group consisting of doxorubicin, paclitaxel, taxol, cytarabine, mifamurtide, irinotecan, verteporfin, daunorubicin, and vincristine. In some embodiments, the nanoparticle, for example, a liposome, comprises about 0.2 to about 2 mole percent C-type lectin receptor or a fragment thereof relative to total lipid content. For example, the liposome can comprise about 0.2 to about 2, about 0.3 to about 2, about 0.4 to about 2, 0.5 to about 2, 0.6 to about 2, 0.7 to about 2, 0.8 to about 2, 0.9 to about 2, 1.0 to about 2, 1.1 to about 2, 1.2 to about 2, 1.3 to about 2, 1.4 to about 2, 1.5 to about 2, 1.6 to about 2, 1.7 to about 2, 1.8 to about 2 or 1.9 to about 2 mole percent C-type lectin receptor or a fragment thereof relative to total lipid content. In some embodiments, the nanoparticle comprises about 0.2, 0.3, 0.4, 0.5, 0.6, 0.7, 0.8, 0.9, 1, 1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8, 1.9 or 2.0 mole percent C-type lectin receptor or a fragment thereof relative to total lipid content. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) In some embodiments, the nanoparticle, for example, a liposome, comprises about 0.1 to about 5 mole percent imaging agent relative to total lipid content. In some embodiments, In some embodiments, the nanoparticle comprises about 0.1, 0.20.3, 0.4, 0.5, 0.6, 0.7, 0.8, 0.9, 1, 1.5, 2.0, 2.5, 3.0, 3.5, 4.0, 4.5 or 5 mole percent imaging agent relative to lipid. In some embodiments, the imaging agent is a fluorescent imaging agent, such as, for example, rhodamine or fluorescein isothiocyanate. Table 2 provides components and corresponding mole percent ratios for exemplary cancer-targeted nanoparticles comprising doxorubicin and other anticancer agents. Table 2: Components of exemplary cancer-targeted nanoparticles PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) As used herein, mole ratio is the ratio between the amounts in moles of two components, for example, the ratio between the number of moles of a targeting molecule (for example, a C- type lectin receptor or a fragment thereof, and the number of moles of lipid (targeting molecules: moles of lipid) or the number of moles of an anticancer agent and the number of moles of lipid (moles of anticancer agent: moles of lipid). And similarly, the nanoparticles can comprise a 0.002:100, 0.05:100, 0.1:100, 0.5:100, 1:100, 2:100, 3:100, 4:100, 5:100, 10: 100, 15:100, 20:100, 25:100 mole ratio of targeting molecule to liposomal lipid or greater. As used herein, mole percent ratio or mole percentage expresses the concentration of a substance in a mixture as the number of moles of that substance divided by the total number of moles, multiplied by 100. Pluralities of two or more of any of the nanoparticles described herein are also provided. For example, a plurality of liposomes can comprise from about two to about 1 x 1014(100 trillion) liposomes. For example, a plurality can have at least 100, 250, 500, 750, 1000, 5000, 10,000, 25,000, 50,000,100,000, 500,000, 1 million or more liposomes. In some embodiments, at least 80%, 85%, 90%, 95%, or 99% of the liposomes in the plurality comprise and anticancer agent or an imaging agent. Optionally, from two cancer-targeting molecules to about 1,000, 1,500, 2,000, 2,500, 3,000, 3,500, 4,000, 4,500, 5,000, 5,500, 6,000, 6,500, 7,000, 7,500, 8,000, 8,500, 9,000, 9,500 or 10,000 cancer-targeting molecules (e.g., a C-type lectin receptor or fragment thereof) can be coupled to the liposomes provided herein. For example, from about five to about one hundred, about five to about two hundred, about five to about three hundred, about five to about four hundred, about five to about five hundred, about five to about six hundred, about five to about seven hundred, about five to about eight hundred, about five to about nine hundred, about five to about one thousand, about five to about 1100, about five to about 1200, about five to about 1300, about five to about 1400, about five to about 1500, about five to about 1600, about five to about 1700, about five to about 1800, about five to about 1900, about five to about 2000, about five to about 2250, about five to about 2500, or about five to about 3000, about five to PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) about 3500, about five to about 4000, about five to about 4500, about five to about 5000, about five to about 5500, about 5 to about 6000, about 5 to about 6500, about 5 to about 7000, about 5 to about 7500, about 5 to about 8000, about 5 to about 8500, about 5 to about 9000, about 5 to about 9500 or about 5 to about 10,000 cancer-targeting molecules can be incorporated into one or more liposomes described herein. In some examples, about two molecules to about 3,000 cancer-targeting molecules are incorporated into nanoparticles that are between about 50 nm and 100 nm in diameter. Those of skill in the art would know how to calculate the number of C-type lectin receptor polypeptides or fragments thereof that can be incorporated into a nanoparticle, for example between about two and 10,000 C-type lectin receptor polypeptides or fragments thereof or greater depending on the size of the nanoparticle. Diagnostics Also provided is a nanoparticle comprising: (a) a C-type lectin receptor or fragment thereof that binds an antigen on a cancer cell; and (b) a signal-generating molecule, wherein the C-type lectin receptor or fragment thereof is coupled to the surface of the nanoparticle and the signal-generating molecule generates a signal when the C-type lectin receptor or fragment thereof binds the antigen on the cancer cell. In some embodiments the signal-generating molecule is linked to the C-type lectin receptor or fragment thereof. In some embodiments, the signal-generating molecule is incorporated into or attached to the outer surface of the nanoparticle, for example, a liposome. In some embodiments, the signal-generating molecule is a fluorescent dye or fluorescent polypeptide. In some embodiments, the C-type lectin receptor or fragment thereof is linked to the C-terminal and / or an N-terminal fragment of a fluorescent protein. Also provided is a plurality of any of the nanoparticles described herein that comprise a signal-generating molecule. Also provided is a method for detecting cancer in a subject or a sample from a subject comprising: (a) contacting the subject or a sample from the subject with a plurality of any of the cancer-targeted nanoparticles comprising a signaling molecule described herein; (b) detecting a signal, wherein a signal indicates the presence of cancer. In some methods, the C- type lectin receptor or fragment thereof is linked to a fluorescent protein, an antibody or a fragment thereof, or an enzyme. In some methods, the signal is directly or indirectly detected. As used herein, a biological sample is a sample derived from a subject and includes, but is not limited to, any cell, tissue or biological fluid. The sample can be, but is not limited PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) to, blood, plasma, serum, sputum, urine, saliva, bronchoalveolar lavage fluids, biopsy (e.g., tissue or cells isolated from organ tissue, for example, from lung, liver, kidney, skin etc.), vaginal secretion, nasal secretion, skin, gastric secretion, or bone marrow specimens. Methods of Treatment Also provided are methods for treating or preventing cancer in a subject. The methods comprise administering to the subject having cancer or at risk of developing cancer an effective amount of a plurality of any of the nanoparticles described herein. In some embodiments, each nanoparticle in the plurality comprises an anticancer or antineoplastic agent and a C-type lectin receptor or fragment thereof that binds a target antigen on a cancer cell, wherein the C-type lectin receptor or fragment thereof is coupled to the outer surface of the liposome and the anticancer or antineoplastic agent is encapsulated in the liposome. In some embodiments, at least 80%, 85%, 90%, 95%, or 99% of the nanoparticles in the plurality comprise an anticancer or antineoplastic agent and a C-type lectin receptor or fragment thereof that binds a target antigen on a cancer cell, wherein the C-type lectin receptor or fragment thereof is coupled to the outer surface of the liposome and the anticancer or antineoplastic agent is encapsulated in the liposome. Throughout, treat, treating, and treatment refer to a method of reducing or delaying one or more effects or symptoms of cancer. The subject can be diagnosed with cancer. Treatment can also refer to a method of reducing the underlying pathology rather than just the symptoms. The effect of the administration to the subject can have the effect of, but is not limited to, reducing one or more symptoms of the disease, a reduction in the severity of the disease, the complete ablation of the disease, or a delay in the onset or worsening of one or more symptoms. For example, a disclosed method is considered to be a treatment if there is about a 10% reduction in one or more symptoms of the disease in a subject when compared to the subject prior to treatment or when compared to a control subject or control value. Thus, the reduction can be about a 10, 20, 30, 40, 50, 60, 70, 80, 90, 100%, or any amount of reduction in between. As used herein, by prevent, preventing, or prevention is meant a method of precluding, delaying, averting, obviating, forestalling, stopping, or hindering the onset, incidence, severity, or recurrence of a disease or disorder. For example, the disclosed method is considered to be a prevention if there is a reduction or delay in onset, incidence, severity, or recurrence of cancer in a subject susceptible to cancer or recurrence of cancer compared to control subjects susceptible to cancer or recurrence of cancer that did not receive treatment. The reduction or PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) delay in onset, incidence, severity, or recurrence of cancer can be about a 10, 20, 30, 40, 50, 60, 70, 80, 90, 100%, or any amount of reduction in between. The methods provided herein optionally further include administering an effective amount of a second therapeutic agent or therapy to the subject. The second therapeutic agent or therapy can be administered to the subject prior to, simultaneously with, or subsequent to administration of the plurality of nanoparticles. In some methods, the second therapeutic therapy is surgery. In some methods, the second therapeutic agent is a second anticancer agent (e.g., a chemotherapeutic, immunotherapeutic, or cellular therapy (e.g., CAR T cell therapy). Any of the methods described herein can be used to kill cancer cells in in vitro, in vivo or ex vivo methods. As used herein, cancer is a disease characterized by the rapid and uncontrolled growth of aberrant cells. Cancer cells can spread locally or through the bloodstream and lymphatic system to other parts of the body. The cancer can be a solid tumor. In some embodiments, the cancer is a blood or hematological cancer, such as a leukemia Solid tumors include, by way of example, bone and connective tissue sarcomas (e.g., bone sarcoma, osteosarcoma, chondrosarcoma, Ewing's sarcoma, malignant giant cell tumor, fibrosarcoma of bone, chordoma, periosteal sarcoma, soft-tissue sarcomas, angiosarcoma (hemangiosarcoma), fibrosarcoma, Kaposi's sarcoma, leiomyosarcoma, liposarcoma, lymphangiosarcoma, neurilemmoma, rhabdomyosarcoma, synovial sarcoma), brain tumors (e.g., glioma, astrocytoma, brain stem glioma, ependymoma, oligodendroglioma, nonglial tumor, acoustic neurinoma, craniopharyngioma, medulloblastoma, meningioma, pineocytoma, pineoblastoma, primary brain lymphoma), breast cancer (e.g., adenocarcinoma, lobular (small cell) carcinoma, intraductal carcinoma, medullary breast cancer, mucinous breast cancer, tubular breast cancer, papillary breast cancer, Paget's disease, and inflammatory breast cancer), triple negative breast cancer, adrenal cancer (e.g., pheochromocytoma and adrenocortical carcinoma), thyroid cancer (e.g., papillary or follicular thyroid cancer, medullary thyroid cancer and anaplastic thyroid cancer), pancreatic cancer (e.g., insulinoma, gastrinoma, glucagonoma, vipoma, somatostatin- secreting tumor, and carcinoid or islet cell tumor), pituitary cancers (e.g., Cushing's disease, prolactin-secreting tumor, acromegaly, and diabetes insipidus), eye cancers (e.g., ocular melanoma such as iris melanoma, choroidal melanoma, and ciliary body melanoma, and retinoblastoma), vaginal cancers (e.g., squamous cell carcinoma, adenocarcinoma, and melanoma), vulvar cancer (e.g., squamous cell carcinoma, melanoma, adenocarcinoma, basal cell carcinoma, sarcoma, and Paget's disease), cervical cancers (e.g., squamous cell carcinoma PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) and adenocarcinoma), uterine cancers (e.g., endometrial carcinoma and uterine sarcoma), ovarian cancers (e.g., ovarian epithelial carcinoma, borderline tumor, germ cell tumor, and stromal tumor), esophageal cancers (e.g., squamous cancer, adenocarcinoma, adenoid cystic carcinoma, mucoepidermoid carcinoma, adenosquamous carcinoma, sarcoma, melanoma, plasmacytoma, verrucous carcinoma, and oat cell (small cell) carcinoma), stomach cancers (e.g., adenocarcinoma, fungating (polypoid), ulcerating, superficial spreading, diffusely spreading, malignant lymphoma, liposarcoma, fibrosarcoma, and carcinosarcoma), colon cancers, rectal cancers, liver cancers (e.g., hepatocellular carcinoma and hepatoblastoma), gallbladder cancers (e.g., adenocarcinoma), cholangiocarcinomas (papillary, nodular, and diffuse), lung cancers (e.g., non-small cell lung cancer, squamous cell carcinoma (epidermoid carcinoma), adenocarcinoma, large-cell carcinoma and small-cell lung cancer), testicular cancers (e.g., germinal tumor, seminoma, anaplastic, classic (typical), spermatocytic, nonseminoma, embryonal carcinoma, teratoma carcinoma, choriocarcinoma (yolk-sac tumor)), prostate cancers (e.g., adenocarcinoma, leiomyosarcoma, and rhabdomyosarcoma), penile cancers, oral cancers (e.g., squamous cell carcinoma), basal cancers, salivary gland cancers (e.g., adenocarcinoma, mucoepidermoid carcinoma, and adenoidcystic carcinoma), esopharyngeal cancers (e.g., squamous cell cancer and verrucous cancer), skin cancers (e.g., basal cell carcinoma, squamous cell carcinoma and melanoma, superficial spreading melanoma, nodular melanoma, lentigo malignant melanoma, acral lentiginous melanoma), kidney cancers (e.g., renal cell cancer, adenocarcinoma, hypernephroma, fibrosarcoma, transitional cell cancer (renal pelvis and / or ureter), Wilms' tumor), bladder cancers (e.g., transitional cell carcinoma, squamous cell cancer, adenocarcinoma, and carcinosarcoma). In addition, cancers include myxosarcoma, osteogenic sarcoma, endotheliosarcoma, lymphangio endothelio sarcoma, mesothelioma, synovioma, hemangioblastoma, epithelial carcinoma, cystadenocarcinoma, bronchogenic carcinoma, sweat gland carcinoma, sebaceous gland carcinoma, papillary carcinoma and papillary adenocarcinomas. Representative anticancer agents include, but are not limited to amsacrine, bleomycin, busulfan, capecitabine, carboplatin, carmustine, chlorambucil, cisplatin, cladribine, clofarabine, crisantaspase, cyclophosphamide, cytarabine, dacarbazine, dactinomycin, daunorubicin, docetaxel, doxorubicin, epirubicin, etoposide, everolimus, fludarabine, fluorouracil, gemcitabine, hydroxycarbamide, idarubicin, ifosfamide, irinotecan, leucovorin, doxorubicin, daunorubicin, lomustine, melphalan, mercaptopurine, mesna, methotrexate, mitomycin, mitoxantrone, oxaliplatin, paclitaxel, pemetrexed, pentostatin, procarbazine, PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) raltitrexed, satraplatin, streptozocin, tegafur-uracil, temozolomide, teniposide, thiotepa, tioguanine, topotecan, treosulfan, vinblastine, vincristine, vindesine, vinorelbine, or a combination thereof. It is understood that the terms “anticancer agent”, “anticancer drug” and “antineoplastic agent” are used interchangeably throughout. In some embodiments, for example, to treat brain cancer, the anticancer agent is selected from the group consisting of temozolomide, procarbazine, carmustine, lomustine, and vincristine. As used throughout, by subject is meant an individual. The subject can be an adult subject or a pediatric subject. Pediatric subjects include subjects ranging in age from birth to eighteen years of age. Thus, pediatric subjects of less than about 10 years of age, five years of age, two years of age, one year of age, six months of age, three months of age, one month of age, one week of age or one day of age are also included as subjects. Preferably, the subject is an animal, for example, a mammal such as a primate, and, more preferably, a human. Non- human primates are subjects as well. The term subject includes domesticated animals, such as cats, dogs, etc., livestock (for example, cattle, horses, pigs, sheep, goats, etc.) and laboratory animals (for example, ferret, chinchilla, mouse, rabbit, rat, gerbil, guinea pig, etc.). Thus, veterinary uses and medical formulations are contemplated herein. Pharmaceutical Compositions Any of the nanoparticles or pluralities of nanoparticles provided herein can be in a pharmaceutical composition. Uses of any of the pharmaceutical compositions are provided herein, including use of an effective amount of the pharmaceutical composition for the treatment or prevention of cancer. The term effective amount, as used throughout, is defined as any amount necessary to produce a desired physiologic response, for example, treating or preventing cancer. The dosage ranges for administration are those large enough to produce the desired effect in which one or more symptoms of the disease or disorder are affected (e.g., reduced or delayed). The dosage should not be so large as to cause substantial adverse side effects, such as unwanted cross-reactions, unwanted cell death, and the like. Generally, the dosage will vary with the type of inhibitor, the species, age, body weight, general health, sex and diet of the subject, the mode and time of administration, rate of excretion, drug combination, and severity of the particular condition and can be determined by one of skill in the art. The dosage can be adjusted by the individual physician in the event of any contraindications. Dosages can vary and can be administered in one dose or multiple doses administered daily or at extended intervals. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) Any of the liposomes described herein can be provided in a composition, for example, a pharmaceutical composition. The composition can include one or more liposomes disclosed herein. Optionally, the composition comprising one or more liposomes is in a kit. Pharmaceutical compositions include, for example, a pharmaceutical composition comprising a therapeutically effective amount of any of the liposomes described herein and a pharmaceutical carrier. The term carrier means a compound, composition, substance, or structure that, when in combination with a compound or composition, aids or facilitates preparation, storage, administration, delivery, effectiveness, selectivity, or any other feature of the compound or composition for its intended use or purpose. For example, a carrier can be selected to minimize any degradation of the active ingredient and to minimize any adverse side effects in the subject. Such pharmaceutically acceptable carriers include sterile biocompatible pharmaceutical carriers, including, but not limited to, saline, buffered saline, artificial cerebral spinal fluid, dextrose, and water. Pharmaceutical compositions comprising any of the liposomes described herein can be prepared according to standard techniques and further comprise a pharmaceutically acceptable carrier. Generally, normal saline will be employed as the pharmaceutically acceptable carrier. Other suitable carriers include, e.g., water, buffered water or saline, 0.4% saline, 0.3% glycine, dextrose, and the like, including glycoproteins for enhanced stability, such as albumin, lipoprotein, and globulin. These compositions are usually sterile. The pharmaceutical compositions can also contain a pharmaceutically acceptable excipient. Such excipients include any pharmaceutical agent that does not itself induce an immune response harmful to the individual receiving the composition, and which may be administered without undue toxicity. Pharmaceutically acceptable excipients include, but are not limited to, liquids such as water, saline, glycerol, sugars and ethanol. Pharmaceutically acceptable salts can be included therein, for example, mineral acid salts such as hydrochlorides, hydrobromides, phosphates, sulfates, and the like; and the salts of organic acids such as acetates, propionates, malonates, benzoates, and the like. Additionally, auxiliary substances, such as wetting or emulsifying agents, pH buffering substances, and the like, may be present in such vehicles. The preparation of pharmaceutically acceptable carriers, excipients and formulations containing these materials is described in, e.g., Remington: The Science and Practice of Pharmacy, 22nd edition, Loyd V. Allen et al, editors, Pharmaceutical Press (2012). Aqueous solutions can be packaged for use or filtered under aseptic conditions and lyophilized, the lyophilized preparation being combined with a sterile aqueous solution prior PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) to administration. The compositions can contain pharmaceutically acceptable auxiliary substances as required to approximate physiological conditions, such as pH adjusting and buffering agents, tonicity adjusting agents and the like, for example, sodium acetate, sodium lactate, sodium chloride, potassium chloride, and calcium chloride. Additionally, the liposome suspension may include lipid-protective agents which protect lipids against free-radical and lipid-peroxidative damages on storage. Lipophilic free-radical quenchers, such as alphatocopherol and water-soluble iron-specific chelators, such as ferrioxamine, are suitable. The concentration of the nanoparticles (e.g., liposomes) in the pharmaceutical formulations can vary widely, i.e., from less than about 0.05%, usually at or at least about 2- 5% to as much as 10 to 30% by weight and will be selected primarily by fluid volumes, viscosities, in accordance with the particular mode of administration selected. In some instances, the liposomes may be dried or lyophilized and resuspended to a desired concentration in water or buffers at time of use. The amount of active agent in the liposome or plurality of liposomes administered depends upon the particular label used, the disease state being diagnosed and the judgment of the clinician but is generally between about 0.01 and about 150 mg per kilogram of body weight, preferably between, about 0.1 and about 30 mg / kg of body weight, about 0.1 and about 20 mg / kg (e.g., 1 mg / kg, 2mg / kg, 3 mg / kg, 4 mg / kg, 5 mg / kg , 6 mg / kg, 7 mg / kg, 8 mg / kg, 9 mg / kg , 10 mg / kg, 11 mg / kg, 12mg / kg, 13 mg / kg, 14 mg / kg, 15 mg / kg , 16 mg / kg, 17 mg / kg, 18 mg / kg, 19 mg / kg, 20 mg / kg) of body weight, about 0.1 to about 10 mg / kg (e.g., 1 mg / kg, 2mg / kg, 3 mg / kg, 4 mg / kg, 5 mg / kg , 6 mg / kg, 7 mg / kg, 8 mg / kg, 9 mg / kg or 10 mg / kg) of body weight, or about 0.1 to about 5 mg / kg (e.g., 1 mg / kg, 2mg / kg, 3 mg / kg, 4 mg / kg, or 5 mg / kg) of body weight, which may be administered in a single dose or in the form of individual doses, such as from 1 to 4 times per day. Administration can be performed for 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,14, 15, 16, 17, 18, 19, 20 or more days. One of skill in the art would adjust the dosage as described below based on specific characteristics of the agent and the subject receiving it. The compositions disclosed herein are administered in a number of ways depending on whether local or systemic treatment is desired, and on the area to be treated. The compositions are administered via any of several routes of administration, including orally, intranasally, via inhalation, via nebulizer, parenterally, intravenously, intraperitoneally, intracranially, intraspinally, intrathecally, intraventricularly, intramuscularly, subcutaneously, intracavity, transdermally, or via convection-enhanced delivery. Pharmaceutical compositions can also be delivered locally to the area in need of treatment, for example by topical application or local PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) injection. The pharmaceutical compositions can also be delivered via pump or at a surgical site. Effective doses for any of the administration methods described herein can be extrapolated from dose-response curves derived from in vitro or animal model test systems. Disclosed are materials, compositions, and components that can be used for, can be used in conjunction with, can be used in preparation for, or are products of the disclosed methods and compositions. These and other materials are disclosed herein, and it is understood that when combinations, subsets, interactions, groups, etc. of these materials are disclosed that while specific reference of each various individual and collective combinations and permutations of these compounds may not be explicitly disclosed, each is specifically contemplated and described herein. For example, if a method is disclosed and discussed and a number of modifications that can be made to a number of molecules including in the method are discussed, each and every combination and permutation of the method, and the modifications that are possible are specifically contemplated unless specifically indicated to the contrary. Likewise, any subset or combination of these is also specifically contemplated and disclosed. This concept applies to all aspects of this disclosure including, but not limited to, steps in methods using the disclosed compositions. Thus, if there are a variety of additional steps that can be performed, it is understood that each of these additional steps can be performed with any specific method steps or combination of method steps of the disclosed methods, and that each such combination or subset of combinations is specifically contemplated and should be considered disclosed. Publications cited herein and the material for which they are cited are hereby specifically incorporated by reference in their entireties. Embodiments 1. A cancer-targeting nanoparticle comprising: a. an anticancer agent; and b. a C-type lectin receptor or a fragment thereof that is coupled to the surface of the nanoparticle, wherein the C-type lectin receptor or a fragment thereof binds an antigen expressed by a cancer cell. 2. The cancer-targeting nanoparticle of embodiment 1, wherein the anticancer agent is encapsulated in the nanoparticle. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) The cancer-targeting nanoparticle of any of embodiments 1 or 2 , wherein the C-type lectin receptor or fragment thereof is coupled to the surface of the nanoparticle by inserting the C-type lectin receptor or fragment thereof into the surface of the nanoparticle. The cancer-targeting nanoparticle of any of embodiments 1or 2, wherein the C-type lectin receptor or fragment thereof is coupled to the surface of the nanoparticle by attaching the C-type lectin receptor or fragment thereof to the surface of the nanoparticle. The cancer-targeting nanoparticle of any one of embodiments 1-3, wherein the C-type lectin receptor or fragment thereof is selected from the group consisting of Dectin-1 or a fragment thereof, Dectin-2 or a fragment thereof, Dectin-3 or a fragment thereof, and DC-SIGN or a fragment thereof. The cancer-targeting nanoparticle of any one of embodiments 1-4, wherein the C-type lectin receptor fragment is a soluble C-type lectin receptor fragment, wherein the soluble C-type lectin receptor fragment is not a full-length C-type lectin receptor, and wherein the C-type lectin receptor fragment comprises an amino acid sequence having at least 65%, 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 10, SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 16, SEQ ID NO: 18, SEQ ID NO: 41, SEQ ID NO: 42, SEQ ID NO: 43, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46, SEQ ID NO: 47 or SEQ ID NO: 48. The cancer-targeting nanoparticle of embodiment 5, wherein the soluble C-type lectin receptor or a fragment thereof is a soluble human Dectin-1 comprising an amino acid sequence having at least 85%, 90%, 95%, or 99% identity to SEQ ID NO: 1, SEQ ID NO: 14, SEQ ID NO: 40, or a fragment thereof. The cancer-targeting nanoparticle of embodiment 7, wherein the soluble human Dectin-1 comprises: a. SEQ ID NO: 1 or a fragment thereof; or PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) b. a polypeptide comprising amino acids 35-214 of SEQ ID NO: 14 or a fragment thereof. The cancer-targeting nanoparticle of embodiment 5, wherein the soluble C-type lectin receptor or a fragment thereof is a soluble human Dectin-2 comprising an amino acid sequence having at least 85%, 90%, 95%, or 99% identity to SEQ ID NO: 2, SEQ ID NO: 16, SEQ ID NO: 41 or a fragment thereof. The cancer-targeting nanoparticle of embodiment 9, wherein the soluble human Dectin-2 comprises: c. SEQ ID NO: 2 or a fragment thereof; or d. a polypeptide comprising amino acids 35-203 of SEQ ID NO: 16, or a fragment thereof. The cancer-targeting nanoparticle of embodiment 5, wherein the soluble C-type lectin receptor or a fragment thereof is a soluble human Dectin-3 comprising an amino acid sequence having at least 85%, 90%, 95%, or 99% identity to SEQ ID NO: 3, SEQ ID NO: 18, SEQ ID NO: 42 or a fragment thereof. The cancer-targeting nanoparticle of embodiment 11, wherein the soluble human Dectin-3 comprises: e. SEQ ID NO: 3 or a fragment thereof; or f. a polypeptide comprising amino acids 35-207 of SEQ ID NO: 18 or a fragment thereof. The cancer-targeting nanoparticle of any one of embodiments 1-5, wherein the C-type lectin receptor comprises a Dendritic Cell-Specific Intercellular adhesion molecule-3- Grabbing Non-integrin (DC-SIGN) polypeptide or a fragment thereof. The cancer-targeting nanoparticle of any one of embodiments 1-13, wherein the C- type lectin receptor fragment comprises a carbohydrate recognition domain (CRD). The cancer-targeting nanoparticle of embodiment 13 or 14, wherein the DC-SIGN polypeptide comprises a DC-SIGN CRD (SEQ ID NO: 21) and one or more neck PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) regions of DC-SIGN selected from the group consisting of (NR1) SEQ ID NO: 22, (NR2) SEQ ID NO: 23, (NR3) SEQ ID NO: 24, (NR4) SEQ ID NO: 25, (NR5) SEQ ID NO: 26, (NR6) SEQ ID NO: 27, (NR7) SEQ ID NO: 28 and (NR8) SEQ ID NO: 29. The cancer-targeting nanoparticle of embodiment 15, wherein the DC-SIGN polypeptide comprises a DC-SIGN CRD (SEQ ID NO: 21), NR1 (SEQ ID NO: 22) and NR2 (SEQ ID NO: 23). The cancer-targeting nanoparticle of embodiment 16, wherein the DC-SIGN polypeptide has at least 90% identity to SEQ ID NO: 32. The cancer-targeting nanoparticle of embodiment 15, wherein the DC-SIGN polypeptide comprises a DC-SIGN CRD (SEQ ID NO: 21), NR7 (SEQ ID NO: 28) and NR8 (SEQ ID NO: 29). The cancer-targeting nanoparticle of embodiment 18, wherein the DC-SIGN polypeptide has at least 90% identity to SEQ ID NO: 30. The cancer-targeting nanoparticle of any one of embodiments 15-19, wherein the DC- SIGN CRD (SEQ ID NO: 21) and the one or more neck regions are joined with one or more linkers. The cancer-targeting nanoparticle of any one of embodiments 1-20, wherein the C- type lectin receptor or fragment thereof is conjugated to a lipid carrier. The cancer-targeting nanoparticle of embodiment 21, wherein the lipid carrier is a DSPE lipid moiety. The cancer-targeting nanoparticle of embodiment 22, wherein the DSPE lipid moiety is DSPE-PEG. The cancer-targeting nanoparticle of any one of embodiments 1-20, wherein the concentration of the anticancer agent is reduced as compared to the concentration of PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) the anticancer agent in a nanoparticle that does not comprise a C-type lectin receptor or a fragment thereof coupled to the surface of the nanoparticle. The cancer-targeting nanoparticle of any one of embodiments 1-21, wherein the antigen is a tumor-specific antigen. The cancer-targeting nanoparticle of embodiment 25, wherein the tumor-specific antigen is solid tumor antigen. The cancer-targeting nanoparticle of embodiment 26, wherein the solid tumor antigen is a breast tumor antigen, a prostrate tumor antigen or a lung tumor antigen. The cancer-targeting nanoparticle of any one of embodiments 25-27, wherein the tumor-specific antigen is a glycan. The cancer-targeting nanoparticle of any one of embodiments 1-28, wherein the nanoparticle is a liposome. The cancer-targeting nanoparticle of embodiment 29, wherein the liposome comprises from about 40 to about 70 mole percent phosphatidylcholine relative to total lipid content. The cancer-targeting nanoparticle of embodiment 30, wherein the liposome comprises from about 50 to about 70 mole percent phosphatidylcholine relative to total lipid content. The cancer-targeting nanoparticle of any one of embodiments 30-31, wherein the liposome comprises from about 50 to about 60 mole percent phosphatidylcholine relative to total lipid content. The cancer-targeting nanoparticle of any one of embodiments 30-32, wherein the liposome comprises from about 55 to about 60 mole percent phosphatidylcholine relative to total lipid content. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) The cancer-targeting nanoparticle of any one of embodiments 30-33, wherein the phosphatidylcholine is fully hydrogenated soy phosphatidylcholine (18:0-18:1 PC, 1- stearoyl-2-oleoyl-sn-glycero-3-phosphocholine). The cancer-targeting nanoparticle of any one of embodiments 29-34, wherein the liposome comprises about 20% to 50% mole percent cholesterol relative to total lipid content. The cancer-targeting nanoparticle of embodiment 35, wherein the liposome comprises about 35% to 40% mole percent cholesterol relative to total lipid content. The cancer targeting nanoparticle of any one of embodiments 29-36, wherein the liposome comprises about 1 to about 6 mole percent polyethylene glycol (PEG) relative to total lipid content. The cancer targeting nanoparticle of embodiment 37, wherein the liposome comprises about 4 to about 6 mole percent polyethylene glycol (PEG) relative to total lipid content. The cancer targeting nanoparticle of embodiment 38, wherein the PEG is mPEG- 2000-DSPE (18:0 PEG2000 PE) (sodium;[(2R)-2,3-di(octadecanoyloxy)propyl] 2-(2- methoxyethoxycarbonylamino)ethyl phosphate). The cancer-targeting nanoparticle of any of embodiments 29-39, wherein the liposome comprises about 5 to 25 mole percent anti-cancer agent relative to total lipid content. The cancer-targeting nanoparticle of any of embodiments 29-40, wherein the liposome comprises about 10 to 25 mole percent anti-cancer agent relative to total lipid content. The cancer-targeting nanoparticle of any of embodiments 29-41, wherein the liposome comprises about 10 to 20 mole percent anti-cancer agent relative to total lipid content. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) The cancer-targeting nanoparticle of any of embodiments 29-42, wherein the liposome comprises about 0.3 to about 1.2 mole percent C-type lectin receptor or a fragment thereof relative to total lipid content. A plurality of cancer-targeting nanoparticles according to any one of embodiments 1- 43 Use of the cancer-targeting nanoparticle of any one of embodiments 30-43 or the plurality of embodiment 44 for the treatment of cancer. A pharmaceutical composition comprising a plurality of cancer-targeting nanoparticles according to any one of embodiments 1-43. A nanoparticle comprising: g. a C-type lectin receptor or fragment thereof that binds an antigen on a cancer cell; and h. a signal-generating molecule, wherein the C-type lectin receptor or fragment thereof is coupled to the surface of the nanoparticle and the signal-generating molecule generates a signal when the C-type lectin receptor or fragment thereof binds the antigen on the cancer cell. The nanoparticle of embodiment 47, wherein the C-type lectin receptor or fragment thereof is selected from the group consisting of Dectin-1 or a fragment thereof, Dectin- 2 or a fragment thereof, Dectin-3, and DC-SIGN or a fragment thereof. The nanoparticle of embodiment 48, wherein the signal-generating molecule is linked to the C-type lectin receptor or fragment thereof. The nanoparticle of any one of embodiments 47-49, wherein the C-type lectin receptor or a fragment thereof is a soluble C-type lectin receptor or a fragment thereof. The nanoparticle of embodiment 50, wherein the soluble C-type lectin receptor or a fragment thereof is a human Dectin-1 comprising an amino acid sequence having at PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) least 85%, 90%, 95%, or 99% identity to SEQ ID NO: 1, SEQ ID NO: 14, SEQ ID NO: 40, or a fragment thereof. The nanoparticle of embodiment 51, wherein the soluble human Dectin-1 comprises SEQ ID NO: 1 or a fragment thereof. The nanoparticle of embodiment 50, wherein the the soluble C-type lectin receptor or a fragment thereof is a soluble human Dectin-2 comprising an amino acid sequence having at least 85%, 90%, 95%, or 99% identity to SEQ ID NO: 2, SEQ ID NO: 16, SEQ ID NO: 41 or a fragment thereof. The nanoparticle of embodiment 53, wherein the soluble human Dectin-2 comprises SEQ ID NO: 2 or a fragment thereof. The nanoparticle of embodiment 50, wherein the the soluble C-type lectin receptor or a fragment thereof is a soluble human Dectin-3 comprising an amino acid sequence having at least 85%, 90%, 95%, or 99% identity to SEQ ID NO: 3, SEQ ID NO: 18, SEQ. ID NO: 42 or a fragment thereof. The nanoparticle of embodiment 55, wherein the soluble human Dectin-3 comprises SEQ ID NO: 3 or a fragment thereof. The nanoparticle of any one of embodiments 47-50, wherein the C-type lectin receptor comprises a Dendritic Cell-Specific Intercellular adhesion molecule-3- Grabbing Non-integrin (DC-SIGN) polypeptide or a fragment thereof. The nanoparticle of embodiment 57, wherein the DC-SIGN polypeptide comprises a DC-SIGN CRD (SEQ ID NO: 21) and one or more neck regions of DC-SIGN selected from the group consisting of (NR1) SEQ ID NO: 22, (NR2) SEQ ID NO: 23, (NR3) SEQ ID NO: 24, (NR4) SEQ ID NO: 25, (NR5) SEQ ID NO: 26, (NR6) SEQ ID NO: 27, (NR7) SEQ ID NO: 28 and (NR8) SEQ ID NO: 29. The nanoparticle of embodiment 58, wherein the DC-SIGN polypeptide comprises a DC-SIGN CRD (SEQ ID NO: 21), NR1 (SEQ ID NO: 22) and NR2 (SEQ ID NO: 23). PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) The nanoparticle of embodiment 59, wherein the DC-SIGN polypeptide has at least 90% identity to SEQ ID NO: 32. The nanoparticle of embodiment 58, wherein the DC-SIGN polypeptide comprises a DC-SIGN CRD (SEQ ID NO: 21), NR7 (SEQ ID NO: 28) and NR8 (SEQ ID NO: 29). The nanoparticle of embodiment 61, wherein the DC-SIGN polypeptide has at least 90% identity to SEQ ID NO: 30. The nanoparticle of any one of embodiments 58-62, wherein the DC-SIGN CRD (SEQ ID NO: 21) and the one or more neck regions are joined with one or more linkers. The nanoparticle of any one of embodiments 47-63, wherein the signal-generating molecule is incorporated into or attached to the surface of the nanoparticle. The nanoparticle of any one of embodiments 47-64, wherein the signal-generating molecule is a fluorescent dye or fluorescent polypeptide. The nanoparticle of embodiment 65, wherein the C-type lectin receptor or fragment thereof is linked to the C-terminal and / or an N-terminal fragment of a fluorescent protein, an antibody or a fragment thereof or an enzyme. The nanoparticle of any one of embodiments 47-66, wherein the nanoparticle is a liposome. A method of treating or preventing cancer in a subject comprising administering to the subject having cancer or at risk of developing cancer an effective amount of the pharmaceutical composition of embodiment 46. The method of embodiment 68, wherein the subject has breast cancer, prostate cancer or lung cancer. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) . The method of embodiment 68 or 69, wherein a second therapeutic agent or therapy is administered to the subject. . The method of embodiment 70, wherein the second therapeutic agent or therapy is surgery, radiation or immunotherapy. . The method of embodiment 71, wherein the second therapeutic agent is a second anticancer agent. . The method of any one of embodiments 68-72, wherein the anticancer agent is a drug, a peptide or an antibody. . The method of embodiment 73, wherein the drug is a chemotherapeutic drug. . The method of embodiment 74, wherein the chemotherapeutic drug is doxorubicin.. Use of the pharmaceutical composition of embodiment 46 for the treatment of cancer.. The use of embodiment 76, wherein the cancer is breast cancer, prostate cancer or lung cancer. . The use of embodiment 76 or 77, wherein the anticancer agent is a drug, a peptide or an antibody. . The use of embodiment 78, wherein the drug is a chemotherapeutic drug. . The use of embodiment 79, wherein the chemotherapeutic drug is doxorubicin. . A method for detecting cancer in a subject or a sample from a subject comprising: a) contacting the subject or a sample from the subject with the plurality of nanoparticles of any one of embodiments 47-67; and b) detecting a signal, wherein a signal indicates the presence of cancer. . The method of embodiment 81, wherein the signal is a fluorescent signal. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) 83. The method of embodiment 81 or 82, wherein the signal is directly or indirectly detected. EXAMPLE I The following examples are provided by way of illustration only and not by way of limitation. Those of skill in the art will readily recognize a variety of non-critical parameters that could be changed or modified to yield essentially the same or similar results. Methods Liposomal preparations Liposome preparations used to stain cells were prepared as described previously (Ambati et al. mSPhere 4:1-16 (2019)) starting with commercial 100 nm diameter pegylated liposomes from FormuMax Sci. Inc. (Sunnyvale, CA) (F10203A, DSPC:CHOL:mPEG-DSPE (50:45:5 mol / mol). All liposomes were remotely loaded with 2 mol percent DHPE-rhodamine B relative to 100 moles percent liposomal lipid. The 22 kDa PEG-DSPE modified CRD and stalk regions of mouse Dectin-1 (SEQ ID NO: 8), Dectin-2 (SEQ ID ON: 10), Dectin-3 (SEQ ID NO: 12) and human DC-SIGN isoform DCS12 (SEQ ID NO: 32) were loaded at 1 mol percent. PEG- DSPE modified Bovine serum albumin was loaded at only 0.33 moles percent to account for the three-fold larger 66 kDa molecular size of BSA. Hence, by weight the protein-coated liposome control BSA-Ls had the same amount of protein on its surface. Binding to in vitro grown cells The various cancer cell lines and human fetal epithelial kidney (HEK-293T) cells (ATCC CRL-1573) were grown in 24 well microtiter plates in RPMI media plus 10% fetal calf serum and lacking red indicator dye. When cells were to 50 to 90% confluence, they were washed with growth media, and stained live for 1 hr with CTL coated, BSA coated, or plain AmB-LLs, and bovine serum albumin coated BSA-AmB-LLs in their growth media. For staining all three liposome preparations were diluted to the same degree, which for the CTL and BSA coated liposomes meant 1:200, w:v, protein:media. The cells were washed thrice with media and photographed at 10X magnification taking bright field and red epifluorescent images on ECHO RSVF1000 / REVOLVE R4 microscope (VWR International, Radnor PA) in the inverted PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) position. In some cases, the cells were costained with DAPI (4′,6-diamidino-2-phenylindole) in which case the DAPI channel was recorded in place of the visible light channel. The rhodamine red channel was merged with the bright field channel to generate the images presented. The area of red fluorescence was measured in ImageJ using our recently developed Cell Profiler pipeline AreaPipe to automate and standardize ImageJ analysis of large stacks of fluorescent images (Choudhury et al., J Fungi 8: 1-14 (2023)). Results Design of a cancer cell targeted nanoparticle An exemplary design of a CTL-targeted nanoparticle bound to a cancer cell is shown in FIG.1. To build a CTL-targed nanoaparticle, a plain, pegylated bilipid membrane liposome was used. This liposome contains the CRD and stalk region of a CTL such as Dectin-2 conjugated to the lipid carrier DSPE-PEG, which was then inserted into the liposomal membrane via the DSPE lipid moiety. DHPE-rhodamine B is inserted via its DHPE lipid moiety so that binding to cells can be monitored and quantified by fluorescence. CRD and Rhodamine were loaded at 1 and 2 mol percent, respectively, relative to moles of liposomal lipid in a 100 nm liposome. To prepare an anti-cancer cell nanoparticle (FIG.1) liposomes pre- loaded with an anti-cancer drug, for example, Doxil® (a.k.a., Doxosome), which is loaded with 16 mol % doxorubicin (DOX) relative to moles of liposomal lipid, were used. These studies focused on determining whether C-Type Lectin-coated nanoparticles bind efficiently to cancer cell lines representing diverse types of cancer. Nanoparticles coated with the DC-SIGN isoform (DCS12-Ls), Dectin-1 (DEC1-Ls), Dectin-2 (DEC2-Ls), and Dectin-3 (DEC3-Ls) were prepared. BSA coated BSA-Ls, an untargeted protein coated control, and plain liposomes, lacking any protein as an additional control, were prepared. All six of the preparations of liposomes do not contain the DOX shown in FIG.1. Representative breast, prostate, and lung cancer cell lines (Table 1) and control cell lines were grown on the surface of 24 well plastic microtiter plates to between 50% and 90% confluence and washed once with growth media. The cancer cell lines employed did not lend themselves to cytometric assays of reagent binding, because they tend to grow best attached to a surface. Cells were stained for 1 hr with various targeted and untargeted liposomes and washed extensively. Ten random images of fluorescent liposome binding were taken for each treatment and the area of red fluorescent liposome binding quantified. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) Table 1. Cell lines examined for binding Breast Cancer In the representative experiment shown in FIG.2, DEC1-Ls, DEC2-Ls and DEC3-Ls bound very efficiently to the triple-negative (ER-, PR-, HER2-) breast cancer cell line MDA- MB-231. For each treatment ten random fields of cells were identified by DAPI nuclear staining and then photographed using combined blue DAPI and red Rhodamine fluorescence. The red fluorescent images were used to quantify liposome binding. Note the numerous fluorescent red spots of liposome staining in FIG.2B, 2C & 2D. Respectively, DEC1-Ls, DEC2-Ls and DEC3-Ls bound 1,700-fold (p=0.0017), ~6,900-fold (p=2x10-5) and ~3,800- fold (p=3x10-5) more strongly than the background binding by BSA-Ls protein coated PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) control (FIG.2E & 2G). Untargeted liposomes did not bind significantly. Z-stack images at 20X suggest that DEC2-Ls bound to patches of glycoprotein on the exposed top surface of the cells (FIG. H). CTL liposome binding appears to be specific for only one or a few glycoprotein membrane rafts on the surface of any one cell. Biological and experimental replicates of this experiment showed nearly identical results. DEC2-Ls bound up to 80% of the cells in some microscopic fields. A similar result was obtained for DEC1-Ls, DEC2-Ls and DEC3-Ls staining of a triple positive breast cancer cell line MCF7. This demonstration of such strong specific binding encouraged examination of cancer cell lines representative of other cancers. Prostate cancer The experiment illustrated in FIG.3 examined DCS-12-Ls, DEC1-Ls, DEC2-Ls and DEC3-Ls binding to the prostate epithelial adenocarcinoma cancer cell line PC3. As shown by the numerous red patches of targeted nanoparticle binding in FIG.3B, 3C, and 3D, DEC1- Ls, DEC2-Ls and DEC3-Ls bound 2,600-fold (p=9.6x10-6), 6,400-fold (p=2.6x10-10) and 5,800-fold (p=2.5x10-8) more strongly (FIG.3G), respectively, than untargeted BSA-Ls (FIG.3E). Untargeted fluorescent liposomes did not bind significantly. A biological replicate experiment gave similar results. Other prostate cell lines such as, but not limited to, DU-145 and LNCaP-LN3, can also be examined using methodology as described above.. FFPE prostate patient tumor samples are available from TissueArray.com and other sources. Lung cancer The representative experiment in FIG.4 examines DCS12-Ls, DEC1-Ls, DEC2-Ls and DEC3-Ls binding to the non-small cell lung carcinoma (NSCLC) cancer line A594. As shown by the numerous red patches of targeted nanoparticle binding in FIG.4B, 4C, and 4D. DEC1-Ls, DEC2-Ls and DEC3-Ls bound 2,200-fold (p=9.6x10-4), 11,000-fold (p=8.3x10-6) and 4,700-fold (p=1.3x10-6) more strongly, respectively (FIG.4G), than untargeted BSA-Ls (FIG.4E). Untargeted fluorescent Ls did not bind. A biological replicate experiment gave similar results. Other metastatic lung cancer cell lines that can be examined using methodology described above include H-1975 and HCC-827. FFPE NSCLC patient tumor samples are available from TissueArray and other sources. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) Control cells As a negative control, binding to HEK293T cells was examined. These human embryonic kidney cells were artificially immortalized first by transformation with sheared fragments of adenovirus type 5 DNA that delivered oncogene analogs E1A and E1B and then with SV40 T antigen gene (Kovesdi and Hedley, Viruses 2: 1681-1703 (2010)). For each treatment ten random fields of cells identified in bright field and then photographed using combined bight field and red fluorescence. Red fluorescence was used to quantify liposome binding. In most of the photographic images, red fluorescence from liposome binding was absent as shown in the representative images above (FIG.5). DEC1-L, DEC2-L and DEC3-L binding was of relatively low or no statistical significance as compared to binding by BSA-L control liposomes (FIG.5 G). DC-SIGN-Ls and plain Ls did not bind. A replicate experiment produced similar results. Other negative control cells that can be used include epithelial primary lung, prostate, and breast cell lines from American Type Culture Collection (ATCC). Summary of binding data Targeted nanoparticles bound to breast, prostate and lung cancer cells compared to non-cancer control HEK293T cells. DEC1-Ls, DEC2-Ls, and DEC3-L bound with remarkable strength and specificity to diverse types of cancer cells. It was surprising that DEC2-Ls and DEC3-Ls bound so efficiently to all of these various cancer cell types. C-type lectin receptor targeted inhibition and killing of in vitro grown cells Doxorubicin loaded 100 nm liposomes, DOX-LL, were purchased from Encapsula Nano Sciences (Doxil®, SKU# DOX-1000). The DOX-LLs contain 16 mol % DOX relative to moles of lipid. These liposomes were coated with the CRDs of Dectin-1, Dectin-2, and Dectin-3, and DC-SIGN at 1 mol % to make four kinds of CTL targeted liposomes (i.e., DCS12-DOXIL, DEC1-DOXIL, DEC2-DOXIL, and DEC3-DOXIL) To assay DOX loaded liposome inhibition and killing of cancer cells, MDA-MB-231 cells, i.e., triple negative breast cancer cells, were grown in DMEM + 10% fetal calf serum in microtiter plate at 37oC with 5% CO2. Cells were grown to about 25% density and treated once daily with Doxil®or various C-type lectin receptor-targeted versions of Doxil®delivering 10 μM or 5 μM DOX for 2 hr, after which the media was replaced with drug free media until the next day. Dead cells were washed off the plate with each change of media. A PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) Cell Titer Blue (CTB) assay of metabolic activity in live cells was performed a few hr after treatment on the third day. Statistics and graphics The binding data from AreaPipe and cell killing data were first processed in Microsoft Excel (version 16.76) and moved into Graph Pad Prism Version 10.0.2, where bar plots or scatter bar plots were prepared. P values were estimated using the Student’s T Test program, T.Test, in Excel. When a data set from one or both members of a comparison contained non- parametric data (i.e., not normally distributed), more conservative Mann Whitney PMW values were estimated in Prism. Cancer cell-killing experiments The efficacy of DCS12-DOXIL, DEC1-DOXIL, DEC3-DOXIL, and DEC3-DOXIL to inhibit and / or kill MDA-MB-231 triple negative breast cancer cells was tested. Cells were grown to ~25% density and treated once a day with commercial DOXIL® and C-type lectin- receptor targeted liposomes (DCS12-DOXIL, DEC1-DOXIL, DEC3-DOXIL, and DEC3- DOXIL) delivering 10 uM or 5 uM DOX, and control cells were treated with the liposomal buffer. After 2 hr of being treated with these DOXIL reagents, reagents were replaced with fresh media each day. A Cell Titer Blue (CTB) assay of metabolic activity in live cells was performed a few hr after treatment on the third day (FIG.7). DOXIL reduced cell activity several fold relative to the control cells (FIG.7A). DCS12-DOXIL, DEC1-DOXIL, DEC3- DOXIL, and DEC3-DOXIL delivering 10 uM DOX all showed order of magnitude improvements in cell killing of the triple negative breast cancer cells relative to DOXIL (FIG. 7A, second bar vs bar 3, 4, 5, and 6). For example, DEC2-DOXIL treated cells had 22-fold lower metabolic activity (PMW=0.0002). In other words, there was 95% more killing than by DOXIL itself. C-type lectin targeted liposomes delivering 5 uM DOX were less effective relative to DOXIL® (FIG.3B). Clearly, C-type lectin receptor targeting dramatically improved the performance of DOXIL. These studies showed that Dectin-1, Dectin-2, Dectin-3 (MCL) and DSC-12 coated liposomes bind and kill cancer cells, for example, triple negative breast cancer cells. It was surprising that, although Dectin-1, Dectin-2, and Dectin-3 coated liposomes bound to relatively small patches on the surface of cancer cell lines, these C-type receptor targeted liposomes were highly efficient at killing cancer cells, as shown in FIG.7. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) EXAMPLE II DEC2-DOX-LLs specifically stain cancer cells in human Ductal Carcinoma In Situ (DCIS) tissue sections. Methods Tissue Arrays Formalin Fixed Paraffin Embedded (FFPE) human breast cancer tissue arrays (Version CHTN_BrCaProg3) were obtained from the Cooperative Human Tissue Network (CHTN, Rockville, MD). Seven samples were from seven different patients with high (H) levels of human Ductal Carcinoma In Situ (DCIS-H) and seven different non-neoplastic breast samples from seven patients without breast carcinoma (NB-NC) were on each array. FFPE patient TNBC tumor tissue samples, HuCAT292, were obtained from TissueArray (Derwood, MD). Reagents LDB2 tissue blocking, labeling and washing buffer (20 mM HEPES, 10 mM triethanolamine, 150 mM NaCl, 10 mM CaCl2, 1 mM BME, 5% BSA w / v, pH 8.0). DAPI at 5 ug / 1000 uL in LDB2. DAPI diluted to 1 ug / 100 uL in LDB2. Liposomes DEC2-DOX-LLs and DOX-LLs tagged with lissamine rhodamine B were prepared as described above. DEC2-DOX-LLs we diluted so that DEC2 protein concentration was at 1.0 ug / 150 uL (1:150 w / v) in LDB2 liposome dilution buffer. Control DOX-LL were diluted equivalently. Staining the FFPE tissue arrays Microscope slides with the FFPE tissue BrCaProg3 arrays or FFPE patient TNBC tumor sections were deparaffinized at the University of Georgia’s (UGA) Veterinary Diagnostic Laboratory. The area with tissue sections was encircled with a Liquid repellent pencil-Liquid blocker (Agar Scientific Inc., Rotherham, UK). All procedures were carried out at room temperature. FFPE tissue samples was blocked for 30 min to 1 hr with ~600 uL of LDB2 that covered the area within the repellent border. This solution was replaced with ~600 uL of liposomes diluted into LDB2 and incubated for one hr. The samples were washed PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) briefly twice with 600 uL of LDB2 and then stained for 30 min with DAPI. The sample was washed twice more. All but 20 to 50 uL of the LDB2 was removed and a coverslip was placed over the array. The slides were sealed with clear finger-nail polish, which was let dry for 20 min. Parallel slides were stained with Hematoxylin and Eosin (H&E) at the UGA Veterinary Diagnostic Laboratory. Microscopy Images (.jpg) were taken on a RVSF1000 REVOLVE R4 microscope (VWR International, LLC, Radnor, PA) top down using a 20X 0.8 NA lens. Fluorescent merged images were taken combining the TXRED red fluorescent channel (Ex560 / Em630) to visualize liposomes and the DAPI blue channel (Ex380 / Em450) to visualize nuclei. Red and blue, fluorescent channels were equivalently enhanced by 50% in brightness to make viewing easier. The blue channel was then removed to view the red fluorescent liposome staining alone. H&E-stained-sections were photographed with the same lens in bright field. Figures were assembled in PowerPoint, converted to a pdf, captured, and then converted flattened jpg image in Photoshop for presentation herein. Results Specific binding of DEC2-DOX-LLs to patient Ductal Carcinoma In Situ DCIS-H tissue FFPE human breast cancer tissue arrays with one set of seven patient samples scored as having high levels of Ductal Carcinoma In Situ (DCIS-H) were stained with DEC2-DOX- LLs and control DOX-LLs (FIG.8). DEC2-DOX-LLs-stained tissue with the DCIS-H morphology in 4 of the 7 patient samples. An example image from one patient with the red and blue, fluorescent channels merged is shown in FIG.8A top. The purple area shows the concentration of red fluorescent DEC2-DOX-LL staining in the areas with tightly packed blue, fluorescent nuclei. The red liposome channel alone is shown below (FIG.8A bottom). An H&E-stained section from a duplicate BrCaProg3 array shows that the typical morphology of DCIS-H tumors (FIG.8D) matches the morphology of the DEC2-DOX-LL- stained tissue. DOX-LLs did not stain tissue with the DCIS-H, morphology (FIG.8B), although some background punctate red fluorescent staining was observed in most images. DEC2-DOX-LL did not significantly stain control non-neoplastic breast from patients without breast carcinoma (a.k.a., NB-NC) with ductal morphology (FIG.8C), although again some background red fluorescent staining was observed in most images. The scatter bar plot in FIG.8E shows that DEC2-DOX-LLs bound to cancer tissues about 31-fold (P=1.9x10- PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1)4)more strongly than did DOX-LLs and 28-fold (P=5.3x10-4) more strongly than to NB-NC tissue. Specific binding of DEC2-DOX-LLs to patient TNBC tumor tissue sections. FFPE tissue tumor sections from patients with TNBC breast cancer were stained with DEC2-DOX- LLs and control DOX-LLs. Example images with the red liposomes and blue, fluorescent nuclei are shown in FIG.9 (A & B, top row). TNBC tumor cells have been characterized as small and disorganized with very little cytoplasm (Schmadeka et al., 2014. Am J Clin Path, 141:462-477). H&E-stained images of an adjacent tissue section confirmed that regions within adjacent tissue sections had cells with this expected morphology (FIG.8C). Using DAPI staining as a guide in the microscope, regions of the tissue having cells with this morphology were easily identified and photographed. Close examination of FIG 9A shows DEC2-DOX-LLs staining in a tight ring around the nuclei, matching this phenotype and as expected for cells with scant cytoplasm. Untargeted DOX-LLs staining showed some red fluorescent background, but background staining was not concentrated in TNBC cells (FIG. 9B). Quantification of the red fluorescent pixel areas from several randomly taken original images of cells with TNBC morphology (FIG.1D) showed that the DEC2-DOX-LLs stained a 100-fold larger area than DOX-LLs (p =5.5x10-7). The staining of red blood cells seen in capillaries (FIG.9A and 9B) and other background staining results is likely the results from the transfer of lissamine rhodamine from liposome membranes to membrane rich cells. FIGS. 14A-13B also show that DEC2-DOX-LLs labeled TNBC tissue within a TNBC patient tumor FFPE breast tissue section far more efficiently than untargeted DOX-LLs. (HuCAT292 FFPE tissue section from TissueArray.) In another exemplary experiment, as shown in FIGS.10A-10B, DEC2-DOX-LLs labeled the metastatic triple negative breast cancer (TNBC) cell line MDA-MB-468 far more efficiently than untargeted DOX-LLs. In another exemplary experiment, as shown in FIGS.11A-11B, DEC2-DOX-LLs labeled the metastatic HER2 overexpressing breast cancer cell line SKBR3 far more efficiently than untargeted DOX-LLs. In another exemplary experiment, DEC2-DOX-LLs labeled the metastatic triple negative breast cancer (TNBC) cell line MDA-MB-231 far more efficiently than untargeted DOX-LLs. See, FIGS.12A-12B. Also, as shown in FIGS.13A-B, DEC2-DOX-LLs labeled the metastatic non-small cell lung carcinoma (NSCLC) cell line A549 far more efficiently than untargeted DOX-LLs. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) FIGS.14A-B showed that DEC2-DOX-LLs label TNBC tissue within a TNBC patient tumor FFPE breast tissue section HuCAT292 far more efficiently than untargeted DOX-LLs. Similar results are expected with other metastatic breast cancer cells lines such as, but not limited to, other TNBC cell lines (for example, BT-20, HCC-79, and BT-549). Non- metastatic breast cancer cell lines such as, but not limited to MCF-7, can also be examined using methodology as described above. Additional tumor samples that can be examined, for example, other FFPE TNBC patient tumor samples, are available from TissueArray and other sources. These exemplary studies showed that Dectin-2 targeted rhodamine tagged DEC2-DOX- LLs specifically stained two types of breast cancer cells in FFPE tissue sections, with little background staining by DOX-LLs. DEC2-DOX-LLs specifically stained cancerous mammary ductal DCIS-H tissue in patient tissue arrays, but not breast tissue from healthy individuals. DOX-LLs did not bind cancerous mammary ductal DCIS-H tissue in these same patient tissue samples. DEC2-DOX-LLs specifically stained TNBC cells in patient tissue samples, and DOX-LLs did not. Additional experiments using FFPE tissue sections of mouse xenografted human tumors (e.g., MDA-MB-231 and BT474), available from Charles River Labs can also be used in staining studies (as described above) for any of the C-type lectin receptors or fragments thereof described herein. TNBC breast tumor sections, such as HUCAT292 are commercially available from TissueArray. Mouse Xenograft Model The efficacy of DEC2-DOX-LL DectiSomes in mouse xenograft models of three deadly metastatic cancers, non-small cell lung carcinoma (NSCLC), prostate cancer, and triple negative breast cancer (TNBC) can be determined. When Dectin-2 coated DOXIL DectiSomes (DEC2-DOX-LLs) are delivered intravenously (i.v.) to mice with various metastatic tumors, the drug can reach tumor cells and kill or inhibit the tumor growth more effectively than commercial DOXIL (DOX-LLs). A significant reduction in the dose of DOX required when it is delivered by DEC2-DOX-LLs is expected. Establishing improved efficacy at a reduced dose in mice, using multiple xenograft models, can be extrapolated into efficacy with reduced toxicity to patients relative to untargeted DOXIL or other cancer drugs. PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) Successful xenografts of human cancer cells into mice, require that the mice are immunodeficient (Sargent et al. “Genetically diverse mouse platform to xenograft cancer cells,” Dis Model Mech 15, 10.1242 / dmm 049457 (2022)). NOD / ShiLtJ-Rag1em5Lutzy / J inbred RAG KO mice or NOD SCID NOD.Cg-Prkdcscid / J mice (JAX:001303) can be used for these experiments. They are both deficient in both B and T cells, and readily xenograft (Hudson et al. Leukemia 12, 2029-33.10.1038 / sj.leu.2401236 (1998). Well-characterized metastatic cell lines to establish tumors in mice, including NSCLC cell lines (A549, H-1975, and HCC-827), prostate cancer cell lines (PC-3, DU-145, and LNCaP-LN3), and the TNBC cell lines (MDA-MB-231, MDA-MB-468, BT-20, HCC-70 and BT-549), can be used. Mice will be given a subcutaneous injection (s.c.) in both flanks with 5x106cells on Day 0 (D0) (Jones et al., Leukemia 12, 2029-33.10.1038 / sj.leu.2401236 2005)). The goal is to achieve satisfactory xenograft model tumor volumes of 150 to 200 mm3(Vt=(length x width2) x 2) at D21 (3 weeks). However, three-week tumor volumes can vary. Although variation can occur, one of skill in the art would know how to obtain adequate tumor volumes for these studies. The ability of DEC2-DOX-LLs to suppress tumor growth relative to DOXIL (DOX- LLs) will be studied. A mock treatment control will be included. On D7, D14 and D21 after initiating s.c. tumors, mice will be given a retro-orbital (intravenous) injection of the liposome reagents. Treatment will be started with both type of liposomes delivering 4 mg / kg DOX, but doses can range from 1 to 10 mg / kg. A set of mock treated control mice with tumors will be given liposomal buffer. Reductions in tumor size greater than 50% at D28 and 50% survival at D42 can be expected. It is possible that higher leves of tumor size reduct and survival will be observed during these time frames. Survival studies will be carried out for 5 to 8 weeks, but the time necessary to reach a humane endpoint will likely vary widely among NSCLC, prostate, and TNBC cancers and cell lines. Power analysis. An exemplary power analysis for TNBC tumors is provided below. Following various therapeutic treatments (Georgievski et al., 2024 Cell Death Dis 15, 328. 10.1038 / s41419-024-06715-5; Hong et al., 2016 Int Neurourol J 20, S2-7. 10.5213 / inj.1632604.302; Kazan et al., 2019 Cancers (Basel) 11, 10.3390 / cancers11040460; Kim et al., 2013 J Clin Biochem Nutr 53, 21-6.10.3164 / jcbn.12-78; Schade et al., 2023) PLoS Biol 21, e3002038.10.1371 / journal.pbio.3002038), reductions in MDA-MB-231 murine xenograft tumor volume (Vt) range from 2- to 10- fold, but were typically 2-fold. Power analysis will be based on effect sizes (Tomczak and Tomczak, 2014 Trends in Sport PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) Sciences 21, 19-25; Vargha and Delaney, 2000 Journal of Educational and Behavioral Statistics 25, 101-132.10.3102 / 10769986025002101) while avoiding both Type I (false positive) and Type II (false negative) errors (Happ et al., 2019 Stat Med 38, 363-375. 10.1002 / sim.7983). In this power analysis, a 2-fold effect size will be used, with a conservative estimate of the final control tumor volume reaching a conservative size of 1,000 mm3and a desired P value of 0.01. https: / / clincalc.com / stats / samplesize.aspx was used as the sample size calculator to estimate that four mice per treatment per experiment are needed. However, six mice in each treatment group analysis will be used to ensure statistically significant results. The statistical significance of survival data will be determined using the Wilcoxon rank sum test (Mollan et al., 2019 "Exact Power of the Rank-Sum Test for a Continuous Variable," arXiv e-prints arXiv:1901.04597.; Noether, 1987 "Sample Size Determination for Some Common Nonparametric Tests," Journal of the American Statistical Association 82, 645-647.10.2307 / 2289477; Shieh et al., 2006 Journal of Nonparametric Statistics 18, 33-43.10.1080 / 10485250500473099). Toxicity. Quantitative microtiter plate assay kits will be used to assess serum levels of urea nitrogen (BUN) and creatinine (Ray Biotech, # MA-BUN-1 and # MA-CTNSP-2, respectively) to see if liver or kidney toxicity, respectively, can be detected. Since in vitro binding and killing data provided herein for metastatic cancer cells are so strong, significant suppression of xenograft tumor growth and improved survival are expected . Treatment of Cancer A subject that has cancer (e.g., breast cancer, prostate cancer, lung cancer or brain cancer) can be treated using any of the pharmaceutical compositions or methods described herein. For example, an effective amount of any of the plurality of C-type receptor targeted nanoparticles comprising an anticancer agent described herein (for example, C-type receptor targeted liposomes comprising about 5 to 25% mole percent anticancer agent relative to total lipid content of the liposome) can be administered intravenously to a subject. Intravenous delivery can be perfomed by infusion of the plurality of nanoparticles over the course of 15 minutes to an hour or more. The subject can be dosed in this manner, for example, once every few weeks (for example, every three or four weeks), for as long as the cancer in the subject PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) does not progress, shows no evidence of cardiotoxicity and continues to tolerate treatment. In some embodiments, for example, in the treatment of brain cancer, the plurality of nanoparticles is delivered via intracarotid, intranasal, intracranial, intraperitoneal, or convection-enhanced delivery. In some cases, the subject will undergo monthly treatments for two, three, four or months. At predetermined timepoints, a clinician can assess whether the subject is responding to treatment or not. If the subject is not responding or the subject is experiencing adverse effects, the dosage of the anticancer agent can be altered or a second therapeutic agent can be added to the subject treatment regimen. SEQUENCES Human Dectin-1 (SEQ ID NO: 1) IWRSNSGSNTLENGYFLSRNKENHSQPTQSSLEDSVTPTKAVKTTGVLSSPCPPNWII YEKSCYLFSMSLNSWDGSKRQCWQLGSNLLKIDSSNELGFIVKQVSSQPDNSFWIGL SRPQTEVPWLWEDGSTFSSNLFQIRTTATQENPSPNCVWIHVSVIYDQLCSVPSYSICE KKFSM Human Dectin-2 (SEQ ID NO: 2) TYHFTYGETGKRLSELHSYHSSLTCFSEGTKVPAWGCCPASWKSFGSSCYFISSEEKV WSKSEQNCVEMGAHLVVFNTEAEQNFIVQQLNESFSYFLGLSDPQGNNNWQWIDKT PYEKNVRFWHLGEPNHSAEQCASIVFWKPTGWGWNDVICETRRNSICEMNKIYL Human Dectin-3 (SEQ ID NO: 3) HNFSRCKRGTGVHKLEHHAKLKCIKEKSELKSAEGSTWNCCPIDWRAFQSNCYFPLT DNKTWAESERNCSGMGAHLMTISTEAEQNFIIQFLDRRLSYFLGLRDENAKGQWRW VDQTPFNPRRVFWHKNEPDNSQGENCVVLVYNQDKWAWNDVPCNFEASRICKIPG TTLN Mouse Dectin-1 (SEQ ID NO: 4) FWRHNSGRNPEEKDSFLSRNKENHKPTESSLDEKVAPSKASQTTGGFSQSCLPNWIM HGKSCYLFSFSGNSWYGSKRHCSQLGAHLLKIDNSKEFEFIESQTSSHRINAFWIGLSR NQSEGPWFWEDGSAFFPNSFQVRNAVPQESLLHNCVWIHGSEVYNQICNTSSYSICE KEL Mouse Dectin-2 (SEQ ID NO: 5) IMDQPSRRLYELHTYHSSLTCFSEGTMVSEKMWGCCPNHWKSFGSSCYLISTKENFW STSEQNCVQMGAHLVVINTEAEQNFITQQLNESLSYFLGLSDPQGNGKWQWIDDTPF SQNVRFWHPHEPNLPEERCVSIVYWNPSKWGWNDVFCDSKHNSICEMKKIYL PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) Mouse Dectin-3 (SEQ ID NO: 6) HNFSRCKRGTGVHKLEHHAKLKCIKEKSELKSAEGSTWNCCPIDWRAFQSNCYFPLT DNKTWAESERNCSGMGAHLMTISTEAEQNFIIQFLDRRLSYFLGLRDENAKGQWRW VDQTPFNPRRVFWHKNEPDNSQGENCVVLVYNQDKWAWNDVPCNFEASRICKIPG TTLN Human DC-SIGN (SEQ ID NO: 19) MSDSKEPRLQQLGLLEEEQLRGLGFRQTRGYKSLAGCLGHGPLVLQLLSFTLLAGLL VQVSKVPSSISQEQSRQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELP EKSKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTWLKAAVGELPEKSKMQEIYQE LTRLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGEL PEKSKQQEIYQELTQLKAAVERLCHPCPWEWTFFQGNCYFMSNSQRNWHDSITACK EVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDLNQEGTWQWVDGSPLLPSFKQ YWNRGEPNNVGEEDCAEFSGNGWNDDKCNLAKFWICKKSAASCSRDEEQFLSPAP ATPNPPPA Human DC-SIGN signal sequence and transmembrane domain (SEQ ID NO: 20) MSDSKEPRLQQLGLLEEEQLRGLGFRQTRGYKSLAGCLGHGPLVLQLLSFTLLAGLL VQVSKVPSSISQE SEQ ID NO: 21 Carbohydrate Recognition Domain (CRD) of DC-SIGN CHPCPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQLQSS RSNRFTWMGLSDLNQEGTWQWVDGSPLLPSFKQYWNRGEPNNVGEEDCAEFSGNG WNDDKCNLAKFWICKKSAASCSRDEEQFLSPAPATPNPPPA SEQ ID NO: 22 (NR1) of DC-SIGN QSRQDAIYQNLTQLKAAVGEL SEQ ID NO: 23 (NR2) of DC-SIGN SEKSKLQEIYQELTQLKAAVGEL SEQ ID NO: 24 (NR3) of DC-SIGN PEKSKLQEIYQELTRLKAAVGEL SEQ ID NO: 25 (NR4) of DC-SIGN PEKSKLQEIYQELTWLKAAVGEL SEQ ID NO: 26 (NR5) of DC-SIGN PEKSKMQEIYQELTRLKAAVGEL SEQ ID NO: 27 (NR6) of DC-SIGN PEKSKQQEIYQELTRLKAAVGEL SEQ ID NO: 28 (NR7) of DC-SIGN PEKSKQQEIYQELTRLKAAVGEL SEQ ID NO: 29 (NR8) of DC-SIGN PEKSKQQEIYQELTQLKAAVERL PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) SEQ ID NO: 30 (full-length DCS78) MAHHHHHHYGT GSG KGK GSGSG GELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTQLKAAVERLCHPCPWEW TFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWM GLSDLNQEGTWQWVDGSPLLPSFKQYWNRGEPNNVGEEDCAEFSGNGWNDDKCN LAKFWICKKSAASCSRDEEQFLSPAPATPNPPPA SEQ ID NO: 31 (nucleic acid encoding DCS78) GGTACCATGGCTCACCATCACCACCACCATTATGGAACTGGTTCTGGCAAGGGCA AGGGCAGCGGCAGCGGTGGAGAACTACCCGAGAAGTCAAAACAGCAAGAGATT TACCAGGAGTTGACTCGTCTGAAGGCGGCGGTGGGCGAACTTCCGGAAAAATCG AAACAGCAGGAGATCTACCAAGAGTTGACGCAGTTGAAGGCGGCGGTTGAACGT CTGTGTCATCCGTGTCCGTGGGAATGGACCTTCTTCCAGGGCAACTGCTATTTCA TGTCTAACAGCCAGAGAAATTGGCACGACAGCATTACCGCATGTAAAGAAGTTG GTGCACAGCTGGTGGTGATCAAATCTGCGGAGGAACAAAACTTTCTCCAACTGC AATCCAGCCGTAGCAATCGTTTTACCTGGATGGGTCTGAGCGACCTGAATCAGGA GGGCACCTGGCAGTGGGTTGACGGCTCGCCGCTGCTGCCATCATTTAAACAATAT TGGAACCGCGGTGAACCGAACAACGTCGGTGAGGAAGATTGCGCCGAGTTCAGC GGTAACGGCTGGAACGATGACAAGTGCAATCTGGCAAAGTTCTGGATCTGCAAG AAATCCGCGGCCAGCTGCAGCCGCGATGAAGAGCAATTTTTATCCCCGGCTCCG GCGACCCCGAATCCGCCTCCGGCTTAATTAA SEQ ID NO: 32 (full-length DCS12) MAHHHHHHYGTGSGKGKGSGSGQSRQDAIYQNLTQLKAAVGELSEKSKLQEIYQE LTQLKAAVERLCHPCPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSA EEQNFLQLQSSRSNRFTWMGLSDLNQEGTWQWVDGSPLLPSFKQYWNRGEPNNVG EEDCAEFSGNGWNDDKCNLAKFWICKKSAASCSRDEEQFLSPAPATPNPPPA SEQ ID NO: 33 (nucleic acid encoding DCS12) GGTACCATGGCTCACCATCACCACCACCATTATGGAACTGGTTCTGGCAAGGGTA AGGGTAGCGGCTCTGGCCAGAGCAGACAAGACGCAATTTACCAGAACCTGACCC AGCTTAAGGCGGCGGTTGGCGAGCTGTCCGAAAAAAGCAAACTGCAAGAGATCT ACCAAGAGTTGACGCAGTTGAAGGCTGCTGTGGAACGTCTGTGCCATCCGTGTCC GTGGGAATGGACCTTTTTCCAGGGTAACTGCTATTTCATGAGCAACAGCCAGCGT AATTGGCACGACTCGATCACCGCGTGCAAAGAAGTTGGTGCACAGCTGGTCGTG ATCAAAAGCGCGGAGGAACAAAACTTTTTGCAACTCCAATCAAGTCGCTCCAAT CGTTTCACCTGGATGGGTCTGTCGGATCTGAATCAGGAGGGCACCTGGCAATGG GTTGATGGCAGCCCGCTGCTGCCGAGCTTTAAACAGTATTGGAACCGCGGTGAG CCGAATAACGTGGGCGAAGAAGATTGTGCGGAGTTCAGCGGTAATGGTTGGAAC GACGACAAGTGCAACCTGGCGAAATTCTGGATTTGTAAAAAGTCTGCAGCCTCCT GCAGCCGTGATGAAGAGCAGTTTTTGTCCCCGGCGCCAGCTACGCCGAACCCGC CGCCTGCTTAATTAA SEQ ID NO: 34 (DCS12345678) PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) MAHHHHHHYGTGSGKGKGSGSGQSRQDAIYQNLTQLKAAVGELSEKSKLQEIYQE LTQLKAAVGELPEKSKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTWLKAAVGEL PEKSKMQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQ ELTRLKAAVGELPEKSKQQEIYQELTQLKAAVERLCHPCPWEWTFFQGNCYFMSNS QRNWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDLNQEGTWQ WVDGSPLLPSFKQYWNRGEPNNVGEEDCAEFSGNGWNDDKCNLAKFWICKKSAAS CSRDEEQFLSPAPATPNPPPA SEQ ID NO: 35 (na encoding DCS12345678) ATGGCTCACCATCACCACCACCATTATGGAACCGGTAGCGGCAAGGGTAAAGGC TCTGGTTCTGGTCAGAGCCGCCAGGATGCGATTTATCAAAACCTGACCCAACTGA AGGCTGCTGTGGGTGAACTTTCAGAAAAGAGCAAGTTACAAGAAATTTACCAAG AGCTCACGCAGCTGAAAGCGGCCGTTGGCGAGTTGCCGGAGAAGTCGAAGCTGC AAGAGATTTACCAAGAACTTACCCGTTTGAAGGCTGCGGTAGGGGAGCTGCCGG AAAAATCCAAACTGCAAGAAATCTACCAGGAGCTCACGTGGCTGAAGGCTGCGG TGGGCGAGTTGCCAGAAAAGTCCAAAATGCAGGAGATCTACCAAGAGCTGACGC GTTTAAAGGCGGCGGTCGGCGAGCTGCCGGAAAAATCTAAGCAACAGGAGATCT ACCAGGAGTTGACTCGCTTAAAGGCGGCTGTGGGCGAGTTGCCGGAAAAGTCCA AGCAACAAGAGATCTACCAAGAGTTAACACGTTTGAAAGCGGCGGTCGGTGAGT TGCCAGAAAAGTCGAAACAGCAAGAGATCTATCAGGAACTGACCCAGCTCAAAG CCGCCGTGGAAAGACTGTGCCATCCGTGTCCGTGGGAATGGACCTTTTTCCAAGG TAACTGCTATTTCATGAGCAACAGCCAGCGTAATTGGCACGACAGCATTACCGCA TGTAAAGAAGTTGGCGCACAGCTGGTTGTGATTAAATCTGCAGAAGAACAAAAT TTTCTGCAGCTGCAGAGCAGCCGCTCGAACCGTTTCACCTGGATGGGTCTGTCCG ACCTGAATCAGGAGGGCACCTGGCAGTGGGTTGATGGTTCGCCGCTGCTGCCGA GCTTTAAACAGTATTGGAATCGCGGTGAGCCGAACAACGTTGGCGAGGAAGATT GTGCGGAATTTAGCGGCAACGGTTGGAACGACGACAAATGCAATCTGGCAAAAT TCTGGATCTGCAAGAAATCCGCAGCGAGTTGCAGCCGTGATGAAGAGCAGTTCC TGAGCCCGGCGCCGGCGACCCCGAACCCGCCTCCGGCT

Claims

PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) What is claimed is:

1. A cancer-targeting nanoparticle comprising: a. an anticancer agent; and b. a C-type lectin receptor or a fragment thereof that is coupled to the surface of the nanoparticle, wherein the C-type lectin receptor or a fragment thereof binds an antigen expressed by a cancer cell.

2. The cancer-targeting nanoparticle of claim 1, wherein the anticancer agent is encapsulated in the nanoparticle.

3. The cancer-targeting nanoparticle of claim 1, wherein the C-type lectin receptor or fragment thereof is coupled to the surface of the nanoparticle by inserting the C-type lectin receptor or fragment thereof into the surface of the nanoparticle.

4. The cancer-targeting nanoparticle of claim 1, wherein the C-type lectin receptor or fragment thereof is coupled to the surface of the nanoparticle by attaching the C-type lectin receptor or fragment thereof to the surface of the nanoparticle.

5. The cancer-targeting nanoparticle of claim 1, wherein the C-type lectin receptor or fragment thereof is selected from the group consisting of Dectin-1 or a fragment thereof, Dectin-2 or a fragment thereof, Dectin-3 or a fragment thereof, and DC-SIGN or a fragment thereof.

6. The cancer-targeting nanoparticle of claim 1, wherein the C-type lectin receptor or a fragment thereof is a soluble C-type lectin receptor or a fragment thereof, optionally wherein the soluble C-type lectin receptor fragment is not a full-length C-type lectin receptor, optionally wherein the soluble C-type lectin receptor fragment comprises an amino acid sequence having at least 80%, 85%, 90%, 95%, or 99% identity to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 10, SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 16, SEQ ID NO: 18, SEQ ID NO: 41, SEQ ID NO: 42, SEQ ID NO: 43, SEQ ID NO: 44 or SEQ ID NO: 45.PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) 7. The cancer-targeting nanoparticle of claim 5, wherein the soluble C-type lectin receptor or a fragment thereof is a soluble human Dectin-1 comprising an amino acid sequence having at least 85%, 90%, 95%, or 99% identity to SEQ ID NO: 1, SEQ ID NO: 14, SEQ ID NO: 40, or a fragment thereof.

8. The cancer-targeting nanoparticle of claim 7, wherein the soluble human Dectin-1 comprises: a. SEQ ID NO: 1 or a fragment thereof; or b. a polypeptide comprising amino acids 35-214 of SEQ ID NO: 14 or a fragment thereof.

9. The cancer-targeting nanoparticle of claim 5, wherein the soluble C-type lectin receptor or a fragment thereof is a soluble human Dectin-2 comprising an amino acid sequence having at least 85%, 90%, 95%, or 99% identity to SEQ ID NO: 2, SEQ ID NO: 16, SEQ ID NO: 41 or a fragment thereof.

10. The cancer-targeting nanoparticle of claim 9, wherein the soluble human Dectin-2 comprises: a. SEQ ID NO: 2 or a fragment thereof; or b. a polypeptide comprising amino acids 35-203 of SEQ ID NO: 16, or a fragment thereof.

11. The cancer-targeting nanoparticle of claim 5, wherein the soluble C-type lectin receptor or a fragment thereof is a soluble human Dectin-3 comprising an amino acid sequence having at least 85%, 90%, 95%, or 99% identity to SEQ ID NO: 3, SEQ ID NO: 18, SEQ ID NO: 42 or a fragment thereof.

12. The cancer-targeting nanoparticle of claim 11, wherein the soluble human Dectin-3 comprises: a. SEQ ID NO: 3 or a fragment thereof; or b. a polypeptide comprising amino acids 35-207 of SEQ ID NO: 18 or a fragment thereof.PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) 13. The cancer-targeting nanoparticle of claim 1, wherein the C-type lectin receptor comprises a Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Non- integrin (DC-SIGN) polypeptide or a fragment thereof.

14. The cancer-targeting nanoparticle of claim 1, wherein the C-type lectin receptor fragment comprises a carbohydrate recognition domain (CRD).

15. The cancer-targeting nanoparticle of claim 13, wherein the DC-SIGN polypeptide comprises a DC-SIGN CRD (SEQ ID NO: 21) and one or more neck regions of DC- SIGN selected from the group consisting of (NR1) SEQ ID NO: 22, (NR2) SEQ ID NO: 23, (NR3) SEQ ID NO: 24, (NR4) SEQ ID NO: 25, (NR5) SEQ ID NO: 26, (NR6) SEQ ID NO: 27, (NR7) SEQ ID NO: 28 and (NR8) SEQ ID NO:

29.

16. The cancer-targeting nanoparticle of claim 15, wherein the DC-SIGN polypeptide comprises a DC-SIGN CRD (SEQ ID NO: 21), NR1 (SEQ ID NO: 22) and NR2 (SEQ ID NO: 23).

17. The cancer-targeting nanoparticle of claim 16, wherein the DC-SIGN polypeptide has at least 90% identity to SEQ ID NO:

32.

18. The cancer-targeting nanoparticle of claim 15, wherein the DC-SIGN polypeptide comprises a DC-SIGN CRD (SEQ ID NO: 21), NR7 (SEQ ID NO: 28) and NR8 (SEQ ID NO: 29).

19. The cancer-targeting nanoparticle of claim 18, wherein the DC-SIGN polypeptide has at least 90% identity to SEQ ID NO:

30.

20. The cancer-targeting nanoparticle of claim 15, wherein the DC-SIGN CRD (SEQ ID NO: 21) and the one or more neck regions are joined with one or more linkers.

21. The cancer-targeting nanoparticle of any one of claims 1-20, wherein the C-type lectin receptor or fragment thereof is conjugated to a lipid carrier.

22. The cancer-targeting nanoparticle of claim 21, wherein the lipid carrier is a DSPE lipid moiety.PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) 23. The cancer-targeting nanoparticle of claim 22, wherein the DSPE lipid moiety is DSPE-PEG.

24. The cancer-targeting nanoparticle of any one of claims 1-23, wherein the concentration of the anticancer agent is reduced as compared to the concentration of the anticancer agent in a nanoparticle that does not comprise a C-type lectin receptor or a fragment thereof coupled to the surface of the nanoparticle.

25. The cancer-targeting nanoparticle of any one of claims 1-24, wherein the antigen is a tumor-specific antigen.

26. The cancer-targeting nanoparticle of claim 25, wherein the tumor-specific antigen is solid tumor antigen.

27. The cancer-targeting nanoparticle of claim 26, wherein the solid tumor antigen is a breast tumor antigen, a prostrate tumor antigen or a lung tumor antigen.

28. The cancer-targeting nanoparticle of any one of claims 25-27, wherein the tumor- specific antigen is a glycan.

29. The cancer-targeting nanoparticle of any one of claims 1-28, wherein the nanoparticle is a liposome.

30. The cancer-targeting nanoparticle of claim 29, wherein the liposome comprises from about 40 to about 70 mole percent phosphatidylcholine relative to total lipid content.

31. The cancer-targeting nanoparticle of claim 30, wherein the liposome comprises from about 50 to about 70 mole percent phosphatidylcholine relative to total lipid content.

32. The cancer-targeting nanoparticle of any one of claims 30-31, wherein the liposome comprises from about 50 to about 60 mole percent phosphatidylcholine relative to total lipid content.PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) 33. The cancer-targeting nanoparticle of any one of claims 30-32, wherein the liposome comprises from about 55 to about 60 mole percent phosphatidylcholine relative to total lipid content.

34. The cancer-targeting nanoparticle of any one of claims 30-33, wherein the phosphatidylcholine is fully hydrogenated soy phosphatidylcholine (18:0-18:1 PC, 1- stearoyl-2-oleoyl-sn-glycero-3-phosphocholine).

35. The cancer-targeting nanoparticle of any one of claims 29-34, wherein the liposome comprises about 20% to 50% mole percent cholesterol relative to total lipid content.

36. The cancer-targeting nanoparticle of claim 35, wherein the liposome comprises about 35% to 40% mole percent cholesterol relative to total lipid content.

37. The cancer targeting nanoparticle of any one of claims 29-36, wherein the liposome comprises about 1 to about 6 mole percent polyethylene glycol (PEG) relative to total lipid content.

38. The cancer targeting nanoparticle of claim 37, wherein the liposome comprises about 4 to about 6 mole percent polyethylene glycol (PEG) relative to total lipid content.

39. The cancer targeting nanoparticle of claim 38, wherein the PEG is mPEG-2000-DSPE (18:0 PEG2000 PE) (sodium;[(2R)-2,3-di(octadecanoyloxy)propyl] 2-(2- methoxyethoxycarbonylamino)ethyl phosphate).

40. The cancer-targeting nanoparticle of any of claims 29-39, wherein the liposome comprises about 5 to 25 mole percent anti-cancer agent relative to total lipid content.

41. The cancer-targeting nanoparticle of any of claims 29-40, wherein the liposome comprises about 10 to 25 mole percent anti-cancer agent relative to total lipid content.

42. The cancer-targeting nanoparticle of any of claims 29-41, wherein the liposome comprises about 10 to 20 mole percent anti-cancer agent relative to total lipid content.PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) 43. The cancer-targeting nanoparticle of any of claims 29-42, wherein the liposome comprises about 0.3 to about 1.2 mole percent C-type lectin receptor or a fragment thereof relative to total lipid content.

44. A plurality of cancer-targeting nanoparticles according to any one of claims 1-43 45. Use of the cancer-targeting nanoparticle of any one of claims 30-43 or the plurality of claim 44 for the treatment of cancer.

46. A pharmaceutical composition comprising a plurality of cancer-targeting nanoparticles according to any one of claims 1-43.

47. A nanoparticle comprising: a. a C-type lectin receptor or fragment thereof that binds an antigen on a cancer cell; and b. a signal-generating molecule, wherein the C-type lectin receptor or fragment thereof is coupled to the surface of the nanoparticle and the signal-generating molecule generates a signal when the C-type lectin receptor or fragment thereof binds the antigen on the cancer cell.

48. The nanoparticle of claim 47, wherein the C-type lectin receptor or fragment thereof is selected from the group consisting of Dectin-1 or a fragment thereof, Dectin-2 or a fragment thereof, Dectin-3, and DC-SIGN or a fragment thereof.

49. The nanoparticle of claim 48, wherein the signal-generating molecule is linked to the C-type lectin receptor or fragment thereof.

50. The nanoparticle of any one of claims 47-49, wherein the C-type lectin receptor or a fragment thereof is a soluble C-type lectin receptor or a fragment thereof.

51. The nanoparticle of claim 50, wherein the soluble C-type lectin receptor or a fragment thereof is a human Dectin-1 comprising an amino acid sequence having at least 85%, 90%, 95%, or 99% identity to SEQ ID NO: 1, SEQ ID NO: 14, SEQ ID NO: 40, or a fragment thereof.PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) 52. The nanoparticle of claim 51, wherein the soluble human Dectin-1 comprises SEQ ID NO: 1 or a fragment thereof.

53. The nanoparticle of claim 50, wherein the the soluble C-type lectin receptor or a fragment thereof is a soluble human Dectin-2 comprising an amino acid sequence having at least 85%, 90%, 95%, or 99% identity to SEQ ID NO: 2, SEQ ID NO: 16, SEQ ID NO: 41 or a fragment thereof.

54. The nanoparticle of claim 53, wherein the soluble human Dectin-2 comprises SEQ ID NO: 2 or a fragment thereof.

55. The nanoparticle of claim 50, wherein the the soluble C-type lectin receptor or a fragment thereof is a soluble human Dectin-3 comprising an amino acid sequence having at least 85%, 90%, 95%, or 99% identity to SEQ ID NO: 3, SEQ ID NO: 18, SEQ. ID NO: 42 or a fragment thereof.

56. The nanoparticle of claim 55, wherein the soluble human Dectin-3 comprises SEQ ID NO: 3 or a fragment thereof.

57. The nanoparticle of any one of claims 47-50, wherein the C-type lectin receptor comprises a Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Non- integrin (DC-SIGN) polypeptide or a fragment thereof.

58. The nanoparticle of claim 57, wherein the DC-SIGN polypeptide comprises a DC- SIGN CRD (SEQ ID NO: 21) and one or more neck regions of DC-SIGN selected from the group consisting of (NR1) SEQ ID NO: 22, (NR2) SEQ ID NO: 23, (NR3) SEQ ID NO: 24, (NR4) SEQ ID NO: 25, (NR5) SEQ ID NO: 26, (NR6) SEQ ID NO: 27, (NR7) SEQ ID NO: 28 and (NR8) SEQ ID NO:

29.

59. The nanoparticle of claim 58, wherein the DC-SIGN polypeptide comprises a DC- SIGN CRD (SEQ ID NO: 21), NR1 (SEQ ID NO: 22) and NR2 (SEQ ID NO: 23).

60. The nanoparticle of claim 59, wherein the DC-SIGN polypeptide has at least 90% identity to SEQ ID NO: 32.PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) 61. The nanoparticle of claim 58, wherein the DC-SIGN polypeptide comprises a DC- SIGN CRD (SEQ ID NO: 21), NR7 (SEQ ID NO: 28) and NR8 (SEQ ID NO: 29).

62. The nanoparticle of claim 61, wherein the DC-SIGN polypeptide has at least 90% identity to SEQ ID NO:

30.

63. The nanoparticle of any one of claims 58-62, wherein the DC-SIGN CRD (SEQ ID NO: 21) and the one or more neck regions are joined with one or more linkers.

64. The nanoparticle of any one of claims 47-63, wherein the signal-generating molecule is incorporated into or attached to the surface of the nanoparticle.

65. The nanoparticle of any one of claims 47-64, wherein the signal-generating molecule is a fluorescent dye or fluorescent polypeptide.

66. The nanoparticle of claim 65, wherein the C-type lectin receptor or fragment thereof is linked to the C-terminal and / or an N-terminal fragment of a fluorescent protein, an antibody or a fragment thereof or an enzyme.

67. The nanoparticle of any one of claims 47-66, wherein the nanoparticle is a liposome.

68. A method of treating or preventing cancer in a subject comprising administering to the subject having cancer or at risk of developing cancer an effective amount of the pharmaceutical composition of claim 46.

69. The method of claim 68, wherein the subject has breast cancer, prostate cancer or lung cancer.

70. The method of claim 68 or 69, wherein a second therapeutic agent or therapy is administered to the subject.

71. The method of claim 70, wherein the second therapeutic agent or therapy is surgery, radiation or immunotherapy.PATENT ATTORNEY DOCKET NO.0U6500-1491008 (010WO1) 72. The method of claim 71, wherein the second therapeutic agent is a second anticancer agent.

73. The method of any one of claims 68-72, wherein the anticancer agent is a drug, a peptide or an antibody.

74. The method of claim 73, wherein the drug is a chemotherapeutic drug.

75. The method of claim 74, wherein the chemotherapeutic drug is doxorubicin.

76. Use of the pharmaceutical composition of claim 46 for the treatment of cancer.

77. The use of claim 76, wherein the cancer is breast cancer, prostate cancer or lung cancer.

78. The use of claim 76 or 77, wherein the anticancer agent is a drug, a peptide or an antibody.

79. The use of claim 78, wherein the drug is a chemotherapeutic drug.

80. The use of claim 79, wherein the chemotherapeutic drug is doxorubicin.

81. A method for detecting cancer in a subject or a sample from a subject comprising: a) contacting the subject or a sample from the subject with the plurality of nanoparticles of any one of claims 47-67; and b) detecting a signal, wherein a signal indicates the presence of cancer.

82. The method of claim 81, wherein the signal is a fluorescent signal.

83. The method of claim 81 or 82, wherein the signal is directly or indirectly detected.

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