CPMV-rna immunotherapy

Abstract

Provided herein are compositions comprising an isolated Secoviridae plant virus B and / or M component that are useful as potent anticancer agents, and to raise an immune response when administered to a patient or subject. In one aspect, the Secoviridae plant virus is a Cowpea mosaic virus (CPMV).

Description

[0001] CPMV-RNA IMMUNOTHERAPY CROSS-REFERENCE TO RELATED APPLICATION This application claims priority under 35 U.S.C. 119(e) to Application U.S. Serial No. 63 / 464,455, filed May 5, 2023, the content of which is incorporated by reference herein in its entirety. STATEMENT OF GOVERNMENT SUPPORT This invention was made with government support under Grants R01 CA274640, R01 CA224605 and R01 CA253615 awarded by the National Institutes of Health. The government has certain rights in the invention. BACKGROUND Throughout and within this disclosure, patent and technical publications are referenced by a citation or an Arabic number, the complete citation for which is found immediately preceding the claims. These technical and patent publications are incorporated by reference in their entireties to more fully describe the state of the art to which this disclosure pertains. Cancer immunotherapy aims to strengthen the immune response against tumors and elicit long-term immune memory to prevent recurrence.1-3Although immunotherapy has achieved promising clinical outcomes, only a small subset of patients shows a response to treatment and the efficacy differs according to the tumor type.4, 5Immunotherapy can also trigger severe adverse effects in some patients, including autoimmune reactions, cytokine release syndrome, and vascular leak syndrome.6-8To enhance the efficacy and reduce the side effects of cancer immunotherapy, cancer vaccine candidates have been developed using various nanomaterial formulations, including polymers, lipids, metals and viruses, the latter offering key advantages of versatility and biocompatibility.9, 10Plant viruses are particularly suitable for cancer immunotherapy because they possess intrinsic immunostimulatory properties and are noninfectious in mammals.11, 12Plant viruses act as adjuvants by activating pattern recognition receptors (PRPs) that counter the immunosuppression in the tumor microenvironment (TME) by increasing the production of pro-inflammatory cytokines such as type I and II interferons (IFNα, IFNγ), interleukin-12 (IL-12), and tumor necrosis factor alpha (TNFα).13, 14SUMMARY OF THE DISCLSOURE Plant virus nanoparticles can be used as drug carriers, imaging reagents, vaccine carriers, and immune adjuvants in the formulation of intratumoral in situ cancer vaccines. Cowpea mosaic virus (CPMV) is a non-enveloped plant virus belonging to the Secoviridae family that has been investigated as a vaccine adjuvant for cancer immunotherapy. The efficacy of CPMV as an in situ / intratumoral cancer vaccine has been demonstrated in melanoma, colon cancer, breast cancer, glioma, and ovarian cancer.13, 15-19Efficacy has also been demonstrated in canine patients with melanoma and inflammatory mammary cancer.20,21CPMV transforms immunosuppressive “cold” tumors into immunogenic “hot” tumors with high levels of innate immune cell infiltration and antigen presentation priming systemic and durable anti-tumor adaptive immunity.14, 22Mechanistically, CPMV is taken up by phagocytes and signals through toll-like receptors (TLRs) 2, 4, and 714, which promotes the secretion of pro-inflammatory cytokines into the TME, including IFNα, IFNγ, IL-6 and IL- 12, while reducing secretion of immunosuppressive cytokines such as TGFβ and IL-10.17, 18CPMV acts on the innate immune system which then induces systemic adaptive anti-tumor immunity – therefore localized intratumoral (i.t.) treatment (i.e. in situ vaccination) induces systemic efficacy with observed abscopal effect and long-lasting immune memory.22While potent as a solo therapy, CPMV in situ vaccination has also been combined with chemotherapy23and radiation,24increasing the number of antigen-specific effector T cells against resistant cancers and making the tumors more immunogenic, thus synergistically eliciting anti-tumor effects. CPMV is uniquely potent and outperforms other plant viruses as an in situ vaccine.16Studies pointed to the importance of the RNA cargo; RNA-free “empty” virus-like particles of CPMV are less potent than native CPMV.25This is attributed to TLR-7 signaling from encapsidated viral single strand RNA, leading to type-I interferon secretion.14CPMV has an icosahedral capsid that consists of 60 identical copies of a large (L, 42 kDa) and small (S, 24 kDa) coat protein. Its two bipartite positive-sense RNA genomes (RNA-1 and RNA-2) are packaged in separate capsids with identical protein composition.26, 27This results in a mixed population of bottom (B) components containing RNA-1 (6 kb) and middle (M) components containing RNA-2 (3.5 kb). RNA-free top (T) components also form during infection in plants; however, these are not isolated using a purification protocol which ends with an isopycnic sucrose gradient to collect the B and M components.25While studies have pointed to the importance of the RNA cargo, it is unclear whether the two strands of genomic RNA have similar or distinct immunomodulatory effects. Applicant compared the effects of B component (RNA-1), M component (RNA-2) and unfractionated CPMV particles in cancer models. This disclosure provides compositions of use against various diseases, such as cancer including, for example, melanoma and colon cancer. BRIEF DESCRIPTION OF THE DRAWINGS Figure 1A-1B. Schematic diagram of the two CPMV components. FIG. 1A shows the separation of CPMV into B and M components by Nycodenz gradient centrifugation reveals identical particles carrying distinct RNAs. The small coat protein (CP) is shown in on the vertices of the pentagon representing the B and M components and the large CP is shown in the interior of the pentagons representing the B and M components. FIG. 1B shows a schematic of RNA-2 and RNA-1. RNA-2 is the RNA component encapsidated within the M component and RNA-1 is the RNA component encapsidated within the B component. VPg – genome-linked protein, MP – movement protein, CP – coat protein, ProC – protease cofactor, AA(A)n – PolyA tail. Figure 2A-2H. Characterization of mixed and separated CPMV components. (FIG. 2A) Nycodenz gradient after ultracentrifugation at 26,000 g for 24 h (visualized under white light). The upper band consists of M components containing RNA-2. The lower band consists of B components containing RNA-1. (FIG. 2B) GelRed agarose gel electrophoresis of nucleic acids extracted from mixed and separated CPMV. Gels were stained with nucleic acid stain and the image was acquired under UV light. M = ssRNA ladder marker. (FIG. 2C) GelRed agarose gel electrophoresis of mixed and separated CPMV particles. Gels containing nucleic acid stain were imaged under UV light (left, RNA detection), then stained with protein stain (Coomassie staining) and imaged under white light (right, protein detection). (FID. 2D) 4-12% Nu-PAGE gel of CPMV particles stained with GelCode Blue Safe protein stain. M = SeeBlue Plus2 molecular weight marker. (FIG. 2E) TEM images of CPMV particles. Scale bar = 200 nm. (FIG. 2F) Size distribution and (FIG. 2G) surface charge of CPMV particles dispersed in 0.1 M KP buffer (pH 7.0). (FIG. 2H) SEC profiles of CPMV particles. Figure 3A-3C. Immunogenicity of mixed and separated CPMV components are similar in a reporter line and tumor-associated peritoneal cells ex vivo. (FIG. 3A) Activation of RAW-Blue cells after incubation with 1 μg of CPMV for 24 h. The results in each treatment group were compared by one-way ANOVA with Tukey’s multiple comparisons test. (FIG 3B) Cytokine expression ex vivo of immune cells harvested from peritoneal cavity washes in PBS-treated CT26 tumor-bearing mice on day 18. Cells were treated with 10 μg of CPMV particles for 24 h, and cytokine levels in the supernatant were determined by ELISA. (FIG. 3C) IL-6 and IFNα production in the splenocytes of each mouse strain following exposure to CPMV particles. The ELISA results in each treatment group were compared by one-way ANOVA with Tukey’s multiple comparisons test. (***p < 0.001, **p < 0.01, *p < 0.05, ns = not significant). FIGS. 3A and 3B, from left to right treatments in column charts are PBS (control), CPMV, CPMV B, and CPMV M. FIG. 3C, from left to right treatments in column charts are CPMV, CPMV B, CPMV M, CPMV B+M, and PBS (control). In FIG. 3C this is the order for both C57BL6 and TLR7- / - column sets. Figure 4A-4E. Similar therapeutic effects of mixed and separated CPMV particles in vivo in a mouse model of CT26 colon cancer. (FIG. 4A) Schematic timeline showing the establishment of CT26 colon cancer and subsequent treatments. (FIG. 4B) Change in abdominal circumference. Arrows indicate the dates of injection. (FIG. 4C) Tumor growth kinetics in each treatment group. (FIG. 4D) Survival curves of mice treated with CPMV particles. (FIG. 4E) Change in body weight over time. Tumor volumes were compared using two-way ANOVA and survival rates were compared using a log-rank (Mantel-Cox) test (**p < 0.01, *p < 0.05). FIGS. 4B and 4E, Circle = PBS (control), Square = CPMV, Upright Triangle = CPMV B, and Upside-down Triangle = CPMV M. FIG. 4D includes arrows indicating which treatment a line corresponds to. Figure 5A-5D. Similar therapeutic effects of mixed and separated CPMV particles in vivo in a mouse model of B16F10 melanoma. (FIG. 5A) Schematic timeline showing the establishment of B16F10 melanoma challenge and the subsequent treatments. (FIG. 5B) Tumor growth curves in mice treated with CPMV particles. Arrows indicate the dates of injection. (FIG. 5C) Tumor growth kinetics in each treatment group. (FIG. 5D) Survival curves of mice treated with CPMV particles. Tumor volumes were compared using an using two-way ANOVA and survival rates were compared using a log-rank (Mantel-Cox) test (***p < 0.001, **p < 0.01). FIG.5B, Circle = PBS (control), Square = CPMV, Upright Triangle = CPMV B, and Upside-down Triangle = CPMV M. FIG. 5D includes arrows indicating which treatment a line corresponds to. Figure 6. Similar modification of cytokine levels in vivo in a mouse model of CT26 colon cancer. Peritoneal cavity washes were harvested and cytokine levels were quantified by ELISA as in Fig. 4A. The results were compared by one-way ANOVA (***p < 0.001, **p < 0.01). From left to right treatments in column charts are PBS (control), CPMV, CPMV B, and CPMV M. DETAILED DESCRIPTION Definitions Embodiments according to the present disclosure will be described more fully hereinafter. Aspects of the disclosure may, however, be embodied in different forms and should not be construed as limited to the embodiments set forth herein. Rather, these embodiments are provided so that this disclosure will be thorough and complete, and will fully convey the scope of the disclosure to those skilled in the art. The terminology used in the description herein is for the purpose of describing particular embodiments only and is not intended to be limiting. Unless otherwise defined, all terms (including technical and scientific terms) used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this disclosure belongs. It will be further understood that terms, such as those defined in commonly used dictionaries, should be interpreted as having a meaning that is consistent with their meaning in the context of the present application and relevant art and should not be interpreted in an idealized or overly formal sense unless expressly so defined herein. While not explicitly defined below, such terms should be interpreted according to their common meaning. The terminology used in the description herein is for the purpose of describing particular embodiments only and is not intended to be limiting of the disclosure. All publications, patent applications, patents and other references mentioned herein are incorporated by reference in their entirety. Unless the context indicates otherwise, it is specifically intended that the various features of the disclosure described herein can be used in any combination. Moreover, the disclosure also contemplates that in some embodiments, any feature or combination of features set forth herein can be excluded or omitted. To illustrate, if the specification states that a complex comprises components A, B and C, it is specifically intended that any of A, B or C, or a combination thereof, can be omitted and disclaimed singularly or in any combination. Unless explicitly indicated otherwise, all specified embodiments, features, and terms intend to include both the recited embodiment, feature, or term and biological equivalents thereof. All numerical designations, e.g., pH, temperature, time, concentration, and molecular weight, including ranges, are approximations which are varied ( + ) or ( - ) by increments of 1.0 or 0.1, as appropriate, or alternatively by a variation of + / - 15 %, or alternatively 10%, or alternatively 5%, or alternatively 2%. It is to be understood, although not always explicitly stated, that all numerical designations are preceded by the term “about”. It also is to be understood, although not always explicitly stated, that the reagents described herein are merely exemplary and that equivalents of such are known in the art. Throughout this disclosure, various publications, patents, and published patent specifications are referenced by an identifying citation or by an Arabic numeral. The full citation for the publications identified by an Arabic numeral is found immediately preceding the claims. The disclosures of these publications, patents and published patent specifications are hereby incorporated by reference into the present disclosure in their entirety to more fully describe the state of the art to which this disclosure pertains. The practice of the present technology will employ, unless otherwise indicated, conventional techniques of organic chemistry, pharmacology, immunology, molecular biology, microbiology, cell biology and recombinant DNA, which are within the skill of the art. See, e.g., Sambrook, Fritsch and Maniatis, Molecular Cloning: A Laboratory Manual, 2nd edition (1989); Current Protocols In Molecular Biology (F. M. Ausubel, et al. eds., (1987)); the series Methods in Enzymology (Academic Press, Inc.): PCR 2: A Practical Approach (M.J. MacPherson, B.D. Hames and G.R. Taylor eds. (1995)), Harlow and Lane, eds. (1988) Antibodies, a Laboratory Manual, and Animal Cell Culture (R.I. Freshney, ed. (1987)). As used in the description of the disclosure and the appended claims, the singular forms “a,” “an” and “the” are intended to include the plural forms as well, unless the context clearly indicates otherwise. The term “about,” as used herein when referring to a measurable value such as an amount or concentration and the like, is meant to encompass variations of 20%, 10%, 5%, 1 %, 0.5%, or even 0.1 % of the specified amount. As used herein, the term “comprising” is intended to mean that the compositions or methods include the recited steps or elements, but do not exclude others. “Consisting essentially of” shall mean rendering the claims open only for the inclusion of steps or elements, which do not materially affect the basic and novel characteristics of the claimed compositions and methods. “Consisting of” shall mean excluding any element or step not specified in the claim. Embodiments defined by each of these transition terms are within the scope of this disclosure The terms or “acceptable,” “effective,” or “sufficient” when used to describe the selection of any components, ranges, dose forms, etc. disclosed herein intend that said component, range, dose form, etc. is suitable for the disclosed purpose. Also 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 when interpreted in the alternative (“or”). As used herein, the term “animal” refers to living multi-cellular vertebrate organisms, a category that includes, for example, mammals and birds. The term “mammal” includes both human and non-human mammals. The term “subject,” “host,” “individual,” and “patient” are as used interchangeably herein to refer to animals, typically mammalian animals. Any suitable mammal can be treated by a method, cell or composition described herein. Non-limiting examples of mammals include humans, non-human primates (e.g., apes, gibbons, chimpanzees, orangutans, monkeys, macaques, and the like), domestic animals (e.g., dogs and cats), farm animals (e.g., horses, cows, goats, sheep, pigs) and experimental animals (e.g., mouse, rat, rabbit, guinea pig). In some embodiments a mammal is a human. A mammal can be any age or at any stage of development (e.g., an adult, teen, child, infant, or a mammal in utero). A mammal can be male or female. A mammal can be a pregnant female. In some embodiments a subject is a human. In some embodiments, a subject has or is suspected of having a cancer or neoplastic disorder. “Eukaryotic cells” comprise, or alternatively consist essentially of, or yet further consist of all of the life kingdoms except monera. They can be easily distinguished through a membrane-bound nucleus. Animals, plants, fungi, and protists are eukaryotes or organisms whose cells are organized into complex structures by internal membranes and a cytoskeleton. The most characteristic membrane-bound structure is the nucleus. Unless specifically recited, the term “host” includes a eukaryotic host, including, for example, yeast, higher plant, insect and mammalian cells. Non-limiting examples of eukaryotic cells or hosts include simian, bovine, porcine, murine, rat, avian, reptilian and human, “Prokaryotic cells” that usually lack a nucleus or any other membrane-bound organelles and are divided into two domains, bacteria and archaea. In addition to chromosomal DNA, these cells can also contain genetic information in a circular loop called on episome. Bacterial cells are very small, roughly the size of an animal mitochondrion (about 1-2 μm in diameter and 10 μm long). Prokaryotic cells feature three major shapes: rod shaped, spherical, and spiral. Instead of going through elaborate replication processes like eukaryotes, bacterial cells divide by binary fission. Examples include but are not limited to Bacillus bacteria, E. coli bacterium, and Salmonella bacterium. A “composition” typically intends a combination of the active agent, e.g., virus or agonist of this disclosure and a naturally-occurring or non-naturally-occurring carrier, inert (for example, a detectable agent or label) or active, such as an adjuvant, diluent, binder, stabilizer, buffers, salts, lipophilic solvents, preservative, adjuvant or the like and include pharmaceutically acceptable carriers. Carriers also include pharmaceutical excipients and additives proteins, peptides, amino acids, lipids, and carbohydrates (e.g., sugars, including monosaccharides, di-, tri, tetra-oligosaccharides, and oligosaccharides; derivatized sugars such as alditols, aldonic acids, esterified sugars, and the like; and polysaccharides or sugar polymers), which can be present singly or in combination, comprising alone or in combination 1-99.99% by weight or volume. Exemplary protein excipients include serum albumin such as human serum albumin (HSA), recombinant human albumin (rHA), gelatin, casein, and the like. Representative amino acid components, which can also function in a buffering capacity, include alanine, arginine, glycine, arginine, betaine, histidine, glutamic acid, aspartic acid, cysteine, lysine, leucine, isoleucine, valine, methionine, phenylalanine, aspartame, and the like. Carbohydrate excipients are also intended within the scope of this technology, examples of which include but are not limited to monosaccharides such as fructose, maltose, galactose, glucose, D-mannose, sorbose, and the like; disaccharides, such as lactose, sucrose, trehalose, cellobiose, and the like; polysaccharides, such as raffinose, melezitose, maltodextrins, dextrans, starches, and the like; and alditols, such as mannitol, xylitol, maltitol, lactitol, xylitol sorbitol (glucitol) and myoinositol. The compositions used in accordance with the disclosure, including cells, treatments, therapies, agents, drugs and pharmaceutical formulations can be packaged in dosage unit form for ease of administration and uniformity of dosage. The term “unit dose” or “dosage” refers to physically discrete units suitable for use in a subject, each unit containing a predetermined quantity of the composition calculated to produce the desired responses in association with its administration, i.e., the appropriate route and regimen. The quantity to be administered, both according to number of treatments and unit dose, depends on the result and / or protection desired. Precise amounts of the composition also depend on the judgment of the practitioner and are peculiar to each individual. Factors affecting dose include physical and clinical state of the subject, route of administration, intended goal of treatment (alleviation of symptoms versus cure), and potency, stability, and toxicity of the particular composition. Upon formulation, solutions will be administered in a manner compatible with the dosage formulation and in such amount as is therapeutically or prophylactically effective. The formulations are easily administered in a variety of dosage forms, such as the type of injectable solutions described herein. As used herein, the terms “nucleic acid sequence” and “polynucleotide” are used interchangeably to refer to a polymeric form of nucleotides of any length, either ribonucleotides or deoxyribonucleotides. Thus, this term includes, but is not limited to, single-, double-, or multi-stranded DNA or RNA, genomic DNA, cDNA, DNA-RNA hybrids, or a polymer comprising purine and pyrimidine bases or other natural, chemically or biochemically modified, non-natural, or derivatized nucleotide bases. The term “encode” as it is applied to nucleic acid sequences refers to a polynucleotide which is said to “encode” a polypeptide if, in its native state or when manipulated by methods well known to those skilled in the art, can be transcribed and / or translated to produce the mRNA for the polypeptide and / or a fragment thereof. The antisense strand is the complement of such a nucleic acid, and the encoding sequence can be deduced therefrom. As used herein, the term “isolated cell” generally refers to a cell that is substantially separated from other cells of a tissue. The term includes prokaryotic and eukaryotic cells. As used herein, the phrase “inducing an immune response”, “immune response” or its equivalent “immunological response” refers to the development of a cell-mediated response (e.g. mediated by antigen-specific T cells or their secretion products). A cellular immune response is elicited by the presentation of polypeptide epitopes in association with Class I or Class II MHC molecules, to treat or prevent a viral infection, expand antigen-specific B-reg cells, TC1, CD4+ T helper cells and / or CD8+ cytotoxic T cells and / or disease generated, autoregulatory T cell and B cell “memory” cells. The response may also involve activation of other components. In some aspect, the term “immune response” may be used to encompass the formation of a regulatory network of immune cells. Thus, the term “regulatory network formation” may refer to an immune response elicited such that an immune cell, preferably a T cell, more preferably a T regulatory cell, triggers further differentiation of other immune cells, such as but not limited to, B cells or antigen-presenting cells – non-limiting examples of which include dendritic cells, monocytes, and macrophages. In certain embodiments, regulatory network formation involves B cells being differentiated into regulatory B cells; in certain embodiments, regulatory network formation involves the formation of tolerogenic antigen-presenting cells. Thus, in one aspect, inducing an immune response refers to activating the cellular immune response in a subject after therapy. Methods to determine if an immune response are known in the art, and include assaying for the induction of cytokines, radioimmunoassay (RIA), enzyme-linked immunoabsorbent assay (ELISA), and immunoblotting techniques. The term “immune cells” includes, e.g., white blood cells (leukocytes) which are derived from hematopoietic stem cells (HSC) produced in the bone marrow, lymphocytes (T cells, B cells, natural killer (NK) cells) and myeloid-derived cells (neutrophil, eosinophil, basophil, monocyte, macrophage, dendritic cells). “T cell” includes all types of immune cells expressing CD3 including T-helper cells (CD4+ cells), cytotoxic T-cells (CD8+ cells), natural killer T-cells, T-regulatory cells (Treg) and gamma-delta T cells. A “cytotoxic cell” includes CD8+ T cells, natural-killer (NK) cells, and neutrophils, which cells are capable of mediating cytotoxicity responses. Cytokines are small secreted proteins released by immune cells that have a specific effect on the interactions and communications between the immune cells. Cytokines can be pro-inflammatory or anti-inflammatory. Non-limiting example of a cytokine is Granulocyte-macrophage colony-stimulating factor (GM-CSF), which stimulates stem cells to produce granulocytes (neutrophils, eosinophils, and basophils) and monocytes. As used herein, the term “vector” refers to a nucleic acid construct deigned for transfer between different hosts, including but not limited to a plasmid, a virus, a cosmid, a phage, a BAC, a YAC, etc. A “viral vector” is defined as a recombinantly produced virus or viral particle that comprises a polynucleotide to be delivered into a host cell, either in vivo, ex vivo or in vitro. In some embodiments, plasmid vectors may be prepared from commercially available vectors. In other embodiments, viral vectors may be produced from baculoviruses, retroviruses, adenoviruses, AAVs, etc. according to techniques known in the art. In one embodiment, the viral vector is a lentiviral vector. Examples of viral vectors include retroviral vectors, adenovirus vectors, adeno-associated virus vectors, alphavirus vectors and the like. Further details as to modern methods of vectors for use in gene transfer may be found in, for example, Kotterman et al. (2015) Viral Vectors for Gene Therapy: Translational and Clinical Outlook Annual Review of Biomedical Engineering 17. Vectors that contain both a promoter and a cloning site into which a polynucleotide can be operatively linked are well known in the art. Such vectors are capable of transcribing RNA in vitro or in vivo and are commercially available from sources such as Agilent Technologies (Santa Clara, Calif.) and Promega Biotech (Madison, Wis.). An “effective amount” or “efficacious amount” refers to the amount of an agent or combined amounts of two or more agents, that, when administered for the treatment of a mammal or other subject, is sufficient to impact such treatment for the disease. The “effective amount” will vary depending on the agent(s), the disease and its severity and the age, weight, etc., of the subject to be treated. In some embodiments the effective amount will depend on the size and nature of the application in question. It will also depend on the nature and sensitivity of the target subject and the methods in use. The skilled artisan will be able to determine the effective amount based on these and other considerations. The effective amount may comprise, or alternatively consist essentially of, or yet further consist of one or more administrations of a composition depending on the embodiment. In one embodiment, the term “disease” or “disorder” as used herein refers to a cancer or a tumor (which are used interchangeably herein), a status of being diagnosed with such disease, a status of being suspect of having such disease, or a status of at high risk of having such disease, relapse or recurrence. As used herein, “cancer” or “malignancy” or “tumor” are used as synonymous terms and refer to any of a number of diseases that are characterized by uncontrolled, abnormal proliferation of cells, the ability of affected cells to spread locally or through the bloodstream and lymphatic system to other parts of the body (i.e., metastasize) as well as any of a number of characteristic structural and / or molecular features. A “solid tumor” is an abnormal mass of tissue that usually does not contain cysts or liquid areas. Solid tumors can be benign or malignant. Different types of solid tumors are named for the type of cells that form them. Examples of solid tumors include, but not limited to, sarcomas, carcinomas, and lymphomas. In some embodiments, a solid tumor comprises bladder cancer, bone cancer, brain cancer, breast cancer, colorectal cancer, esophageal cancer, eye cancer, head and neck cancer, kidney cancer, lung cancer, melanoma, ovarian cancer, pancreatic cancer, prostate cancer, skin cancer, gastric cancer, esophageal cancer, colon cancer, glioma, cervical cancer, hepatocellular, thyroid cancer, or stomach cancer. As used herein, a “metastatic cancer” is a cancer that spreads from where it originated to another part of the body. As used herein, a “cancer cell” are cells that have uncontrolled cell division and form solid tumors or enter the blood stream. As used herein, the term “administer” or “administration” or “administering” intends to mean delivery of a substance to a subject such as an animal or human. Administration can be in one dose, continuously or intermittently throughout the course of treatment. Methods of determining the most effective means and dosage of administration are known to those of skill in the art and will vary with the composition used for therapy, the purpose of the therapy, as well as the age, health or gender of the subject being treated. Single or multiple administrations can be carried out with the dose level and pattern being selected by the treating physician or in the case of pets and animals, treating veterinarian. Suitable dosage formulations and methods of administering the agents are known in the art. Route of administration can also be determined and method of determining the most effective route of administration are known to those of skill in the art and will vary with the composition used for treatment, the purpose of the treatment, the health condition or disease stage of the subject being treated and the target cell or tissue. Non-limiting examples of route of administration include intravenous, intra-arterial, intramuscular, intracardiac, intrathecal, subventricular, epidural, intracerebral, intracerebroventricular, sub-retinal, intravitreal, intraarticular, intraocular, intraperitoneal, intrauterine, intradermal, subcutaneous, transdermal, transmuccosal, and inhalation. An agent of the present disclosure can be administered for therapy by any suitable route of administration. It will also be appreciated that the optimal route will vary with the condition and age of the recipient, and the disease being treated. “Therapeutically effective amount” of a drug or an agent refers to an amount of the drug or the agent that is an amount sufficient to obtain a pharmacological response such as passive immunity; or alternatively, is an amount of the drug or agent that, when administered to a patient with a specified disorder or disease, is sufficient to have the intended effect, e.g., treatment, alleviation, amelioration, palliation or elimination of one or more manifestations of the specified disorder or disease in the patient. A therapeutic effect does not necessarily occur by administration of one dose, and may occur only after administration of a series of doses. Thus, a therapeutically effective amount may be administered in one or more administrations. As used herein, the term “expression” refers to the process by which polynucleotides are transcribed into mRNA and / or the process by which the transcribed mRNA is subsequently being translated into peptides, polypeptides, or proteins. If the polynucleotide is derived from genomic DNA, expression may include splicing of the mRNA in a eukaryotic cell. The expression level of a gene may be determined by measuring the amount of mRNA or protein in a cell or tissue sample. In one aspect, the expression level of a gene from one sample may be directly compared to the expression level of that gene from a control or reference sample. In another aspect, the expression level of a gene from one sample may be directly compared to the expression level of that gene from the same sample following administration of a compound. As used herein, “homology” or “identical”, percent “identity” or “similarity”, when used in the context of two or more nucleic acids or polypeptide sequences, refers to two or more sequences or subsequences that are the same or have a specified percentage of nucleotides or amino acid residues that are the same, e.g., at least 60% identity, preferably at least 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or higher identity over a specified region (e.g., nucleotide sequence encoding the RNA described herein). Homology can be determined by comparing a position in each sequence which may be aligned for purposes of comparison. When a position in the compared sequence is occupied by the same base or amino acid, then the molecules are homologous at that position. A degree of homology between sequences is a function of the number of matching or homologous positions shared by the sequences. A polynucleotide or polynucleotide region (or a polypeptide or polypeptide region) having a certain percentage (for example 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 98% or 99%) of “sequence identity” to another sequence means that, when aligned, that percentage of bases (or amino acids) are the same in comparing the two sequences. The alignment and the percent homology or sequence identity can be determined using software programs known in the art, for example those described in Current Protocols in Molecular Biology (Ausubel et al., eds. 1987) Supplement 30, section 7.7.18, Table 7.7.1. Preferably, default parameters are used for alignment. A preferred alignment program is BLAST, using default parameters. In particular, preferred programs are BLASTN and BLASTP, using the following default parameters: Genetic code = standard; filter = none; strand = both; cutoff = 60; expect = 10; Matrix = BLOSUM62; Descriptions = 50 sequences; sort by = HIGH SCORE; Databases = non-redundant, GenBank + EMBL + DDBJ + PDB + GenBank CDS translations + SwissProtein + SPupdate + PIR. Details of these programs can be found at the following Internet address: ncbi.nlm.nih.gov / cgi-bin / BLAST. The terms “homology” or “identical,” percent “identity” or “similarity” also refer to, or can be applied to, the complement of a test sequence. The terms also include sequences that have deletions and / or additions, as well as those that have substitutions. As described herein, the preferred algorithms can account for gaps and the like. Preferably, identity exists over a region that is at least about 25 amino acids or nucleotides in length, or more preferably over a region that is at least 50-100 amino acids or nucleotides in length. An “unrelated” or “non-homologous” sequence shares less than 40% identity, or alternatively less than 25% identity, with one of the sequences disclosed herein. The phrase “first line” or “second line” or “third line” refers to the order of treatment received by a patient. First line therapy regimens are treatments given first, whereas second or third line therapy are given after the first line therapy or after the second line therapy, respectively. The National Cancer Institute defines first line therapy as “the first treatment for a disease or condition. In patients with cancer, primary treatment can be surgery, chemotherapy, radiation therapy, or a combination of these therapies. First line therapy is also referred to those skilled in the art as “primary therapy and primary treatment.” See National Cancer Institute website at www.cancer.gov, last visited on May 1, 2008. Typically, a patient is given a subsequent chemotherapy regimen because the patient did not show a positive clinical or sub-clinical response to the first line therapy or the first line therapy has stopped. It is to be inferred without explicit recitation and unless otherwise intended, that when the present disclosure relates to a polypeptide, protein, polynucleotide, an equivalent or a biologically equivalent of such is intended within the scope of this disclosure. As used herein, the term “biological equivalent thereof” is intended to be synonymous with “equivalent thereof” when referring to a reference protein, polypeptide or nucleic acid, intends those having minimal homology while still maintaining desired structure or functionality. Unless specifically recited herein, it is contemplated that any of the above also includes equivalents thereof. For example, an equivalent intends at least about 70% homology or identity, or at least 80% homology or identity and alternatively, or at least about 85%, or alternatively at least about 90%, or alternatively at least about 95%, or alternatively at least 98% percent homology or identity and / or exhibits substantially equivalent biological activity to the reference protein, polypeptide, or nucleic acid. Alternatively, when referring to polynucleotides, an equivalent thereof is a polynucleotide that hybridizes under stringent conditions to the reference polynucleotide or its complement. As used herein, the term “an equivalent thereof” in reference to a polynucleotide or a protein in a virus (e.g., a capsid or coat protein) include a polynucleotide or a protein that comprise, or consists essentially of, or yet further consists of, at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99% sequence identify to the respective polynucleotide or protein of which it is compared to, while still retaining a functional activity. In the instances with reference to a capsid or coat protein, a functional activity refers to the formation of a virus. The phrase “equivalent polypeptide” or “equivalent peptide fragment” refers to protein, polynucleotide, or peptide fragment encoded by a polynucleotide that hybridizes to a polynucleotide encoding the exemplified polypeptide or its complement of the polynucleotide encoding the exemplified polypeptide, under high stringency and / or which exhibit similar biological activity in vivo, e.g., approximately 100%, or alternatively, over 90% or alternatively over 85% or alternatively over 70%, as compared to the standard or control biological activity. Additional embodiments within the scope of this disclosure are identified by having more than 60%, or alternatively, more than 65%, or alternatively, more than 70%, or alternatively, more than 75%, or alternatively, more than 80%, or alternatively, more than 85%, or alternatively, more than 90%, or alternatively, more than 95%, or alternatively more than 97%, or alternatively, more than 98% or 99% sequence homology. Percentage homology can be determined by sequence comparison using programs such as BLAST run under appropriate conditions. In one aspect, the program is run under default parameters. “Hybridization” refers to a reaction in which one or more polynucleotides react to form a complex that is stabilized via hydrogen bonding between the bases of the nucleotide residues. The hydrogen bonding may occur by Watson-Crick base pairing, Hoogstein binding, or in any other sequence-specific manner. The complex may comprise two strands forming a duplex structure, three or more strands forming a multi-stranded complex, a single self-hybridizing strand, or any combination of these. A hybridization reaction may constitute a step in a more extensive process, such as the initiation of a PCR reaction, or the enzymatic cleavage of a polynucleotide by a ribozyme. Examples of stringent hybridization conditions include: incubation temperatures of about 25 °C to about 37 °C; hybridization buffer concentrations of about 6x SSC to about 10x SSC; formamide concentrations of about 0% to about 25%; and wash solutions from about 4x SSC to about 8x SSC. Examples of moderate hybridization conditions include: incubation temperatures of about 40 °C to about 50 °C; buffer concentrations of about 9x SSC to about 2x SSC; formamide concentrations of about 30% to about 50%; and wash solutions of about 5x SSC to about 2x SSC. A high stringency hybridization refers to a condition in which hybridization of an oligonucleotide to a target sequence comprises no mismatches (or perfect complementarity). Examples of high stringency conditions include: incubation temperatures of about 55°C to about 68°C; buffer concentrations of about 1x SSC to about 0.1x SSC; formamide concentrations of about 55% to about 75%; and wash solutions of about 1x SSC, 0.1x SSC, or deionized water. In general, hybridization incubation times are from 5 minutes to 24 hours, with 1, 2, or more washing steps, and wash incubation times are about 1, 2, or 15 minutes. SSC is 0.15 M NaCl and 15 mM citrate buffer. It is understood that equivalents of SSC using other buffer systems can be employed. The term “isolated” as used herein refers to molecules or biologicals or cellular materials being substantially free from other materials. In one aspect, the term “isolated” refers to nucleic acid, such as DNA or RNA, or protein or polypeptide, or cell or cellular organelle, or tissue or organ, separated from other DNAs or RNAs, or proteins or polypeptides, or cells or cellular organelles, or tissues or organs, respectively, that are present in the natural source. The term “isolated” also refers to a nucleic acid or peptide that is substantially free of cellular material, viral material, or culture medium when produced by recombinant DNA techniques, or chemical precursors or other chemicals when chemically synthesized. Moreover, an “isolated nucleic acid” is meant to include nucleic acid fragments which are not naturally occurring as fragments and would not be found in the natural state. The term “isolated” is also used herein to refer to polypeptides which are isolated from other cellular proteins and is meant to encompass both purified and recombinant polypeptides. The term “isolated” is also used herein to refer to cells or tissues that are isolated from other cells or tissues and is meant to encompass both cultured and engineered cells or tissues. The term “protein”, “peptide” and “polypeptide” are used interchangeably and in their broadest sense to refer to a compound of two or more subunit amino acids, amino acid analogs or peptidomimetics. The subunits may be linked by peptide bonds. In another aspect, the subunit may be linked by other bonds, e.g., ester, ether, etc. A protein or peptide must contain at least two amino acids and no limitation is placed on the maximum number of amino acids which may comprise a protein’s or peptide’s sequence. As used herein the term “amino acid” refers to either natural and / or unnatural or synthetic amino acids, including glycine and both the D and L optical isomers, amino acid analogs and peptidomimetics. The terms “polynucleotide” and “oligonucleotide” are used interchangeably and refer to a polymeric form of nucleotides of any length, either deoxyribonucleotides or ribonucleotides or analogs thereof. Polynucleotides can have any three-dimensional structure and may perform any function, known or unknown. The following are non-limiting examples of polynucleotides: a gene or gene fragment (for example, a probe, primer, EST or SAGE tag), exons, introns, messenger RNA (mRNA), transfer RNA, ribosomal RNA, RNAi, ribozymes, cDNA, recombinant polynucleotides, branched polynucleotides, plasmids, vectors, isolated DNA of any sequence, isolated RNA of any sequence, nucleic acid probes and primers. A polynucleotide can comprise modified nucleotides, such as methylated nucleotides and nucleotide analogs. If present, modifications to the nucleotide structure can be imparted before or after assembly of the polynucleotide. The sequence of nucleotides can be interrupted by non-nucleotide components. A polynucleotide can be further modified after polymerization, such as by conjugation with a labeling component. The term also refers to both double- and single-stranded molecules. Unless otherwise specified or required, any aspect of this technology that is a polynucleotide encompasses both the double-stranded form and each of two complementary single-stranded forms known or predicted to make up the double-stranded form. As used herein, the term “purified” does not require absolute purity; rather, it is intended as a relative term. Thus, for example, a purified nucleic acid, peptide, protein, biological complexes or other active compound is one that is isolated in whole or in part from proteins or other contaminants. Generally, substantially purified peptides, proteins, biological complexes, or other active compounds for use within the disclosure comprise more than 80% of all macromolecular species present in a preparation prior to admixture or formulation of the peptide, protein, biological complex or other active compound with a pharmaceutical carrier, excipient, buffer, absorption enhancing agent, stabilizer, preservative, adjuvant or other co-ingredient in a complete pharmaceutical formulation for therapeutic administration. More typically, the peptide, protein, biological complex or other active compound is purified to represent greater than 90%, often greater than 95% of all macromolecular species present in a purified preparation prior to admixture with other formulation ingredients. In other cases, the purified preparation may be essentially homogeneous, wherein other macromolecular species are not detectable by conventional techniques. As used herein, “treating” or “treatment” of a disease in a subject refers to (1) preventing the symptoms or disease from occurring in a subject that is predisposed or does not yet display symptoms of the disease; (2) inhibiting the disease or arresting its development; or (3) ameliorating or causing regression of the disease or the symptoms of the disease. As understood in the art, “treatment” is an approach for obtaining beneficial or desired results, including clinical results. For the purposes of the present technology, beneficial or desired results can include one or more, but are not limited to, alleviation or amelioration of one or more symptoms, diminishment of extent of a condition (including a disease), stabilized (i.e., not worsening) state of a condition (including disease), delay or slowing of condition (including disease), progression, amelioration or palliation of the condition (including disease), states and remission (whether partial or total), whether detectable or undetectable. When the disease is cancer, the following clinical end points are non-limiting examples of treatment: reduction in tumor burden, slowing of tumor growth, longer overall survival, longer time to tumor progression, inhibition of metastasis or a reduction in metastasis of the tumor. In one aspect, treatment excludes prophylaxis. A “pharmaceutical composition” is intended to include the combination of an active agent with a carrier, inert or active, making the composition suitable for diagnostic or therapeutic use in vitro, in vivo or ex vivo. “Pharmaceutically acceptable carriers” refers to any diluents, excipients, or carriers that may be used in the compositions disclosed herein. Pharmaceutically acceptable carriers include ion exchangers, alumina, aluminum stearate, lecithin, serum proteins, such as human serum albumin, buffer substances, such as phosphates, glycine, sorbic acid, potassium sorbate, partial glyceride mixtures of saturated vegetable fatty acids, water, salts or electrolytes, such as protamine sulfate, disodium hydrogen phosphate, potassium hydrogen phosphate, sodium chloride, zinc salts, colloidal silica, magnesium trisilicate, polyvinyl pyrrolidone, cellulose-based substances, polyethylene glycol, sodium carboxymethylcellulose, polyacrylates, waxes, polyethylene-polyoxypropylene-block polymers, polyethylene glycol and wool fat. Suitable pharmaceutical carriers are described in Remington's Pharmaceutical Sciences, Mack Publishing Company, a standard reference text in this field. They may be selected with respect to the intended form of administration, that is, oral tablets, capsules, elixirs, syrups and the like, and consistent with conventional pharmaceutical practices. As used herein, the term “overexpress” with respect to a cell, a tissue, or an organ expresses a protein to an amount that is greater than the amount that is produced in a control cell, a control issue, or an organ. A protein that is overexpressed may be endogenous to the host cell or exogenous to the host cell. As used herein, the term “enhancer” denotes sequence elements that augment, improve or ameliorate transcription of a nucleic acid sequence irrespective of its location and orientation in relation to the nucleic acid sequence to be expressed. An enhancer may enhance transcription from a single promoter or simultaneously from more than one promoter. As long as this functionality of improving transcription is retained or substantially retained (e.g., at least 70%, at least 80%, at least 90% or at least 95% of wild-type activity, that is, activity of a full-length sequence), any truncated, mutated or otherwise modified variants of a wild-type enhancer sequence are also within the above definition. The term “promoter” as used herein refers to any sequence that regulates the expression of a coding sequence, such as a gene. Promoters may be constitutive, inducible, repressible, or tissue-specific, for example. A “promoter” is a control sequence that is a region of a polynucleotide sequence at which initiation and rate of transcription are controlled. It may contain genetic elements at which regulatory proteins and molecules may bind such as RNA polymerase and other transcription factors. The term “contacting” means direct or indirect binding or interaction between two or more. A particular example of direct interaction is binding. A particular example of an indirect interaction is where one entity acts upon an intermediary molecule, which in turn acts upon the second referenced entity. Contacting as used herein includes in solution, in solid phase, in vitro, ex vivo, in a cell and in vivo. Contacting in vivo can be referred to as administering, or administration. The term “introduce” as applied to methods of producing modified cells such as chimeric antigen receptor cells refers to the process whereby a foreign (i.e. extrinsic or extracellular) agent is introduced into a host cell thereby producing a cell comprising the foreign agent. Methods of introducing nucleic acids include but are not limited to transduction, retroviral gene transfer, transfection, electroporation, transformation, viral infection, and other recombinant DNA techniques known in the art. In some embodiments, transduction is done via a vector (e.g., a viral vector). In some embodiments, transfection is done via a chemical carrier, DNA / liposome complex, or micelle (e.g., Lipofectamine (Invitrogen)). In some embodiments, viral infection is done via infecting the cells with a viral particle comprising the polynucleotide of interest (e.g., AAV). In some embodiments, introduction further comprises CRISPR mediated gene editing or Transcription activator-like effector nuclease (TALEN) mediated gene editing. Methods of introducing non-nucleic acid foreign agents (e.g., soluble factors, cytokines, proteins, peptides, enzymes, growth factors, signaling molecules, small molecule inhibitors) include but are not limited to culturing the cells in the presence of the foreign agent, contacting the cells with the agent, contacting the cells with a composition comprising the agent and an excipient, and contacting the cells with vesicles or viral particles comprising the agent. The term “culturing” refers to growing cells in a culture medium under conditions that favor expansion and proliferation of the cell. The term “culture medium” or “medium” is recognized in the art and refers generally to any substance or preparation used for the cultivation of living cells. The term “medium”, as used in reference to a cell culture, includes the components of the environment surrounding the cells. Media may be solid, liquid, gaseous or a mixture of phases and materials. Media include liquid growth media as well as liquid media that do not sustain cell growth. Media also include gelatinous media such as agar, agarose, gelatin and collagen matrices. Exemplary gaseous media include the gaseous phase to which cells growing on a petri dish or other solid or semisolid support are exposed. The term “medium” also refers to material that is intended for use in a cell culture, even if it has not yet been contacted with cells. In other words, a nutrient rich liquid prepared for culture is a medium. Similarly, a powder mixture that when mixed with water or other liquid becomes suitable for cell culture may be termed a “powdered medium.” “Defined medium” refers to media that are made of chemically defined (usually purified) components. “Defined media” do not contain poorly characterized biological extracts such as yeast extract and beef broth. “Rich medium” includes media that are designed to support growth of most or all viable forms of a particular species. Rich media often include complex biological extracts. A “medium suitable for growth of a high-density culture” is any medium that allows a cell culture to reach an OD600 of 3 or greater when other conditions (such as temperature and oxygen transfer rate) permit such growth. The term “basal medium” refers to a medium which promotes the growth of many types of microorganisms which do not require any special nutrient supplements. Most basal media generally comprise of four basic chemical groups: amino acids, carbohydrates, inorganic salts, and vitamins. A basal medium generally serves as the basis for a more complex medium, to which supplements such as serum, buffers, growth factors, lipids, and the like are added. In one aspect, the growth medium may be a complex medium with the necessary growth factors to support the growth and expansion of the cells of the disclosure while maintaining their self-renewal capability. Examples of basal media include, but are not limited to, Eagles Basal Medium, Minimum Essential Medium, Dulbecco’s Modified Eagle’s Medium, Medium 199, Nutrient Mixtures Ham’s F-10 and Ham’s F-12, McCoy’s 5A, Dulbecco’s MEM / F-I 2, RPMI 1640, and Iscove’s Modified Dulbecco’s Medium (IMDM). As used herein, the term “modification” include, for example, substitutions, additions, insertions and deletions to the amino acid sequences, which can be referred to as “variants.” Exemplary sequence substitutions, additions, and insertions include a full length or a portion of a sequence with one or more amino acids substituted (or mutated), added, or inserted, for example of a capsid derived from the plant virus. In some instances, a capsid described herein includes, e.g., a modified capsid comprising, or consisting essentially of, or yet further consisting of, at least 70%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to its respective wild-type version. Modified capsid polypeptides include, for example, non-conservative and conservative substitutions of the capsid amino acid sequences. As used herein, the term “conservative substitution” denotes the replacement of an amino acid residue by another, chemically or biologically similar residue. Biologically similar means that the substitution does not destroy a biological activity or function, e.g., assembly of a viral capsid. \Structurally similar means that the amino acids have side chains with similar length, such as alanine, glycine and serine, or a similar size. Chemical similarity means that the residues have the same charge or are both hydrophilic or hydrophobic. Particular examples of conservative substitutions include the substitution of a hydrophobic residue such as isoleucine, valine, leucine or methionine for another, the substitution of a polar residue for another, such as the substitution of arginine for lysine, glutamic for aspartic acids, or glutamine for asparagine, and the like. The term "conservative substitution" also includes the use of a substituted amino acid in place of an unsubstituted parent amino acid. Such proteins that include amino acid substitutions can be encoded by a nucleic acid. Consequently, nucleic acid sequences encoding proteins that include amino acid substitutions are also provided. Modified proteins also include one or more D-amino acids substituted for L-amino acids (and mixtures thereof), structural and functional analogues, for example, peptidomimetics having synthetic or non-natural amino acids or amino acid analogues and derivatized forms. Modifications include cyclic structures such as an end-to-end amide bond between the amino and carboxy-terminus of the molecule or intra- or inter-molecular disulfide bond. Modified forms further include “chemical derivatives,” in which one or more amino acids has a side chain chemically altered or derivatized. Such derivatized polypeptides include, for example, amino acids in which free amino groups form amine hydrochlorides, p- toluene sulfonyl groups, carobenzoxy groups; the free carboxy groups form salts, methyl and ethyl esters; free hydroxl groups that form O-acyl or O-alkyl derivatives as well as naturally occurring amino acid derivatives, for example, 4-hydroxyproline, for proline, 5- hydroxylysine for lysine, homoserine for serine, ornithine for lysine etc. Also included are amino acid derivatives that can alter covalent bonding, for example, the disulfide linkage that forms between two cysteine residues that produces a cyclized polypeptide. As used herein, the term “Secoviridae plant virus” (or “Secoviridae virus”) refers to a virus in the Secoviridae family. Secoviridae is a family of viruses in the order of Picornavirales. Viruses in the Secoviridae family are associated with plants. Secoviridae plant viruses are icosahedral in structure and include a non-enveloped capsid. The Secoviridae family includes multiple genera and dozens of species. Members of the family Secoviridae are non-enveloped viruses with mono- or bipartite (RNA1 and RNA2) linear positive-sense ssRNA genomes of 9 to 13.7 kilobases in total. Secoviruses are related to Picornaviruses and are classified in the order Picornavirales. The majority of known members infect dicotyledonous plants, and many are important plant pathogens. The Secoviridae plant virus genera include Comovirus, Fabavirus, Nepovirus, Cheravirus, Sadwavirus, Sequivirus, Stralarivirus, Torradovirus, and Waikavirus. Non-limiting examples of Secoviridae plant virus species include but are not limited to Cowpea Mosaic Virus (CPMV), Broad Bean Wilt Virus (BBWV), Tomato Ringspot Virus (ToRSV), Cherry Rasp Leaf Virus (CRLV), Satsuma Dwarf Virus (SDV), Strawberry Mottle Virus (SMoV), Black raspberry necrosis virus (BRNV), and Parsnip yellow fleck virus (PYFV). Of particular interest herein are multipartite Secoviridae plant viruses, including bipartite Secoviridae plant viruses. See Fuchs et al. (2022) Journal of General Virology;103:001807 DOI 10.1099 / jgv.0.001807 and corresponding web publication at https: / / ictv.global / report / chapter / secoviridae / secoviridae. According to some embodiments, Secoviridae plant viruses are comprised of three components: a B component, an M component, and a T component. As used herein, the term “B component” refers to the bottom component, a particle comprising the RNA-1 strand of a multipartite virus. According to some embodiments, the RNA-1 strand encodes a viral genome-linked protein (VpG), protease cofactor, helicase, protease, and polymerase. According to other embodiments, the M component includes additional or other elements. FIG. 1B and Table 1 shows an exemplary B component. As used herein, the term “M component” refers to the middle component, a particle comprising the RNA-2 strand of a multipartite virus. According to some embodiments, the RNA-2 strand encodes a movement protein, large coat protein, and small coat protein. According to other embodiments, the B component includes additional or other elements. FIG. 1B and Table 2 shows an exemplary M component. As used herein, the term “T component” refers to the top component, an RNA-free component. As used herein, the term “a polyadenylation site (PolyA tail)” can be represented as “AA(A)n,” wherein n is an integer that is 0 or about from 1 to about 50, or about 75, or about 100, or about 150, or about 175, or about 200, or about 225, or about 250, or about 275, or about 300, or more. Modes For Carrying Out the Disclosure Plant virus nanoparticles can be used as drug carriers, imaging reagents, vaccine carriers, and immune adjuvants in the formulation of intratumoral in situ cancer vaccines. CPMV is a non-enveloped virus with a bipartite positive-strand RNA genome with each RNA (referred to herein as RNA-1 and RNA-2) packaged separately into identical protein capsids. Based on differences in their densities, the components carrying RNA-1 (6 kb) denoted as the bottom (B) component or carrying RNA-2 (3.5 kb) denoted as the middle (M) component, can be separated from each other and from a top (T) component which is devoid of any RNA. As used herein, native CPMV (mixture of B component and M component), or another native virus, is a plant virus nanoparticle which can carry RNA. As used herein, the viral B component and the viral M component are also plant virus nanoparticles which can carry RNA. The following reference is incorporated by reference in its entirety: Jung E, Chung YH, Mao C, Fiering SN, Steinmetz NF. The Potency of Cowpea Mosaic Virus Particles for Cancer In Situ Vaccination Is Unaffected by the Specific Encapsidated Viral RNA. Mol Pharm. 2023 Jul 3;20(7):3589-3597. doi: 10.1021 / acs.molpharmaceut.3c00214. Epub 2023 Jun 9. PMID: 37294891; PMCID: PMC10530639. Plant Virus Components and Compositions Applicant provides herein several compositions. In one aspect, the composition comprises, or consists essentially of, or yet further consists of an isolated Secoviridae plant virus B and / or M component wherein the B and / or M component is the Secoviridae plant viral B and / or M capsid optionally containing RNA, which can be the naturally occurring RNA or any other RNA such as an RNA vaccine or anti-cancer therapy. In one aspect, the composition comprises, or consists essentially of, or yet further consists of an isolated Secoviridae plant virus B component wherein the B component is the Secoviridae plant viral B capsid and optionally which further comprises RNA, which can be the naturally occurring RNA or any other RNA such as an RNA vaccine or anti-cancer therapy. In a further aspect, the composition comprises, or consists essentially of, or yet further consists of an isolated Secoviridae plant virus M component wherein the M component is the Secoviridae plant viral M capsid and optionally which further comprises RNA, which can be the naturally occurring RNA or any other RNA such as an RNA vaccine or anti-cancer therapy. In one embodiment, the isolated B and / or the M Secoviridae plant virus component is the only viral or virally derived component in the composition. In another embodiment, the isolated B and / or the M Secoviridae plant virus component is the only anti- cancer agent in the composition. Also provided is an anti-cancer composition consisting essentially of an isolated Secoviridae plant virus B and / or M component, or alternatively, consisting essentially an isolated Secoviridae plant virus B component, or alternatively, consisting essentially of an isolated Secoviridae plant virus M component, and optionally wherein the B and / or M component is the Secoviridae plant B and / or M component (respectively) viral capsid and optionally which further comprises RNA. The RNA can be the naturally occurring RNA from the Secoviridae plant virus or any other RNA such as an RNA vaccine or anti-cancer therapy. In some aspects, the anti-cancer composition is designed to treat a cancer or induce an immune response. In one embodiment, the virus(es) is a native virus, that is, not inactive / not inactivated. Alternatively, in any of the disclosed aspects, another embodiment is wherein the isolated Secoviridae or capsid component is inactivated. Viral inactivation can take place by UV light or chemicals such as formalin, or further by protein cross-linking. In a further aspect of the above, the isolated Secoviridae B component comprises RNA-1 and the M component comprises RNA-2. FIG. 1 includes a schematic of the B component (RNA-1) and M component (RNA-2). In another aspect, the composition also comprises or contains a pharmaceutically acceptable carrier. The compositions as described herein can comprise a plurality of Secoviridae B and / or M components, that can be the same or different, including for example the same or different encapsulated RNA. The compositions as described herein can comprise B and / or M components that are derived from one or more species, or one or more genera of Secoviridae plant viruses. In a further aspect, the compositions can further contain an additional therapeutic agent. In one aspect, the isolated Secoviridae plant virus is an isolated virus from the Comovirus, Fabavirus, Nepovirus, Cheravirus, Sadwavirus, Sequivirus, Stralarivirus, Torradovirus, or Waikavirus genera. In one embodiment, the isolated Secoviridae is an isolated Comovirus, for example a Cowpea mosaic virus (CPMV). In some embodiments, the Secoviridae virus is or is derived from Cowpea mosaic virus (CPMV). CPMV strains include, but are not limited to, SB (Agrawal, H.O. (1964). Meded. Landb. Hoogesch. Wagen. 64:1) and Vu (Agrawal, H.O. (1964). Meded. Landb. Hoogesch. Wagen. 64:1). For CPMV, the genome is bipartite, with RNA-1 (6 kb) and RNA-2 (3.5 kb) being separately encapsidated. CPMV has an icosahedral capsid structure, which is ~30 nm in diameter and is formed from 60 copies each of a Large (L) and Small (S) coat protein. These two coat proteins are processed from a single RNA-2-encodedprecursor polyprotein (VP60) by the action of the 24 K viral proteinase which is encoded by RNA-1. CPMV’s two bipartite positive-sense RNA genomes (RNA-1 and RNA-2) are packaged in separate capsids with identical protein composition,26, 27which results in a mixed population of bottom (B) components containing RNA-1 (6 kb) and middle (M) components containing RNA-2 (3.5 kb). In one aspect, the B component includes CPMV RNA-1. In some instances, the CPMV RNA-1 (which is encapsidated in the B component) sequence comprises, or consists essentially of, or yet further consists of, the sequence as set forth in NC_003549.1: UAUU (SEQ ID NO: 3), or an equivalent thereof. Further, in one aspect the RNA-1 polynucleotide includes a polyadenylation site (PolyA tail), as seen in FIG. 1B (represented by the AA(A)n, wherein n is an integer that is 0 or about from 1 to about 50, or about 75, or about 100, or about 150, or about 175, or about 200, or about 225, or about 250, or about 275, or about 300, or more. Table 1 below indicates the domain information for the components of CPMV RNA- 1, a schematic of which is in FIG. 1B. In one aspect, the B component includes an RNA polynucleotide encoding the components of CPMV RNA-1, including a protease cofactor, a helicase, a genome-linked protein, a protease, and a polymerase. According to one aspect, the components of CPMV RNA-1 comprise, consists essentially of, or yet further consists of SEQ ID NOs: 5-9 (Table 1). In one aspect a VPg peptide sequence is covalently bound to RNA-1 at the 5’ end. In one aspect, a PolyA tail (AA(A)n) is conjugated to RNA-1 at the 3’ end. In one aspect, the VPg peptide has a sequence that comprises, or consists essentially of, or yet further consists of: SRKPNRFDMQQYRYNNVPLKRRVWADAQ (SEQ ID NO: 4), or an equivalent thereof. The Vpg peptide and sequence is described and given in Carette, J (2002) “Origin of the membrane compartment for cowpea mosaic virus replication.” Thesis, Wageningen University. Table 1. CPMV B Component RNA-1 Components (sequences and locations). RNA-1 is found in the B component of CPMV. Components (including, for example segment location) are according to and part of the RNA-1 full sequence according to SEQ ID NO: 3.

[0002] In one aspect, the M component includes CPMV RNA-2. In some instances, the CPMV RNA-2 (which is contained in the CPMV M component) sequence comprises, or consists essentially of, or yet further consists of, the sequence as set forth in NC_003550.1:

[0003] equivalent thereof. Further, in one aspect the RNA-2 polynucleotide includes a polyadenylation site (PolyA tail), as seen in FIG.1B (represented by the AA(A)n. Table 2 below indicates the domain information for the components of RNA-2, a schematic of which is in FIG. 1B. In one aspect, the M component includes an RNA polynucleotide encoding the components of CPMV RNA-2, including a movement protein, a large coat protein, and a small coat protein. According to one aspect, the components of CPMV RNA-2 comprise, consist essentially of, or yet further consist of SEQ ID NOs: 11-13 (Table 2). In one aspect a VPg peptide sequence is covalently bound to RNA-2 at the 5’ end. In one aspect, a PolyA tail (AA(A)n) is conjugated to RNA-1 at the 3’ end. In one aspect, the VPg peptide has a sequence that comprises, or consists essentially of, or yet further consists of: SRKPNRFDMQQYRYNNVPLKRRVWADAQ (SEQ ID NO: 4), or an equivalent thereof. Table 2. CPMV M Component RNA-2 Components (sequences and locations). RNA-2 is found in the M component of CPMV. Components (for example, sequence location) are according to and part of RNA-2 full sequence according to SEQ ID NO: 10.

[0004] In some instances, the virus from CPMV— including the B and / or M components— comprise, or consists essentially of, or yet further consists of, a plurality of capsid proteins. The coat proteins in CPMV are seen in the schematic according to FIG. 1A, wherein the small coat protein is on the vertices of the pentagon and the large coat protein fills out the remainder of the pentagon. As used herein, capsid protein and coat protein are used interchangeably. In some instances, CPMV produces a large capsid protein and a small capsid protein precursor (which generates a mature small capsid protein). In some cases, CPMV capsid is formed from a plurality of large capsid proteins and mature small capsid proteins. In some cases, the large capsid protein is a wild-type large capsid protein, optionally expressed by SB or Vu strain. In other instances, the large capsid protein is a modified large capsid protein, e.g., comprising, or consisting essentially of, or yet further consisting of, one or more substitutions, insertions, and / or deletions. In some aspects, the large capsid protein comprises, or consists essentially, of, or yet further consists of the large capsid protein (i.e. the large coat protein) encoded by SEQ ID NO: 12. In other cases, the large capsid protein comprises, or consists essentially of, or yet further consists of, the amino acid sequence as set forth in the UniProtKB ID P03599 (residues 460-833): MEQNLFALSLDDTSSVRGSLLDTKFAQTRVLLSKAMAGGDVLLDEYLYDVV NGQDFRATVAFLRTHVITGKIKVTATTNISDNSGCCLMLAINSGVRGKYSTDVYTICS QDSMTWNPGCKKNFSFTFNPNPCGDSWSAEMISRSRVRMTVICVSGWTLSPTTDVIA KLDWSIVNEKCEPTIYHLADCQNWLPLNRWMGKLTFPQGVTSEVRRMPLSIGGGAG ATQAFLANMPNSWISMWRYFRGELHFEVTKMSSPYIKATVTFLIAFGNLSDAFGFYE SFPHRIVQFAEVEEKCTLVFSQQEFVTAWSTQVNPRTTLEADGCPYLYAIIHDSTTGTI SGDFNLGVKLVGIKDFCGIGSNPGIDGSRLLGAIAQ (SEQ ID NO: 1), or an equivalent thereof. In some cases, the mature small capsid protein is a wild-type mature small capsid protein, optionally expressed by SB or Vu strain. In other instances, the mature small capsid protein is a modified mature small capsid protein, e.g., comprising, or consisting essentially of, or yet further consisting of, one or more substitutions, insertions, and / or deletions. In some aspects, the small capsid protein comprises, or consists essentially, of, or yet further consists of the small capsid protein (i.e. the small coat protein) encoded by SEQ ID NO: 13. In some cases, the mature small capsid protein comprises, or consists essentially of, or yet further consists of, the amino acid sequence as set forth in the UniProtKB ID P03599 (residues 834-1022): GPVCAEASDVYSPCMIASTPPAPFSDVTAVTFDLINGKITPVGDDNWNTHIYN PPIMNVLRTAAWKSGTIHVQLNVRGAGVKRADWDGQVFVYLRQSMNPESYDARTF VISQPGSAMLNFSFDIIGPNSGFEFAESPWANQTTWYLECVATNPRQIQQFEVNMRFD PNFRVAGNILMPPFPLSTETPPL (SEQ ID NO: 2), or an equivalent thereof. In some instances, a virus or viral component described herein further comprises, or consists essentially of, or yet further consists of, a label or a tag, e.g., such as a detectable label. A detectable label can be attached to, e.g., to the surface of a virus, B component, or M component. Non-limiting exemplary detectable labels also include a radioactive material, such as a radioisotope, a metal or a metal oxide. Radioisotopes include radionuclides emitting alpha, beta or gamma radiation. In particular embodiments, a radioisotope can be one or more of:3H,10B,18F,11C,14C,13N,18O,15O,32P, P33,35S,35Cl,45Ti,46Sc,47Sc,51Cr,52Fe,59Fe,.57Co,60Cu,61Cu,62Cu,64Cu,67Cu,67Ga,68Ga,72As76Br,77Br,81mKr,82Rb,85Sr,89Sr,86Y,90Y,95Nb,94mTc,99mTc,97Ru,103Ru,105Rh,109Cd,111In,113Sn,113mIn,114In, I125, I131,140La,141Ce,149Pm,153Gd,157Gd,153Sm,161Tb,166Dy,166Ho,169Er,169Y,175Yb,177Lu,186Re,188Re,201Tl,203Pb,211At,212Bi or225Ac. Additional non-limiting exemplary detectable labels include a metal or a metal oxide. In particular embodiments, a metal or metal oxide is one or more of: gold, silver, copper, boron, manganese, gadolinium, iron, chromium, barium, europium, erbium, praseodynium, indium, or technetium. In additional embodiments, a metal oxide includes one or more of: Gd(III), Mn(II), Mn(III), Cr(II), Cr(III), Cu(II), Ffe (III), Pr(III), Nd(III) Sm(III), Tb(III), Yb(III) Dy(III), Ho(III), Eu(II), Eu(III), or Er(III). Further non-limiting exemplary detectable labels include contrast agents (e.g., gadolinium; manganese; barium sulfate; an iodinated or noniodinated agent; an ionic agent or nonionic agent); magnetic and paramagnetic agents (e.g., iron-oxide chelate); nanoparticles; an enzyme (horseradish peroxidase, alkaline phosphatase, β-galactosidase, or acetylcholinesterase); a prosthetic group (e.g., streptavidin / biotin and avidin / biotin); a fluorescent material (e.g., umbelliferone, fluorescein, fluorescein isothiocyanate, rhodamine, dichlorotriazinylamine fluorescein, dansyl chloride or phycoerythrin); a luminescent material (e.g., luminol); or a bioluminescent material (e.g., luciferase, luciferin, aequorin). Additional non-limiting examples of tags and / or detectable labels include enzymes (horseradish peroxidase, urease, catalase, alkaline phosphatase, beta-galactosidase, chloramphenicol transferase); enzyme substrates; ligands (e.g., biotin); receptors (avidin); GST-, T7-, His-, myc-, HA- and FLAG®-tags; electron-dense reagents; energy transfer molecules; paramagnetic labels; fluorophores (fluorescein, fluorscamine, rhodamine, phycoerthrin, phycocyanin, allophycocyanin); chromophores; chemi-luminescent (imidazole, luciferase, acridinium, oxalate); and bio-luminescent agents. As set forth herein, a detectable label or tag can be linked or conjugated (e.g., covalently) to the virus. In various embodiments a detectable label, such as a radionuclide or metal or metal oxide can be bound or conjugated to the agent, either directly or indirectly. A linker or an intermediary functional group can be used to link the molecule to a detectable label or tag. Linkers include amino acid or peptidomimetic sequences inserted between the molecule and a label or tag so that the two entities maintain, at least in part, a distinct function or activity. Linkers may have one or more properties that include a flexible conformation, an inability to form an ordered secondary structure or a hydrophobic or charged character which could promote or interact with either domain. Amino acids typically found in flexible protein regions include Gly, Asn and Ser. The length of the linker sequence may vary without significantly affecting a function or activity. Linkers further include chemical moieties, conjugating agents, and intermediary functional groups. Examples include moieties that react with free or semi-free amines, oxygen, sulfur, hydroxy or carboxy groups. Such functional groups therefore include mono and bifunctional crosslinkers, such as sulfo-succinimidyl derivatives (sulfo-SMCC, sulfo- SMPB), in particular, disuccinimidyl suberate (DSS), BS3 (Sulfo-DSS), disuccinimidyl glutarate (DSG) and disuccinimidyl tartrate (DST). Non-limiting examples include diethylenetriaminepentaacetic acid (DTPA) and ethylene diaminetetracetic acid. In another aspect, provided herein is a combination or composition that further comprises the virus, B and / or M component with at least one carrier, such as a pharmaceutically acceptable carrier or excipient. In one aspect, the composition further comprises a preservative or stabilizer. Compositions, including pharmaceutical compositions comprising, consisting essentially of, or consisting of the virus can be in combination of other therapeutic agents can be manufactured by means of conventional mixing, dissolving, granulating, dragee-making levigating, emulsifying, encapsulating, entrapping, or lyophilization processes. These can be formulated in conventional manner using one or more physiologically acceptable carriers, diluents, excipients, or auxiliaries which facilitate processing of the combinations of compounds provided herein into preparations which can be used pharmaceutically. In some embodiments, the pharmaceutical formulations described herein are administered to a subject by multiple administration routes, including but not limited to, parenteral, subcutaneous, oral, buccal, rectal, sublingual, or transdermal administration routes. In some cases, parenteral administration comprises, or consists essentially of, or yet further consists of, intravenous, subcutaneous, intramuscular, intracerebral, intranasal, intra- arterial, intra-articular, intradermal, intravitreal, intraosseous infusion, intraperitoneal, or intrathecal administration. In some instances, the pharmaceutical composition is formulated for local administration. In other instances, the pharmaceutical composition is formulated for systemic administration. In some embodiments, the pharmaceutical formulations include, but are not limited to, lyophilized formulations, aqueous liquid dispersions, self-emulsifying dispersions, solid solutions, liposomal dispersions, aerosols, solid dosage forms, powders, immediate release formulations, controlled release formulations, fast melt formulations, tablets, capsules, pills, delayed release formulations, extended release formulations, pulsatile release formulations, multiparticulate formulations (e.g., nanoparticle formulations), and mixed immediate and controlled release formulations. In some embodiments, the pharmaceutical formulations include a carrier or carrier materials selected on the basis of compatibility with the composition disclosed herein, and the release profile properties of the desired dosage form. Exemplary carrier materials include, e.g., binders, suspending agents, disintegration agents, filling agents, surfactants, solubilizers, stabilizers, lubricants, wetting agents, diluents, and the like. Pharmaceutically compatible carrier materials include, but are not limited to, acacia, gelatin, colloidal silicon dioxide, calcium glycerophosphate, calcium lactate, maltodextrin, glycerine, magnesium silicate, polyvinylpyrrollidone (PVP), cholesterol, cholesterol esters, sodium caseinate, soy lecithin, taurocholic acid, phosphotidylcholine, sodium chloride, tricalcium phosphate, dipotassium phosphate, cellulose and cellulose conjugates, sugars sodium stearoyl lactylate, carrageenan, monoglyceride, diglyceride, pregelatinized starch, and the like. See, e.g., Remington: The Science and Practice of Pharmacy, Nineteenth Ed (Easton, Pa.: Mack Publishing Company, 1995), Hoover, John E., Remington’s Pharmaceutical Sciences (Mack Publishing Co., Easton, Pennsylvania 1975), Liberman, H.A. and Lachman, L., Eds., Pharmaceutical Dosage Forms, (Marcel Decker, New York, N.Y., 1980,) and Pharmaceutical Dosage Forms and Drug Delivery Systems, Seventh Ed. (Lippincott Williams & Wilkins l999). In some instances, the pharmaceutical formulations further include pH adjusting agents or buffering agents which include acids such as acetic, boric, citric, lactic, phosphoric and hydrochloric acids, bases such as sodium hydroxide, sodium phosphate, sodium borate, sodium citrate, sodium acetate, sodium lactate and tris-hydroxymethylaminomethane, and buffers such as citrate / dextrose, sodium bicarbonate and ammonium chloride. Such acids, bases and buffers are included in an amount required to maintain pH of the composition in an acceptable range. In some instances, the pharmaceutical formulation includes one or more salts in an amount required to bring osmolality of the composition into an acceptable range. Such salts include those having sodium, potassium or ammonium cations and chloride, citrate, ascorbate, borate, phosphate, bicarbonate, sulfate, thiosulfate or bisulfite anions, suitable salts include sodium chloride, potassium chloride, sodium thiosulfate, sodium bisulfite and ammonium sulfate. In some embodiments, the pharmaceutical formulations include, but are not limited to, sugars like trehalose, sucrose, mannitol, maltose, glucose, or salts like potassium phosphate, sodium citrate, ammonium sulfate and / or other agents such as heparin to increase the solubility and in vivo stability of polypeptides. In some instances, the pharmaceutical formulations further include diluent which are used to stabilize compounds because they can provide a more stable environment. Salts dissolved in buffered solutions (which also can provide pH control or maintenance) are utilized as diluents in the art, including, but not limited to a phosphate buffered saline solution. In certain instances, diluents increase bulk of the composition to facilitate compression or create sufficient bulk for homogenous blend for capsule filling. Such compounds can include e.g., lactose, starch, mannitol, sorbitol, dextrose, microcrystalline cellulose such as AVICEL®, dibasic calcium phosphate, dicalcium phosphate dihydrate, tricalcium phosphate, calcium phosphate, anhydrous lactose, spray-dried lactose, pregelatinized starch, compressible sugar, such as Di- PAC®(Amstar), mannitol, hydroxypropylmethylcellulose, hydroxypropylmethylcellulose acetate stearate, sucrose-based diluents, confectioner’s sugar, monobasic calcium sulfate monohydrate, calcium sulfate dihydrate, calcium lactate trihydrate, dextrates, hydrolyzed cereal solids, amylose, powdered cellulose, calcium carbonate, glycine, kaolin, mannitol, sodium chloride, inositol, bentonite, and the like. In some cases, the pharmaceutical formulations include disintegration agents or disintegrants to facilitate the breakup or disintegration of a substance. The term “disintegrate” include both the dissolution and dispersion of the dosage form when contacted with gastrointestinal fluid. Examples of disintegration agents include a starch, e.g., a natural starch such as corn starch or potato starch, a pregelatinized starch such as National 1551 or AMIJEL®, or sodium starch glycolate such as PROMOGEL®or EXPLOTAB®, a cellulose such as a wood product, methylcrystalline cellulose, e.g., AVICEL®, AVICEL®PH101, AVICEL®PH102, AVICEL®PH105, ELCEMA®P100, EMCOCEL®, VIVACEL®, MING TIA®, and SOLKA-FLOC®, methylcellulose, croscarmellose, or a cross-linked cellulose, such as cross-linked sodium carboxymethylcellulose (AC-DI-SOL®), cross-linked carboxymethylcellulose, or cross-linked croscarmellose, a cross- linked starch such as sodium starch glycolate, a cross-linked polymer such as crospovidone, a cross-linked polyvinylpyrrolidone, alginate such as alginic acid or a salt of alginic acid such as sodium alginate, a clay such as VEEGUM®HV (magnesium aluminum silicate), a gum such as agar, guar, locust bean, Karaya, pectin, or tragacanth, sodium starch glycolate, bentonite, a natural sponge, a surfactant, a resin such as a cation-exchange resin, citrus pulp, sodium lauryl sulfate, sodium lauryl sulfate in combination starch, and the like. In some instances, the pharmaceutical formulations include filling agents such as lactose, calcium carbonate, calcium phosphate, dibasic calcium phosphate, calcium sulfate, microcrystalline cellulose, cellulose powder, dextrose, dextrates, dextran, starches, pregelatinized starch, sucrose, xylitol, lactitol, mannitol, sorbitol, sodium chloride, polyethylene glycol, and the like. Lubricants and glidants are also optionally included in the pharmaceutical formulations described herein for preventing, reducing or inhibiting adhesion or friction of materials. Exemplary lubricants include, e.g., stearic acid, calcium hydroxide, talc, sodium stearyl fumerate, a hydrocarbon such as mineral oil, or hydrogenated vegetable oil such as hydrogenated soybean oil (STEROTEX®), higher fatty acids and their alkali-metal and alkaline earth metal salts, such as aluminum, calcium, magnesium, zinc, stearic acid, sodium stearates, glycerol, talc, waxes, STEAROWET®, boric acid, sodium benzoate, sodium acetate, sodium chloride, leucine, a polyethylene glycol (e.g., PEG-4000) or a methoxypolyethylene glycol such as CARBOWAX™, sodium oleate, sodium benzoate, glyceryl behenate, polyethylene glycol, magnesium or sodium lauryl sulfate, colloidal silica such as SYLOID™, CAB-O-SIL®, a starch such as corn starch, silicone oil, a surfactant, and the like. Plasticizers include compounds used to soften the microencapsulation material or film coatings to make them less brittle. Suitable plasticizers include, e.g., polyethylene glycols such as PEG 300, PEG 400, PEG 600, PEG 1450, PEG 3350, and PEG 800, stearic acid, propylene glycol, oleic acid, triethyl cellulose and triacetin. Plasticizers can also function as dispersing agents or wetting agents. Solubilizers include compounds such as triacetin, triethyl citrate, ethyl oleate, ethyl caprylate, sodium lauryl sulfate, sodium docusate, vitamin E TPGS, dimethylacetamide, N- methylpyrrolidone, N-hydroxyethylpyrrolidone, polyvinylpyrrolidone, hydroxypropylmethyl cellulose, hydroxypropyl cyclodextrins, ethanol, n-butanol, isopropyl alcohol, cholesterol, bile salts, polyethylene glycol 200-600, glycofurol, transcutol, propylene glycol, and dimethyl isosorbide and the like. Stabilizers include compounds such as any antioxidation agents, buffers, acids, preservatives and the like. Exemplary stabilizers include L-arginine hydrochloride, tromethamine, albumin (human), citric acid, benzyl alcohol, phenol, disodium biphosphate dehydrate, propylene glycol, metacresol or m-cresol, zinc acetate, poly sorb ate-20 or TWEEN® 20, or trometamol. Suspending agents include compounds such as polyvinylpyrrolidone, e.g., polyvinylpyrrolidone K12, polyvinylpyrrolidone K17, polyvinylpyrrolidone K25, or polyvinylpyrrolidone K30, vinyl pyrrolidone / vinyl acetate copolymer (S630), polyethylene glycol, e.g., the polyethylene glycol can have a molecular weight of about 300 to about 6000, or about 3350 to about 4000, or about 7000 to about 5400, sodium carboxymethylcellulose, methylcellulose, hydroxypropylmethylcellulose, hydroxymethylcellulose acetate stearate, polysorbate-80, hydroxyethylcellulose, sodium alginate, gums, such as, e.g., gum tragacanth and gum acacia, guar gum, xanthans, including xanthan gum, sugars, cellulosics, such as, e.g., sodium carboxymethylcellulose, methylcellulose, sodium carboxymethylcellulose, hydroxypropylmethylcellulose, hydroxyethylcellulose, polysorbate-80, sodium alginate, polyethoxylated sorbitan monolaurate, polyethoxylated sorbitan monolaurate, povidone and the like. Surfactants include compounds such as sodium lauryl sulfate, sodium docusate, Tween 60 or 80, triacetin, vitamin E TPGS, sorbitan monooleate, polyoxyethylene sorbitan monooleate, polysorbates, polaxomers, bile salts, glyceryl monostearate, copolymers of ethylene oxide and propylene oxide, e.g., PLURONIC®(BASF), and the like. Additional surfactants include polyoxyethylene fatty acid glycerides and vegetable oils, e.g., polyoxyethylene (60) hydrogenated castor oil, and polyoxyethylene alkyl ethers and alkylphenyl ethers, e.g., octoxynol 10, octoxynol 40. Sometimes, surfactants is included to enhance physical stability or for other purposes. Viscosity enhancing agents include, e.g., methyl cellulose, xanthan gum, carboxymethyl cellulose, hydroxypropyl cellulose, hydroxypropylmethyl cellulose, hydroxypropylmethyl cellulose acetate stearate, hydroxypropylmethyl cellulose phthalate, carbomer, polyvinyl alcohol, alginates, acacia, chitosans and combinations thereof. Wetting agents include compounds such as oleic acid, glyceryl monostearate, sorbitan monooleate, sorbitan monolaurate, triethanolamine oleate, polyoxyethylene sorbitan monooleate, polyoxyethylene sorbitan monolaurate, sodium docusate, sodium oleate, sodium lauryl sulfate, sodium doccusate, triacetin, Tween 80, vitamin E TPGS, ammonium salts and the like. The pharmaceutical compositions for the administration can be conveniently presented in dosage unit form and can be prepared by any of the methods well known in the art of pharmacy. The pharmaceutical compositions can be, for example, prepared by uniformly and intimately bringing the compounds provided herein into association with a liquid carrier, a finely divided solid carrier or both, and then, if necessary, shaping the product into the desired formulation. In the pharmaceutical composition, each compound of the combination provided herein is included in an amount sufficient to produce the desired therapeutic effect. For example, pharmaceutical compositions of the present technology may take a form suitable for virtually any mode of administration, including, for example, topical, ocular, oral, buccal, systemic, nasal, injection, infusion, transdermal, rectal, and vaginal, or a form suitable for administration by inhalation or insufflation. For topical administration, the combination of compounds can be formulated as solutions, gels, ointments, creams, suspensions, etc., as is well-known in the art. Systemic formulations include those designed for administration by injection (e.g., subcutaneous, intravenous, infusion, intramuscular, intrathecal, or intraperitoneal injection) as well as those designed for transdermal, transmucosal, oral, or pulmonary administration. Useful injectable preparations include sterile suspensions, solutions, or emulsions of the compounds provided herein in aqueous or oily vehicles. The compositions may also contain formulating agents, such as suspending, stabilizing, and / or dispersing agents. The formulations for injection can be presented in unit dosage form, e.g., in ampules or in multidose containers, and may contain added preservatives. Alternatively, the injectable formulation can be provided in powder form for reconstitution with a suitable vehicle, including but not limited to sterile pyrogen free water, buffer, and dextrose solution, before use. To this end, the combination of compounds provided herein can be dried by any art-known technique, such as lyophilization, and reconstituted prior to use. For transmucosal administration, penetrants appropriate to the barrier to be permeated are used in the formulation. Such penetrants are known in the art. For oral administration, the pharmaceutical compositions may take the form of, for example, lozenges, tablets, or capsules prepared by conventional means with pharmaceutically acceptable excipients such as binding agents (e.g., pregelatinised maize starch, polyvinylpyrrolidone, or hydroxypropyl methylcellulose); fillers (e.g., lactose, microcrystalline cellulose, or calcium hydrogen phosphate); lubricants (e.g., magnesium stearate, talc, or silica); disintegrants (e.g., potato starch or sodium starch glycolate); or wetting agents (e.g., sodium lauryl sulfate). The tablets can be coated by methods well known in the art with, for example, sugars, films, or enteric coatings. Compositions intended for oral use can be prepared according to any method known to the art for the manufacture of pharmaceutical compositions, and such compositions may contain one or more agents selected from the group consisting of sweetening agents, flavoring agents, coloring agents, and preserving agents in order to provide pharmaceutically elegant and palatable preparations. Tablets contain the combination of compounds provided herein in admixture with non-toxic pharmaceutically acceptable excipients which are suitable for the manufacture of tablets. These excipients can be for example, inert diluents, such as calcium carbonate, sodium carbonate, lactose, calcium phosphate or sodium phosphate; granulating and disintegrating agents (e.g., corn starch or alginic acid); binding agents (e.g. starch, gelatin, or acacia); and lubricating agents (e.g., magnesium stearate, stearic acid, or talc). The tablets can be left uncoated or they can be coated by known techniques to delay disintegration and absorption in the gastrointestinal tract and thereby provide a sustained action over a longer period. For example, a time delay material such as glyceryl monostearate or glyceryl distearate can be employed. They may also be coated by the techniques well known to the skilled artisan. The pharmaceutical compositions of the present technology may also be in the form of oil-in-water emulsions. Liquid preparations for oral administration may take the form of, for example, elixirs, solutions, syrups, or suspensions, or they can be presented as a dry product for constitution with water or other suitable vehicle before use. Such liquid preparations can be prepared by conventional means with pharmaceutically acceptable additives such as suspending agents (e.g., sorbitol syrup, cellulose derivatives, or hydrogenated edible fats); emulsifying agents (e.g., lecithin, or acacia); non-aqueous vehicles (e.g., almond oil, oily esters, ethyl alcohol, cremophoreTM, or fractionated vegetable oils); and preservatives (e.g., methyl or propyl-p-hydroxybenzoates or sorbic acid). The preparations may also contain buffer salts, preservatives, flavoring, coloring, and sweetening agents as appropriate. In some embodiments, one or more compositions disclosed herein are contained in a kit. Accordingly, in some embodiments, provided herein is a kit comprising, consisting essentially of, or consisting of one or more compositions disclosed herein and instructions for their use. Dosage and Dosage Formulations In some embodiments, the combinations or compositions comprising the B and / or M components are administered to a subject suffering from a condition as disclosed herein, such as a mammal or a human, either alone or as part of a pharmaceutically acceptable formulation, once a week, once a day, twice a day, three times a day, or four times a day, or even more frequently. Administration of the composition or combination alone or in combination with the additional therapeutic agent and compositions containing same can be effected by any method that enables delivery to the site of action. These methods include oral routes, intraduodenal routes, parenteral injection (including intravenous, subcutaneous, intramuscular, intravascular or infusion), topical, and rectal administration. Bolus doses can be used, or infusions over a period of 1, 2, 3, 4, 5, 10, 15, 20, 30, 60, 90, 120 or more minutes, or any intermediate time period can also be used, as can infusions lasting 3, 4, 5, 6, 7, 8, 9, 10, 12, 1416, 20, 24 or more hours or lasting for 1-7 days or more. Infusions can be administered by drip, continuous infusion, infusion pump, metering pump, depot formulation, or any other suitable means. Dosage regimens can be adjusted to provide the optimum desired response. For example, a single bolus can be administered, several divided doses can be administered over time or the dose may be proportionally reduced or increased as indicated by the exigencies of the therapeutic situation. It is especially advantageous to formulate parenteral compositions in dosage unit form for ease of administration and uniformity of dosage. Dosage unit form, as used herein, refers to physically discrete units suited as unitary dosages for the subjects to be treated; each unit containing a predetermined quantity of active compound calculated to produce the desired therapeutic effect in association with the required pharmaceutical carrier. The specification for the dosage unit forms of the disclosure are dictated by and directly dependent on (a) the unique characteristics of the agent and the particular therapeutic or prophylactic effect to be achieved, and (b) the limitations inherent in the art of compounding such an active compound for the treatment of sensitivity in individuals. Thus, the skilled artisan would appreciate, based upon the disclosure provided herein, that the dose and dosing regimen is adjusted in accordance with methods well-known in the therapeutic arts. That is, the maximum tolerable dose can be readily established, and the effective amount providing a detectable therapeutic benefit to a patient can also be determined, as can the temporal requirements for administering each agent to provide a detectable therapeutic benefit to the patient. Accordingly, while certain dose and administration regimens are exemplified herein, these examples in no way limit the dose and administration regimen that can be provided to a patient in practicing the present disclosure. It is to be noted that dosage values can vary with the type and severity of the condition to be alleviated and may include single or multiple doses. It is to be further understood that for any particular subject, specific dosage regimens should be adjusted over time according to the individual need and the professional judgment of the person administering or supervising the administration of the compositions, and that dosage ranges set forth herein are exemplary only and are not intended to limit the scope or practice of the claimed compositions. For example, doses may be adjusted based on pharmacokinetic or pharmacodynamic parameters, which may include clinical effects such as toxic effects and / or laboratory values. Thus, the present disclosure encompasses intra-patient dose-escalation as determined by the skilled artisan. Determining appropriate dosages and regimens for administration are well-known in the relevant art and would be understood to be encompassed by the skilled artisan once provided the teachings disclosed herein. Diagnostic Methods In some embodiments, one or more of the methods described herein further comprise, or consists essentially of, or yet further consists of, a diagnostic step. In some instances, a sample is first obtained from a subject suspected of having a disease or condition described above. Exemplary samples include, but are not limited to, cell sample, tissue sample, tumor biopsy, liquid samples such as blood and other liquid samples of biological origin (including, but not limited to, peripheral blood, sera, plasma, ascites, urine, cerebrospinal fluid (CSF), sputum, saliva, bone marrow, synovial fluid, aqueous humor, amniotic fluid cerumen, breast milk, broncheoalveolar lavage fluid, semen, prostatic fluid, cowper’s fluid or pre-ejaculatory fluid, female ejaculate, sweat, tears, cyst fluid, pleural and peritoneal fluid, pericardial fluid, ascites, lymph, chyme, chyle, bile, interstitial fluid, menses, pus, sebum, vomit, vaginal secretions / flushing, synovial fluid, mucosal secretion, stool water, pancreatic juice, lavage fluids from sinus cavities, bronchopulmonary aspirates, blastocyl cavity fluid, or umbilical cord blood. In some instances, the sample is a tumor biopsy. In some cases, the sample is a liquid sample, e.g., a blood sample. In some cases, the sample is a cell-free DNA sample. Various methods known in the art can be utilized to determine the presence of a disease or condition described herein or to determine whether an immune response has been induced in a subject. Assessment of one or more biomarkers associated with a disease or condition, or for characterizing whether an immune response has been induced, can be performed by any appropriate method. Expression levels or abundance can be determined by direct measurement of expression at the protein or mRNA level, for example by microarray analysis, quantitative PCR analysis, or RNA sequencing analysis. Alternatively, labeled antibody systems may be used to quantify target protein abundance in the cells, followed by immunofluorescence analysis, such as FISH analysis. The compositions of the present disclosure can be administered by parenteral (e.g., intramuscular, intraperitoneal, intravenous, ICV, intracisternal injection or infusion, subcutaneous injection, or implant), oral, by inhalation spray nasal, vaginal, rectal, sublingual, urethral (e.g., urethral suppository) or topical routes of administration (e.g., gel, ointment, cream, aerosol, etc.) and can be formulated in suitable dosage unit formulations containing conventional non-toxic pharmaceutically acceptable carriers, adjuvants, excipients, and vehicles appropriate for each route of administration. Therapeutic Methods Inducing immune response Further disclosed herein are methods for inducing an immune response in a subject consisting essentially of, or yet further consisting of the M components, B components, compositions, or combinations as disclosed herein. In one aspect, the composition or combination comprises or consists essentially of, or consists of a Secoviridae plant virus, e.g., Cowpea mosaic virus (CPMV) B and / or M component. In one aspect, the immune response is activation of innate immune cells to induce secretion of pro-inflammatory cytokines, such IFNα, IFNγ, IL-6 and IL-12. FIG. 3 and FIG. 6 show induced secretion of pro-inflammatory cytokines in CPMV B and CPMV M treated mice as compared to a control treatment in a cancer model. The CPMV B component includes CPMV RNA-1 and the CPMV M component includes CPMV RNA-2. The pro- inflammatory cytokines described herein are exemplary, not limiting. In another aspect, the immune response is inhibiting the secretion innate immune cells to reduce secretion of immunosuppressive cytokines such as TGFβ and IL-10. FIG. 3 and FIG. 6 show inhibited secretion of immunosuppressive cytokines in CPMV B and CPMV M treated mice as compared to a control treatment in a cancer model. The CPMV B component includes CPMV RNA-1 and the CPMV M component includes CPMV RNA-2. The immunosuppressive cytokines described herein are exemplary, not limiting. In one aspect, the subject is a mammal or a human. In one aspect, the administering comprises intravenous, subcutaneous, intratumoral, or intraperitoneal delivery. The method can be practiced with a plurality of B and / or M components from a plurality plant viruses, which can be the same or different from each other. The method can further comprise administration of an additional therapeutic agent, such as for example, those known in the art or alternatively as described herein. Treating or preventing cancer Also provided herein is a method to inhibit the growth of a cancer cell comprising contacting the cell with the M components, B components, compositions, or combinations as described herein. In one aspect the M component, B component, compositions, or combinations comprises, consists essentially of, or consists of, or is derived from, a Secoviridae plant virus. In one aspect, the contacting is in vitro. In one aspect, the contacting is in vivo. In one aspect, the cancer cell is selected from the group of: melanoma, breast cancer, prostate cancer, lung cancer, ovarian cancer, skin cancer, bladder cancer, pancreatic cancer, gastric cancer, esophageal cancer, colon cancer, head and neck cancer, brain cancer, glioma, cervical cancer, hepatocellular cancer, inflammatory mammary cancer or thyroid cancer, that is optionally a primary or a metastatic cancer. In one aspect the cancer cell is a mammalian cell, for example a human cell. Also provided herein is a method for treating cancer in a subject in need thereof, comprising administering to the subject the M components, B components, compositions, or combinations as described herein. In one aspect, the composition or combination comprises, consists essentially of, or consists of, or is derived from a Secoviridae plant virus, e.g., a Cowpea mosaic virus (CPMV). The method of treating cancer can be practiced with a plurality of Secoviridae plant virus B and / or M components or compositions including B and / or M components, which can be the same or different from each other. The Secoviridae plant virus components can be derived from one or more isolates, species, or genera belonging to the Secoviridae family. The method can further comprise administration of an additional therapeutic agent, such as for example, those known in the art or alternatively as described herein. In one aspect, the cancer is a blood cancer or a solid tumor, such as for example, a cancer is selected from melanoma, breast cancer, prostate cancer, lung cancer, ovarian cancer, skin cancer, bladder cancer, pancreatic cancer, gastric cancer, esophageal cancer, head and neck, colon cancer, brain cancer, glioma, cervical cancer, hepatocellular cancer, inflammatory mammary cancer, or thyroid cancer. The cancer can be a primary or a metastatic cancer. In a further aspect, the cancer is metastatic or primary lung cancer, ovarian cancer, colon cancer, melanoma, or breast cancer or alternatively, wherein the cancer is metastatic melanoma or metastatic colon cancer. The method can be combined with a different cancer therapy or tumor resection. The method provides a treatment from one or more of: inhibiting metastatic potential of the cancer; reduction in tumor size; a reduction in tumor burden, longer progression free survival and longer overall survival of the subject. FIGS. 4B and 4C show the tumor reducing potential of CPMV B and CPMV M components as compared to a control in a colon cancer model. The CPMV B component includes CPMV RNA-1 and the CPMV M component includes CPMV RNA-2. Treatment with B or M components slowed the growth rate of the tumors. In FIGS. 4B and 4C circumference indicates tumor size, wherein a larger circumference indicates a larger tumor. Further, CPMV B and CPMV M treated mice had increased longevity as compared to a control in a colon cancer model (FIG. 4D). As shown in FIG. 4D, the PBS control had a 0% survival rate while the mice treated with CPMV (mixed), CPMV M component, and CPMV B component had >50% survival at 40 days post inoculation. FIGS. 5B and 5C show the tumor reducing potential of CPMV B and CPMV M components as compared to a control in a melanoma cancer model. The CPMV B component includes CPMV RNA-1 and the CPMV M component includes CPMV RNA-2. Treatment with B or M components slowed the growth of the tumors. Further, CPMV B alone reduced the tumor volume to a greater extent than native CPMV (i.e. a native mixture of both the CPMV B and M components). Further, CPMV B and CPMV treated mice had increased longevity as compared to a control in a melanoma cancer model (FIG. 5D). As shown in FIG. 5D, the PBS control had a 0% survival rate while the mice treated with CPMV (mixed), CPMV M component, and CPMV B component had >50% survival at 40 days post inoculation In some embodiments, a subject is a mammal. In some embodiments, a subject is a human. In some embodiments, a subject has a condition. In some embodiments, a subject has cancer. In some embodiments, a cancer is selected from melanoma, breast cancer, prostate cancer, lung cancer, ovarian cancer, skin cancer, bladder cancer, pancreatic cancer, gastric cancer, esophageal cancer, head and neck, colon cancer, brain cancer, glioma, cervical cancer, hepatocellular cancer, inflammatory mammary cancer, or thyroid cancer. In some embodiments, the cancer is primary or metastatic cancer. In some embodiments, the cancer is metastatic or primary lung cancer or breast cancer. In some embodiments, the cancer metastatic melanoma or metastatic triple negative breast cancer. In some embodiments, the cancer is a primary or metastatic cancer present in the lung. In some embodiments, administering is selected from intravenous, intra-arterial, intramuscular, intracardiac, intrathecal, subventricular, epidural, intracerebral, intracerebroventricular, sub-retinal, intravitreal, intraarticular, intraocular, intraperitoneal, intrauterine, intradermal, subcutaneous, transdermal, transmucosal, or inhalation. In some embodiments, administering is intravenous. In one aspect, administering is intraperitoneal. The methods and compositions disclosed herein may further comprise or alternatively consist essentially of, or yet further consists of administering to the subject an anti-tumor therapy other than the Secoviridae virus. In some embodiments, anti-tumor therapy may include different cancer therapy or tumor resection. The additional therapeutic can be combined in the same composition or separately administered. In some embodiments, the combination or composition are provided to prevent the symptoms of cancer from occurring in a subject that is predisposed or does not yet display symptoms of the cancer. In some embodiments, the combination or composition disclosed herein may be delivered or administered into a cavity formed by the resection of tumor tissue (i.e. intracavity delivery) or directly into a tumor prior to resection (i.e. intratumoral delivery). In some embodiments. In some embodiments, the administering is intravenous. In some embodiments, the combination or composition are administered to the subject at least 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 times a day. In some embodiments, any of polynucleotides, nanoparticles, vectors, or compositions disclosed herein are administered to the subject at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 times a week. In some embodiments, any of the polynucleotides, nanoparticles, vectors, or compositions disclosed herein are administered to the subject at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, or 31 times a month. In some embodiments, the combination or composition disclosed herein are administered to the subject at least every 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 days. In some embodiments, the combination or composition disclosed herein are administered to the subject at least every 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, or 14 weeks. In some embodiments, the combination or composition disclosed herein are administered to the subject for a period of at least 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 days. In some embodiments, the combination or composition disclosed herein are administered to the subject for a period of at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 weeks. In some embodiments, the combination or composition disclosed herein are administered to the subject for a period of at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 13, 14, 15, 16, 17, 18, 19, or 20 months. In some embodiments, the methods, B components, M components, the combinations, or compositions provided herein, comprising, or alternatively consisting essentially of, or yet further consisting inhibiting metastatic potential of the cancer, reduction in tumor size, a reduction in tumor burden, longer progression free survival, or longer overall survival of the subject. In one aspect, the methods, B components, M components, combination, or compositions further comprise administration of an additional therapeutic agent. In some cases, the additional therapeutic agent disclosed herein comprise, or consists essentially of, or yet further consists of, a chemotherapeutic agent, an immunotherapeutic agent, a targeted therapy, radiation therapy, or a combination thereof. Illustrative additional therapeutic agents include, but are not limited to, alkylating agents such as altretamine, busulfan, carboplatin, carmustine, chlorambucil, cisplatin, cyclophosphamide, dacarbazine, lomustine, melphalan, oxalaplatin, temozolomide, or thiotepa; antimetabolites such as 5-fluorouracil (5-FU), 6- mercaptopurine (6-MP), capecitabine, cytarabine, floxuridine, fludarabine, gemcitabine, hydroxyurea, methotrexate, or pemetrexed; anthracyclines such as daunorubicin, doxorubicin, epirubicin, or idarubicin; topoisomerase I inhibitors such as topotecan or irinotecan (CPT- 11); topoisomerase II inhibitors such as etoposide (VP- 16), teniposide, or mitoxantrone; mitotic inhibitors such as docetaxel, estramustine, ixabepilone, paclitaxel, vinblastine, vincristine, or vinorelbine; or corticosteroids such as prednisone, methylprednisolone, or dexamethasone. In some cases, the B component, M component, combination, or composition with or without the additional therapeutic agent comprise, or consists essentially of, or yet further consists of, or is used as a first-line therapy. As used herein, "first-line therapy" comprises, or consists essentially of, or yet further consists of, a primary treatment for a subject with a cancer. In some instances, the cancer is a primary cancer. In other instances, the cancer is a metastatic or recurrent cancer. In some cases, the first-line therapy comprises, or consists essentially of, or yet further consists of, chemotherapy. In other cases, the first-line treatment comprises, or consists essentially of, or yet further consists of, radiation therapy. A skilled artisan would readily understand that different first-line treatments may be applicable to different type of cancers. In some cases, the additional therapeutic agent comprises, or consists essentially of, or yet further consists of, or is used as a second-line therapy, a third-line therapy, a fourth-line therapy, or a fifth-line therapy. As used herein, a second-line therapy encompasses treatments that are utilized after the primary or first-line treatment stops. They can also be used as third- line, fourth-line or fifth line therapy. A third-line therapy, a fourth-line therapy, or a fifth-line therapy encompass subsequent treatments. As indicated by the naming convention, a third- line therapy encompass a treatment course upon which a primary and second-line therapy have stopped. In some cases, the additional therapeutic agent comprises, or consists essentially of, or yet further consists of, a salvage therapy. In some cases, the additional therapeutic agent comprises, or consists essentially of, or yet further consists of, a palliative therapy. In connection with cancer care, the treatment can comprise an additional therapeutic agent that comprises, or consists essentially of, or yet further consists of, an inhibitor of the enzyme poly ADP ribose polymerase (PARP). Exemplary PARP inhibitors include, but are not limited to, olaparib (AZD-2281, LYNPARZA®, from Astra Zeneca), rucaparib (PF- 01367338, RUBRACA®, from Clovis Oncology), niraparib (MK-4827, ZEJULA®, from Tesaro), talazoparib (BMN-673, from BioMarin Pharmaceutical Inc.), veliparib (ABT-888, from Abb Vie), CK-102 (formerly CEP 9722, from Teva Pharmaceutical Industries Ltd.), E7016 (from Eisai), iniparib (BSI 201, from Sanofi), and pamiparib (BGB-290, from BeiGene). In some cases, the additional therapeutic agent comprises, or consists essentially of, or yet further consists of, an immune checkpoint inhibitor. Exemplary checkpoint inhibitors include: PD-L1 inhibitors such as Genentech' s MPDL3280A (RG7446), anti-PD-Ll monoclonal antibody MDX-1105 (BMS-936559) and BMS-935559 from Bristol -Meyer's Squibb, MSB0010718C, and AstraZeneca's MEDI4736; PD-L2 inhibitors such as GlaxoSmithKline's AMP -224 (Amplimmune), and rHIgM12B7; PD-1 inhibitors such as anti-mouse PD-1 antibody Clone J43 (Cat # BE0033-2) from BioXcell, anti-mouse PD-1 antibody Clone RMP1-14 (Cat # BE0146) from BioXcell, mouse anti-PD-1 antibody Clone EH12, Merck's MK-3475 anti-mouse PD-1 antibody (Keytruda, pembrolizumab, lambrolizumab), AnaptysBio's anti-PD-1 antibody known as ANB011, antibody MDX-1106 (ONO-4538), Bristol-Myers Squibb's human IgG4 monoclonal antibody nivolumab (OPDIVO®, BMS-936558, MDX1106), AstraZeneca's AMP-514 and AMP -224, and Pidilizumab (CT-011) from CureTech Ltd; CTLA-4 inhibitors such as Bristol Meyers Squibb's anti-CTLA-4 antibody ipilimumab (also known as YERVOY®, MDX-010, BMS- 734016 and MDX-101), anti-CTLA4 antibody clone 9H10 from Millipore, Pfizer' s tremelimumab (CP-675,206, ticilimumab), and anti-CTLA4 antibody clone BNI3 from Abeam; LAG3 inhibitors such as anti-Lag-3 antibody clone eBioC9B7W (C9B7W) from eBioscience, anti-Lag3 antibody LS-B2237 from LifeSpan Biosciences, IMP321 (ImmuFact) from Immutep, anti-Lag3 antibody BMS-986016, and the LAG-3 chimeric antibody A9H12; B7-H3 inhibitors such as MGA271; KIR inhibitors such as Lirilumab (IPH2101); CD137 inhibitors such as urelumab (BMS-663513, Bristol-Myers Squibb), PF- 05082566 (anti-4- lBB, PF-2566, Pfizer), or XmAb-5592 (Xencor); PS inhibitors such as Bavituximab; and inhibitors such as an antibody or fragments (e.g., a monoclonal antibody, a human, humanized, or chimeric antibody) thereof, RNAi molecules, or small molecules to TFM3, CD52, CD30, CD20, CD33, CD27, OX40, GITR, ICOS, BTLA (CD272), CD160, 2B4, LAIR1, TIGHT, LIGHT, DR3, CD226, CD2, or SLAM. In some cases, the additional therapeutic agent comprises, or consists essentially of, or yet further consists of, pembrolizumab, nivolumab, tremelimumab, or ipilimumab. In some cases, the additional therapeutic agent comprises, or consists essentially of, or yet further consists of, an antibody such as alemtuzumab, trastuzumab, ibritumomab tiuxetan, brentuximab vedotin, ado-trastuzumab emtansine, or blinatumomab. In some cases, the additional therapeutic agent comprises, or consists essentially of, or yet further consists of, a cytokine. Exemplary cytokines include, but are not limited to, IL-Ιβ, IL-6, IL-7, IL-10, IL-12, IL-15, IL-21, or TNFα. In some embodiments, the additional therapeutic agent comprises, or consists essentially of, or yet further consists of, a receptor agonist. In some instances, the receptor agonist comprises, or consists essentially of, or yet further consists of, a Toll-like receptor (TLR) ligand. In some cases, the TLR ligand comprise, or consists essentially of, or yet further consists of, TLR1, TLR2, TLR3, TLR4, TLR5, TLR6, TLR7, TLR8, or TLR9. In some cases, the TLR ligand comprise, or consists essentially of, or yet further consists of, a synthetic ligand such as, for example, Pam3Cys, CFA, MALP2, Pam2Cys, FSL-1, Hib- OMPC, Poly I:C, poly A:U, AGP, MPL A, RC-529, MDF2p, CFA, or Flagellin. In some cases, the additional therapeutic agent comprises, or consists essentially of, or yet further consists of, an adoptive T cell transfer (ACT) therapy. In one embodiment, ACT involves identification of autologous T lymphocytes in a subject with, e.g., anti-tumor activity, expansion of the autologous T lymphocytes in vitro, and subsequent reinfusion of the expanded T lymphocytes into the subject. In another embodiment, ACT comprise, or consists essentially of, or yet further consists of, use of allogeneic T lymphocytes with, e.g., anti-tumor activity, expansion of the T lymphocytes in vitro, and subsequent infusion of the expanded allogeneic T lymphocytes into a subject in need thereof. In some instances, the additional therapeutic agent is, or can be used as a vaccine, optionally, an oncolytic virus. Exemplary oncolytic viruses include T-Vec (Amgen), G47A (Todo et al.), JX-594 (Sillajen), CG0070 (Cold Genesys), and Reolysin (Oncolytics Biotech). In some instances, the composition or combination is administered in combination with a radiation therapy. Kits In one particular aspect, the present disclosure provides kits for performing the methods of this disclosure as well as instructions for carrying out the methods of the present disclosure. The kit comprises, or alternatively consists essentially of, or yet further consists of one or more of the M component, B component, combinations, or compositions and instructions for use. In a further aspect, the instruction for use provides directions to conduct any of the methods disclosed herein. The kits are useful for detecting the presence of cancer such as lung cancer in a biological sample e.g., any bodily fluid including, but not limited to, e.g., sputum, serum, plasma, lymph, cystic fluid, urine, stool, cerebrospinal fluid, ascitic fluid or blood and including biopsy samples of body tissue. The test samples may also be a tumor cell, a normal cell adjacent to a tumor, a normal cell corresponding to the tumor tissue type, a blood cell, a peripheral blood lymphocyte, or combinations thereof. The test sample used in the above- described method will vary based on the assay format, nature of the detection method and the tissues, cells or extracts used as the sample to be assayed. Methods for preparing protein extracts or membrane extracts of cells are known in the art and can be readily adapted in order to obtain a sample which is compatible with the system utilized. The kit components, (e.g., reagents) can be packaged in a suitable container. The kit can also comprise, or alternatively consist essentially of, or yet further consist of, e.g., a buffering agent, a preservative or a protein-stabilizing agent. The kit can further comprise, or alternatively consist essentially of, or yet further consist of components necessary for detecting the detectably-label, e.g., an enzyme or a substrate. The kit can also contain a control sample or a series of control samples, which can be assayed and compared to the test sample. Each component of the kit can be enclosed within an individual container and all of the various containers can be within a single package, along with instructions for interpreting the results of the assays performed using the kit. The kits of the present disclosure may contain a written product on or in the kit container. The written product describes how to use the reagents contained in the kit. As amenable, these suggested kit components may be packaged in a manner customary for use by those of skill in the art. For example, these suggested kit components may be provided in solution or as a liquid dispersion or the like. As is apparent to those of skill in the art, the aforementioned methods and compositions can be combined with other therapeutic composition and agents for the treatment or the disclosed diseases or conditions. Experimental To determine whether the two RNA genomes that have different size and unrelated sequence cause different immune stimulation, Applicant compared the therapeutic efficacies of B, M components and unfractionated CPMV in vitro and in mouse cancer models. Applicant found that separated B and M particles behaved similarly to the mixed CPMV, activating innate immune cells to induce the secretion of pro-inflammatory cytokines such as IFNα, IFNγ, IL-6 and IL-12, while inhibiting immunosuppressive cytokines such as TGFβ and IL-10. In murine models of melanoma and colon cancer, the mixed and separated CPMV particles all significantly reduced tumor growth and prolonged survival with no significant difference. This shows that the specific RNA genomes similarly stimulate the immune system even though B particles have 40% more RNA than M particles; each CPMV particle type can be used as an effective adjuvant against cancer with the same efficacy as native mixed CPMV. From a translational point of view the use of either B or M component vs. the mixed CPMV formulation offers the advantage that separated B or M alone are non-infectious toward plants and thus provide agronomic safety. Materials and Methods Separation of CPMV into its B and M components. CPMV was propagated in cowpea plants by mechanical inoculation and purified using previously published methods.28In brief, CPMV was purified with a 1:1 chloroform:butanol extraction, PEG precipitation, followed by ultracentrifugation in a 10–40% sucrose density gradient. The B and M components were separated by Nycodenz gradient ultracentrifugation using a 30–60% (w / v) Nycodenz solution prepared in 10 mM sodium phosphate buffer (pH 7.0) and filled into a SW40Ti tube.29The CPMV suspension (0.1 mg / μL) was layered onto the gradient and centrifuged at 26,000 g for 24 h at 4℃. CPMV particles were collected under white light and concentrated by ultracentrifugation at 42,000 g for 2 h at 4℃. The concentration of collected CPMV components were determined using ultraviolet-visible (UV-Vis) spectroscopy (Nanodrop) and, calculated using the Beer-Lambert equation; A= ε*d*c where A is the absorbance at 260 nm, ε is the extinction coefficient of CPMV (8.1 mL mg-1cm-1), and d is the path length (0.1 cm-1). The ratio of B and M components was calculated by dividing the concentration of each component by collected components. Agarose gel electrophoresis of CPMV particles and purified RNA. CPMV particles (10 μg in 1× Gel Loading Purple dye) were loaded onto a 1.2% (w / v) agarose gel stained with GelRed nucleic acid and run at 100 V for 35 min in Tris-acetate EDTA (TAE) buffer. The gel was visualized under UV light using an AlphaImager system (Protein Simple) after staining with Coomassie Brilliant Blue. Encapsidated RNA was extracted using the Quick-RNA Miniprep kit (Zymo Research). RNA purity was determined by measuring the absorbance at 260 and 280 nm and calculating the ratio (A260 / 280). RNAs extracted from mixed and separated CPMV components were analyzed by 1.2% agarose gel electrophoresis as above. Denaturing gel electrophoresis. Mixed and separated CPMV components (10 μg) in 1× LDS loading dye (Thermo Fisher Scientific) were denatured at 95℃ for 5 min before fractionation with sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE, 4-12% NuPAGE, Invitrogen) in 1× (3-(N-morpholino)propanesulfonic acid) (MOPS) buffer. The gel was stained with GelCode Blue Safe protein stain and visualized under white light and imaged on the AlphaImager System. Transmission electron microscopy (TEM). Mixed and separated CPMV components were dispersed in water at a concentration of 0.1 mg / mL and were pipetted onto a 400-mesh hexagonal copper grid on a Formvar support film (Ted Pella) followed by staining with 2% uranyl acetate for 2 min. TEM images were acquired using a JEM-1400Plus microscope (JEOL). Dynamic light scattering (DLS). For the analysis of size and surface charge, CPMV particles and components were dispersed in 0.1 M potassium phosphate (KP) buffer (pH 7.0) at concentrations of 0.1 mg / mL (mixed particles) and 1 mg / mL (separated particles). The size and zeta potential were measured using a Zetasizer Nano ZSP / Zen5600 (Malvern Panalytical). Size-exclusion chromatography (SEC). CPMV particles were loaded onto a Superose 6 increase column mounted on an Äkta Explorer chromatography system (Cytiva) at a flow rate of 0.5 mL / min in 0.1 M KP buffer (pH 7.0). The absorbance was recorded at 260 and 280 nm. Cell culture. RAW-Blue cells (Invivogen) were grown in Dulbecco’s modified Eagle’s medium (DMEM, Gibco) supplemented with 10% (v / v) fetal bovine serum (FBS), 1% (v / v) penicillin-streptomycin, and 100 µg / mL Normocin and Zeocin. B16F10 melanoma cells and CT26 colon cancer cells were obtained from the ATCC and were grown in DMEM and RPMI 1640, respectively, supplemented with 10% (v / v) FBS and 1% (v / v) penicillin- streptomycin. All cells were maintained at 37°C in a humidified 5% CO2incubator. RAW-Blue cell assay. RAW-Blue cells (1 × 105cells / 200 μL) were seeded in 96-well flat-bottom plates and CPMV particles were added at a dose of 1 μg per well. The cells were incubated for 24 h at 37℃ in a 5% CO2. Applicantthen mixed 20 μL of the supernatant with 180 μL of Quanti-Blue solution (Invivogen) and incubated the mixture for 6 h at room temperature. The level of secreted embryonic alkaline phosphatase (SEAP) was measured at 630 nm. Animal studies. All mouse studies were approved by the Institutional Animal Care and Use Committee (IACUC) at the University of California, San Diego. Female C57BL / 6J and BALB / c mice were purchased from The Jackson Laboratory. BALB / c mice (n = 5, 6–8 weeks old) were intraperitoneally (i.p.) implanted with 5 × 105CT26 cells in 200 μL phosphate-buffered saline (PBS). Mice were randomly assigned to four groups: (1) PBS control, (2) CPMV mix, (3) CPMV B-type, and (4) CPMV M-type. The treatments were administered i.p. three times at weekly intervals, starting on day 3 at a dose of 100 μg in 200 μL of PBS. Tumor growth was monitored by measuring abdominal circumference and body weight. For melanoma studies, 2.5 × 105B16F10 cells in 20 μL PBS were intradermally (i.d.) inoculated into the left flank of C57BL / 6J mice (n = 7, 6–8 weeks old). CPMV treatments were injected intratumorally (i.t.) at a dose of 100 μg in 20 μL PBS three times per week, starting on day 7 after tumor challenge. Tumor volume was calculated using the following equation: volume = (length × width2) / 2. Tumor volume and survival rates were monitored over time, and mice were euthanized once the tumor volume exceeded 1500 mm3. Cytokine evaluation. Peritoneal cavity washes were collected 7 days after the third CPMV treatment and an enzyme-linked immunosorbent assay (ELISA) was used to determine the quantity of IL-6, IL-10, IL-12, TNFα, TGFβ and IFN ^ in the supernatant (Thermo Fisher Scientific). For ex vivo cytokine secretion assays, peritoneal cavity cells were collected from tumor-bearing mice treated with PBS, 7 days after the third injection. Peritoneal cavity cells (3 × 106cells) were seeded in 24-well plates and stimulated with 10 μg of CPMV. The supernatant was collected after incubation for 24 h. For splenocyte assays, spleens from C57BL / 6 or TLR-7− / −mice were harvested, and 5 × 105splenocytes were cultured with either CPMV mix (12 μg / mL), CPMV M-type (12 μg / mL), CPMV B-type (12 μg / mL), or CPMV M-type (6 μg / mL) + CPMV B-type (6 μg / mL) in 200 μL of complete RPMI 1640 for 24 h in 96-well plates similar to previous studies.14The conditioned medium was analyzed by ELISA to detect IL-6 or IFNα. Statistical analysis. All data were analyzed using GraphPad Prism v7.0 and are presented as means ± standard deviations (SD). ELISA data were determined by one-way analysis of variance (ANOVA) with Turkey’s multiple comparison test. Tumor volumes were compared using an using two-way ANOVA and survival rates were compared using a log- rank (Mantel-Cox) test. A p value below 0.05 was considered statistically significant. Results Preparation and characterization of mixed and separated CPMV components CPMV B and M components were separated by Nycodenz gradient centrifugation (Fig. 1), and their properties were compared to those of the native mixed CPMV sample (Fig. 2A). The B-type particles accounted for 58 ± 7.32% of the mixture by mass, and the M-type particles accounted for 42 ± 7.32% of the mixture, indicating roughly equal numbers of capsids containing RNA-1 or -2. The separation of CPMV particle types was confirmed by agarose gel electrophoresis of the RNA extracted from mixed and separated particles (Fig. 2B). The mixed particles yielded two RNA bands at 3.5 kb (RNA-2) and 6 kb (RNA-1), whereas the separated particles yielded a single band each, confirming separation of the components. To confirm that the isolated components remained intact, mixed and separated CPMV particles were analyzed by agarose gel electrophoresis (Fig. 2C). The separated CPMV particles were intact, as nucleic acids (RNA stain) and CPMV capsids (protein stain) co-migrate under electrophoretic separation. The three preparations were denatured and fractionated by SDS-PAGE. All samples produced identical protein bands of 42 and 24 kDa, representing the L and S coat protein subunits, respectively, and confirming that the two distinct RNAs are encapsidated in identical protein capsids (Fig. 2D). TEM images revealed the monodispersity and icosahedral structure of all three particle preparations (Fig. 2E). DLS showed that all three preparations have a mean particle diameter of ~30 nm (Fig. 2F), and the zeta potentials indicated that the surface charge of B-type particles (–14.6 mV) and M-type particles (–14.69 mV) were similar to native mixed CPMV (–15.5 mV) (Fig. 2G). SEC confirmed the structural integrity of all three preparations, with the same elution volume of 11.5 mL and an absorbance ratio (A260 / 280) of ~1.8, indicating intact capsid proteins with encapsidated RNAs (Fig. 2H). Immunogenicity of mixed and separated CPMV components The immunogenicity of the CPMV particles was confirmed using RAW-Blue cells, which are derived from the murine macrophage cell line RAW264.7 and express numerous PRRs. As expected, the mixed CPMV preparation induced a potent immunostimulatory effect activating NF-κB and eliciting SEAP production. The level of SEAP increased 4.17-fold in response to the mixed particles, 4.6-fold in response to the B component and 3.4-fold in response to the M component, indicating that the mixed and separated particles were similar in immune cell activation (Fig. 3A). The mechanism was confirmed by quantifying cytokine levels in peritoneal cavity washes collected from mice bearing CT26-derived tumors. Generally immune suppressive peritoneal cavity cells from the TME were treated with mixed or separated CPMV before measuring the levels of IL-6, IL-12, IFN ^, IL-10 and TGFβ by ELISA (Fig. 3B). Like the mixed CPMV preparation, the B and M components increased the abundance of pro- inflammatory cytokines (IL-6, IL-12, and IFN ^), which improve antigen priming, recruit immune cells to the TME, and enhance their cytolytic activity.30Similarly, both particle types reduced the abundance of immunosuppressive cytokines (IL-10 and TGFβ) to the same level as CPMV. There were no statistical differences between the mixed and separated particles. To gain further insight into the activation of TLR signaling by CPMV and the separated particles, the stimulation of IL-6 and IFNα was assessed in splenocytes isolated from C57BL / 6 and TLR-7– / –mice (Fig. 3C). The production of IL-6 was induced to a similar extent by all three preparations. Intact CPMV particles containing viral RNA activate TLRs- 2, -4 and -7 with the CPMV capsid activating TLR-2 and -4, and the viral RNA activating TLR-7.14Therefore, release of IL-6 by all three preparations was partially suppressed in TLR-7– / –mice compared to wild-type C57BL / 6 controls, but not completely eliminated due to TLR-2 and -4 activation. The reduction in activation was similar between the CPMV mixed and separated solutions. TLR-7 signaling predominantly regulates the production of type I interferons.31Therefore, Applicant measured the levels of IFNα to confirm the stimulation of immunity via TLR-7 (Fig. 3C). Applicant found that all three preparations induced IFNα production in wild-type mice but none did in the TLR-7– / –mutant. Applicant concluded that IL-6 and IFNα were similarly stimulated in splenocytes treated with mixed or separated CPMV particles and that all three preparations were similarly immunostimulatory. This similar IFNα production by all three preparations demonstrates that TLR-7 responds quantitatively similarly to both B and M components, despite no sequence similarity of the carried RNA and more RNA encapsidated per particle in B than M components. Therapeutic efficacy of mixed and separated CPMV particles in vivo The in vivo therapeutic efficacy of the CPMV particles was investigated using CT26 colon cancer and B16F10 melanoma models. In the colon cancer model, mice were challenged i.p. with 500,000 CT26 cells and treated with each of the three different CPMV preparations or a PBS control three times at weekly intervals, starting on day 3 post tumor inoculation (Fig. 4A). As expected, the mixed CPMV treatment significantly reduced the abdominal circumference of tumor-bearing mice (which increases due to tumor load and ascites) and prolonged their survival. On day 27, the average tumor volume in the PBS control group was 7.75 ± 1.06 cm, compared to 5.38 ± 1.16 cm in the CPMV treatment group, a 67% decrease (FIGS. 4B, 4C). The B and M components showed similar efficacy, reducing tumor growth on day 27 by 70.32% and 63.35%, respectively. The mice treated with mixed CPMV, B and M components demonstrated survival rates of 57.14%, 57.14% and 71.4%, respectively, at day 40, and all had a significant (**p < 0.01) improvement over the PBS control group (FIG. 4D). Tumor growth in the PBS control group was aggressive, with a median overall survival of 23 days. There was no significant body weight loss among the three treatment groups, indicating safety of the treatment (FIG. 4E). Similar results were achieved in the B16F10 melanoma mouse model (FIG. 5). When dermal tumors reached a volume of ~30 mm3(day 7), mice were randomly assigned to one of the three CPMV treatment groups or to the PBS control (Fig. 5A). The three CPMV treatments significantly delayed tumor growth compared to the PBS control (**p < 0.01). The day-40 tumor volumes of mice treated with mixed CPMV, B and M components were 454 ± 272.5, 326 ± 139.2 and 590 ± 297.8 mm3, respectively (FIGS. 5B, 5C). The survival increased significantly in response to the three CPMV treatments compared to PBS (***p < 0.001), and there was no significant difference between the CPMV groups. More than 50% of the animals in the three treatment groups survived until the end of the experiment at 40 days (FIG. 5D). To further compare the in vivo immunogenicity of the three CPMV fractions in animal models, mice were i.p. inoculated with CT26 cells and treated with the mixed or separated CPMV particles as shown in Fig. 4A. On day 24, peritoneal cavity washes were collected for analysis of cytokine levels by ELISA (FIG. 6). As confirmed in the ex vivo experiments, all three CPMV treatments caused elevated production of IL-6, IL-12 and IFN ^ and depleted IL-10 and TGFβ similarly between themselves and significantly compared to the PBS control. Applicant therefore observed no significant differences in immunotherapeutic efficacy between the three CPMV treatment groups, and note that all three treatments resulted in significant improvements compared to PBS controls. Discussion Although CPMV does not infect animal cells, it has demonstrated potency as a cancer immunotherapy due to its ability to stimulate a strong and durable antitumor response against the primary treated tumor that leads to systemic antitumor efficacy and abscopal response.16,18, 32, 33Previous mechanistic studies show that TLR activation, specifically TLRs 2, 4, and 7, mediate CPMV in situ vaccination efficacy.14TLR-7 activation is induced by the RNA of CPMV, therefore, CPMV without RNA demonstrates a significant drop-off in efficacy compared to native CPMV.25The importance of the RNA is also highlighted by studies in which inactivated CPMV was studied: when UV light or chemicals such as formalin were used to inactivate CPMV by RNA and protein crosslinking, in situ vaccine efficacy was lost or reduced and this was consistent with a loss in TLR-7 signaling.25, 34, 35These studies indicate the significance of genomic RNA in CPMV immunotherapy. CPMV has a bipartite genome thereby it has identical particles carrying distinct RNAs (RNA-1 and RNA-2) and both RNAs must be in a single plant cell to mediate productive infection. In past in situ vaccine experiments, CPMV was always utilized as the harvested mixture of different nanoparticles carrying RNA-1 and RNA-2 - efficacy of each CPMV component had never been explicitly tested. Here, Applicant investigated whether CPMV with encapsidated RNA-1 (B-type) and RNA-2 (M-type) have different immune stimulatory properties or therapeutic efficacy in cancer treatment. This study reveals that (i) both CPMV B-type and M-type attenuate tumor growth and improve survival compared to PBS similarly to mixed CPMV, (ii) CPMV components similarly immunomodulate the antitumor response through expression of pro-inflammatory and immunosuppressive cytokines, and (iii) CPMV components demonstrate similar TLR-associated immune recognition and knockout of TLR- 7 dampens efficacy similarly between CPMV mixed, B or M. Thus, the study shows that the immunotherapeutic effects of CPMV encapsidating RNA-1 or RNA-2 have similar immune- mediated anti-cancer effects. Questions remain as to what area of CPMV RNA bind to TLR- 7, and more detailed mechanistic and structure-based experiments investigate that in the future. However, the lack of a difference indicates that binding to TLR-7 is specific to certain regions of the CPMV viral RNA that are present in both RNA-1 and RNA-2, and is not directly proportional to RNA mass, as the longer RNA-1 (6 vs. 3.5 kb) did not induce greater immunotherapeutic responses than RNA-2. This may be similar to how unmethylated CpG oligodeoxynucleotides activate TLR-9, but this must be experimentally determined.36This is the first study comparing immunotherapeutic differences between CPMV particles containing RNA-1 and RNA-2. Applicant’s findings show that treatment with any CPMV mixed, B or M are equally effective immunotherapies in cancer treatment and that isolation and utilization of CPMV B or M will not further improve therapeutic efficacy. Mechanistically this study contributes to the further understanding of the CPMV in situ vaccine, and from a translational development perspective this study adds value in lead candidate selection and development of a manufacturing process. Mixed CPMV is infectious toward crops, but separated B or M components are not. Therefore, one could propose to separate the components and use B or M component as the lead drug candidate. While potency is matched to that of mixed CPMV, separated B or M component offer agronomic safety, because they are non-infectious toward plants. Conclusions CPMV is a promising vaccine component due to its immunostimulatory potency, making it an effective therapeutic strategy for cancer. The aim of this study was to compare the therapeutic efficacy of CPMV particles containing different RNAs for cancer in situ vaccination. Both particle types induced an immune response similar in magnitude and mechanism compared to the mixed CPMV particles. In animal models of melanoma and colon cancer, both particle types showed similar therapeutic efficacy to mixed CPMV, significantly suppressing tumor growth and enhancing the survival rate. Applicant did not observe a statistically significant difference between the native CPMV mixture and the separated RNA-1 and RNA-2 carrying B and M components in any of the efficacy and mechanistic studies. The individual particle types can therefore be utilized as effective immune adjuvants with the same efficacy as native CPMV mixtures. An advantage of using the separated components vs. mixed CPMV is that the separated B and M component alone are not infectious to crops and thus provide agronomic safety. Numbered Embodiments Additional embodiments include the following numbered embodiments: 1. A composition comprising an isolated Secoviridae plant virus B and / or M component. 2. A composition comprising an isolated Secoviridae plant virus B component. 3. A composition comprising an isolated Secoviridae plant virus M component. 4. The composition of any of embodiments 1-3 wherein the B and / or M component is the Secoviridae plant viral capsid containing an RNA polynucleotide, which can further comprise the naturally occurring RNA or any other RNA such as an RNA vaccine or anti- cancer therapy. 5. The composition of any one of embodiments 1-4, wherein the isolated B and / or the M Secoviridae plant virus component is the only viral or virally derived component in the composition. 6. The composition of any one of embodiments 1-5, wherein the isolated B and / or M Secoviridae plant virus component is the only anti-cancer agent in the composition. 7. An anti-cancer composition consisting essentially of an isolated Secoviridae plant virus B and / or M component and viral capsid containing an RNA polynucleotide and optionally wherein component is the B and / or M viral capsid which can further comprise the naturally occurring RNA or any other RNA such as an RNA vaccine or anti-cancer therapy. 8. An anti-cancer composition consisting essentially composition comprising an isolated Secoviridae plant virus B component and optionally wherein B component is the B viral capsid which can further comprise be the naturally occurring RNA or any other RNA such as an RNA vaccine or anti-cancer therapy. 9. An anti-cancer composition consisting essentially of an isolated Secoviridae plant virus M component and optionally wherein M component is the M viral capsid which can further comprise the naturally occurring RNA or any other RNA such as an RNA vaccine or anti-cancer therapy. 10. The composition of any of embodiments 1-9, wherein the isolated Secoviridae is / are not inactivated. 11. The composition of any of embodiments 1-10, wherein the isolated Secoviridae B component comprises RNA-1 and / or the M component comprises RNA-2. 12. An anti-cancer composition for use in treating a cancer or inducing an immune response, the composition comprising the composition of the composition of any of embodiments 1-11. 13. The composition of any of embodiments 1-12, wherein the isolated Secoviridae plant virus is an isolated virus from the Comovirus, Fabavirus, Nepovirus, Cheravirus, Sadwavirus, Sequivirus, Stralarivirus, Torradovirus, or Waikavirus genera. 14. The composition of any of embodiments 1-12, wherein the isolated Secoviridae is an isolated Cowpea mosaic virus (CPMV). 15. The composition of any of embodiments 1-14 and a carrier, optionally a pharmaceutically acceptable carrier. 16. The composition of any of embodiments 1-15, wherein the B and / or M components of the Secoviridae are the same or different. 17. The composition of any of embodiments 1-5 or 7-16, further containing an additional therapeutic agent. 18. The composition of any of embodiments 1-5 or 7-16, further containing an additional anti-cancer agent. 19. The composition of any of embodiments 1-18, wherein the B component comprises an RNA polynucleotide according to SEQ ID NO: 3 and / or the M component comprises an RNA polynucleotide according to SEQ ID NO: 10. 20. The composition of any of embodiments 1-18, wherein the isolated Secoviridae is CPMV, wherein the B component comprises: a) an RNA polynucleotide encoding a protease cofactor, a helicase, a viral genome- linked protein (Vpg), a protease, and a polymerase, wherein the protease cofactor has a sequence according to SEQ ID NO: 5, wherein the helicase has a sequence according to SEQ ID NO: 6, wherein the Vpg has a sequence according to SEQ ID NO: 7, wherein the protease has a sequence according to SEQ ID NO: 8, and wherein the polymerase has a sequence according to SEQ ID NO: 9; b) a VPg peptide has a sequence according to SEQ ID NO: 4; and c) a PolyA tail. 21. The composition of any of embodiments 1-18, wherein the isolated Secoviridae is CPMV, wherein the M component comprises: a) an RNA polynucleotide encoding a movement protein, a large coat protein, and a small coat protein, wherein the movement protein has a sequence according to SEQ ID NO: 11, wherein the large coat protein has a sequence according to SEQ ID NO: 12, and wherein the small coat protein has a sequence according to SEQ ID NO: 13; b) a VPg peptide has a sequence according to SEQ ID NO: 4; and c) a PolyA tail. 22. A method for inducing an immune response in a subject in need thereof comprising administering to the subject the composition of any of embodiments 1-21. 23. The method of embodiment 22, wherein the immune response is activation of innate immune cells to induce secretion of pro-inflammatory cytokines, optionally IFNα, IFNγ, IL-6 and IL-12. 24. The method of embodiment 22 or 23, wherein the immune response is inhibiting the secretion of innate immune cells to induce secretion of immunosuppressive cytokines such as TGFβ and IL-10. 25. A method to inhibit the growth of a cancer cell comprising contacting the cell with a composition of any of embodiments 1-21. 26. The method of embodiment 25, wherein the contacting is in vitro or in vivo. 27. The method of embodiment 25 or 26, wherein the cancer cell is selected from the group of: melanoma, breast cancer, prostate cancer, lung cancer, ovarian cancer, skin cancer, bladder cancer, pancreatic cancer, gastric cancer, esophageal cancer, colon cancer, head and neck cancer, brain cancer, glioma, cervical cancer, hepatocellular cancer, inflammatory mammary cancer or thyroid cancer, that is optionally a primary or a metastatic cancer. 28. The method of any of embodiments 25-27, wherein the cancer cell is a mammalian cell, optionally a human cell. 29. A method for treating cancer in a subject in need thereof, comprising administering to the subject the composition of any of embodiments 1-21. 30. The method of embodiment 29, wherein the cancer is a blood cancer or a solid tumor. 31. The method of embodiment 29, wherein the cancer is selected from the group of: melanoma, breast cancer, prostate cancer, lung cancer, ovarian cancer, skin cancer, bladder cancer, pancreatic cancer, gastric cancer, esophageal cancer, colon cancer, head and neck cancer, brain cancer, glioma, cervical cancer, hepatocellular cancer, inflammatory mammary cancer, or thyroid cancer. 32. The method of embodiment 29, wherein the cancer is a metastatic cancer or a primary colon cancer or a primary or a metastatic melanoma. 33. The method of any of embodiments 29 to 32, wherein the subject is a mammal or a human. 34. The method of any of embodiments 29 to 33, further comprising the administration of a different cancer therapy or tumor resection. 35. The method of any one of embodiments 29-34, wherein the administering comprises intravenous, subcutaneous, intratumoral, or intraperitoneal delivery. 36. The method of any of embodiments 29-35, wherein the treatment comprises one or more of: inhibiting metastatic potential of the cancer; reduction in tumor size; a reduction in tumor burden, longer progression free survival and longer overall survival of the subject. 37. A kit comprising one or more of the composition or combination of any of embodiments 1-21 and optional instructions for use. Equivalents It is to be understood that while the disclosure has been described in conjunction with the above embodiments, that the foregoing description and examples are intended to illustrate and not limit the scope of the disclosure. Other aspects, advantages, and modifications within the scope of the disclosure will be apparent to those skilled in the art to which the disclosure pertains. Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this disclosure belongs. All nucleotide sequences provided herein are presented in the 5’ to 3’ direction. The embodiments illustratively described herein may suitably be practiced in the absence of any element or elements, limitation or limitations, not specifically disclosed herein. Thus, for example, the terms “comprising,” “including,” containing,” etc. shall be read expansively and without limitation. Additionally, the terms and expressions employed herein have been used as terms of description and not of limitation, and there is no intention in the use of such terms and expressions of excluding any equivalents of the features shown and described or portions thereof, but it is recognized that various modifications are possible within the scope of the disclosure. Thus, it should be understood that although the present disclosure has been specifically disclosed by specific embodiments and optional features, modification, improvement and variation of the embodiments therein herein disclosed may be resorted to by those skilled in the art, and that such modifications, improvements and variations are considered to be within the scope of this disclosure. The materials, methods, and examples provided here are representative of particular embodiments, are exemplary, and are not intended as limitations on the scope of the disclosure. The scoped of the disclosure has been described broadly and generically herein. Each of the narrower species and subgeneric groupings falling within the generic disclosure also form part of the disclosure. This includes the generic description with a proviso or negative limitation removing any subject matter from the genus, regardless of whether or not the excised material is specifically recited herein. In addition, where features or aspects of the disclosure are described in terms of Markush groups, those skilled in the art will recognize that embodiments of the disclosure may also thereby be described in terms of any individual member or subgroup of members of the Markush group. All publications, patent applications, patents, and other references mentioned herein are expressly incorporated by reference in their entirety, to the same extent as if each were incorporated by reference individually. In case of conflict, the present specification, including definitions, will control. Other aspects are set forth within the following claims.

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(17) Wang, C.; Fiering, S. N.; Steinmetz, N. F. Cowpea Mosaic Virus Promotes Anti-Tumor Activity and Immune Memory in a Mouse Ovarian Tumor Model. Adv Ther (Weinh) 2019, 2, 5. (18) Kerstetter-Fogle, A.; Shukla, S.; Wang, C.; Beiss, V.; Harris, P. L. R.; Sloan, A. E.; Steinmetz, N. F. Plant Virus-Like Particle In Situ Vaccine for Intracranial Glioma Immunotherapy. Cancers (Basel) 2019, 11, 4. (19) Shukla, S.; Myers, J. T.; Woods, S. E.; Gong, X.; Czapar, A. E.; Commandeur, U.; Huang, A. Y.; Levine, A. D.; Steinmetz, N. F. Plant viral nanoparticles-based HER2 vaccine: Immune response influenced by differential transport, localization and cellular interactions of particulate carriers. Biomaterials 2017, 121, 15-27. (20) Hoopes, P. J.; Wagner, R. J.; Duval, K.; Kang, K.; Gladstone, D. J.; Moodie, K. L.; Crary- Burney, M.; Ariaspulido, H.; Veliz, F. A.; Steinmetz, N. F.; Fiering, S. N. Treatment of Canine Oral Melanoma with Nanotechnology-Based Immunotherapy and Radiation. 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Claims

WHAT IS CLAIMED IS:

1. A composition comprising an isolated Secoviridae plant virus B and / or M component, wherein the B and / or M components of the Secoviridae plant virus are the same or different, the composition optionally comprising a carrier, wherein the carrier is optionally a pharmaceutically acceptable carrier.

2. The composition of claim 1 wherein the B and / or M component is the Secoviridae plant viral capsid containing an RNA polynucleotide, which can further comprise the naturally occurring RNA or any other RNA such as an RNA vaccine or anti-cancer therapy.

3. The composition of claim 1 or 2, wherein the isolated B and / or the M Secoviridae plant virus component is the only viral or virally derived component in the composition.

4. The composition of any one of claims 1-3, wherein the isolated B and / or M Secoviridae plant virus component is the only anti-cancer agent in the composition.

5. An anti-cancer composition consisting essentially of an isolated Secoviridae plant virus B and / or M component and viral capsid containing an RNA polynucleotide and optionally wherein the component is the B and / or M viral capsid which can further comprise the naturally occurring RNA or any other RNA such as an RNA vaccine or anti-cancer therapy.

6. An anti-cancer composition consisting essentially composition comprising an isolated Secoviridae plant virus B component and / or M component, and optionally wherein the B component is the B viral capsid which can further comprise the naturally occurring RNA or any other RNA such as a RNA vaccine or anti-cancer therapy, further optionally wherein the M component is the M viral capsid which can further comprise the naturally occurring RNA or any other RNA such as a RNA vaccine or anti-cancer therapy.

7. The composition of any of claims 1-6, wherein the isolated Secoviridae is / are not inactivated.

8. The composition of any of claims 1-7, wherein the isolated Secoviridae B component comprises RNA-1 and / or the M component comprises RNA-2.

9. An anticancer composition for use in treating a cancer or inducing an immune response, comprising the composition of any of claims 1-8.

10. The composition of any of claims 1-9, wherein the isolated Secoviridae plant virus is an isolated virus from the Comovirus, Fabavirus, Nepovirus, Cheravirus, Sadwavirus, Sequivirus, Stralarivirus, Torradovirus, or Waikavirus genera.

11. The composition of claim 10, wherein the isolated Secoviridae is an isolated Cowpea mosaic virus (CPMV).

12. The composition of any of claims 1-11, wherein the B component comprises an RNA polynucleotide according to SEQ ID NO: 3 and / or the M component comprises an RNA polynucleotide according to SEQ ID NO:

10.

13. The composition of any of claims 1-11, wherein the isolated Secoviridae is CPMV, wherein the B component comprises: a) an RNA polynucleotide encoding a protease cofactor, a helicase, a viral genome- linked protein (VpG), a protease, and a polymerase, wherein the protease cofactor has a sequence according to SEQ ID NO: 5, wherein the helicase has a sequence according to SEQ ID NO: 6, wherein the viral genome linked protein (VPg) has a sequence according to SEQ ID NO: 7, wherein the protease has a sequence according to SEQ ID NO: 8, and wherein the polymerase has a sequence according to SEQ ID NO: 9; b) a VPg peptide has a sequence according to SEQ ID NO: 4; and c) a PolyA tail.

14. The composition of any of claims 1-11, wherein the isolated Secoviridae is CPMV, wherein the M component comprises: a) an RNA polynucleotide encoding a movement protein, a large coat protein, and a small coat protein, wherein the movement protein has a sequence according to SEQ ID NO: 11, wherein the large coat protein has a sequence according to SEQ ID NO: 12, and wherein the small coat protein has a sequence according to SEQ ID NO: 13; b) a VPg peptide has a sequence according to SEQ ID NO: 4; and c) a PolyA tail.

15. The composition of any of claims 1-3 or 4-14, further comprising an additional anti- cancer agent.

16. A method for inducing an immune response in a subject in need thereof comprising administering to the subject the composition of any of claims 1-15, thereby inducing or inhibiting one or more of the following in a subject in in need thereof: activation of innate immune cells to induce secretion of pro-inflammatory cytokines, optionally IFNα, IFNγ, IL-6 and IL-12, or the inhibiting the secretion of innate immune cells to induce secretion of immunosuppressive cytokines, optionally TGFβ and IL-10.

17. A method to inhibit the growth of a cancer cell comprising contacting the cell with a composition of any of claims 1-15, optionally wherein the contacting is in vitro or in vivo, optionally wherein the cancer cell is selected from the group of melanoma, breast cancer, prostate cancer, lung cancer, ovarian cancer, skin cancer, bladder cancer, pancreatic cancer, gastric cancer, esophageal cancer, colon cancer, head and neck cancer, brain cancer, glioma, cervical cancer, hepatocellular cancer, inflammatory mammary cancer or thyroid cancer, that is optionally a primary or a metastatic cancer, and optionally wherein the cancer cell is a mammalian cell.

18. A method for treating cancer in a subject in need thereof comprising administering to the subject the composition of any of claims 1-15, thereby treating the cancer, wherein the subject is a mammal or a human, wherein the cancer is selected from the group of melanoma, breast cancer, prostate cancer, lung cancer, ovarian cancer, skin cancer, bladder cancer, pancreatic cancer, gastric cancer, esophageal cancer, colon cancer, head and neck cancer, brain cancer, glioma, cervical cancer, hepatocellular cancer, inflammatory mammary cancer, or thyroid cancer, optionally wherein the treatment comprises one or more of: inhibiting metastatic potential of the cancer; reduction in tumor size; a reduction in tumor burden, longer progression free survival and longer overall survival of the subject, optionally wherein the administering comprises intravenous, subcutaneous, intratumoral, or intraperitoneal delivery, and optionally wherein a different cancer therapy or tumor resection is additionally administered.

19. The method of claim 16, wherein the cancer is a metastatic cancer or a primary colon cancer or a primary or a metastatic melanoma.

20. A kit comprising one or more of the composition or combination of any of claims 1- 15 and optional instructions for use.

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