VIRUS-LIKE PARTICLES, HETERODIMERIC CAPSID PROTEINS AND METHODS OF PRODUCTION THEREOF Field of the Invention The present invention relates to virus-like particles (VLPs) comprising heterodimeric subunits in which one monomer comprises a single high affinity protein attachment system which allows interchangeable decoration with any functional molecule of choice, wherein the heterodimeric subunits are created by modification of the electrostatic interaction between the monomers forming each heterodimer. The present invention further relates to processes of producing the VLPs, including a rapid single cell process, and uses of the VLPs in research, diagnosis and as vaccines for use in prevention/treatment of diseases. Introduction Virus-like particles (VLPs) are molecules that closely resemble viruses, but contain no viral genetic material. They are formed from viral structural proteins, such as viral capsid proteins that, when individually expressed, self-assemble into a particle. Most Virus-like particles appear as hollow ‘nano-footballs’ where the entire surface of the football is made up by many copies of a single self-assembled protein. For production purposes this means that production of one single protein is sufficient to generate the entire nano-football type VLP structure. This has been exploited in medicine. The most common use of VLPs are as vaccines. Mammals have evolved immune sensing mechanisms to recognise highly repetitive patterns seen on viral capsids as intruders. These patterns are still present in VLPs, which contain repetitive, high density displays of viral surface proteins. Therefore the VLP can generate an immune reaction but the viral genome is typically removed. This is the form of the VLP used in the widespread vaccine against human papillomavirus (HPV) which causes cervical cancer. There are currently a selection of commercially available HPV vaccines of this type such as Cervarix by GlaxoSmithKline along with Gardasil and Gardasil-9, produced by Merck & Co. Further developments of VLPs for use as vaccines involve tethering of other agents to the VLP shell. In this case, the VLP shell serves to present an additional agent as an ‘epitope’ to the immune system and thereby stimulate an immune reaction. In some cases, the viral capsid proteins forming the VLP shell can be modified to directly incorporate the epitope for display through genetic fusion. Current COVID19 vaccines that are under development use this form of VLP, where the spike protein from the coronavirus is directly fused to a viral capsid protein forming a VLP shell from an unrelated virus. However, this approach commonly leads to impaired VLP assembly and large proteins routinely cause VLP instability. Furthermore, this approach cannot be used if the agent is not protein-based. A further alternative is to assemble the VLP and then use attachment means to secure the agent to the VLP shell. Such VLPs with additional attachment means may be termed ‘compound VLPs’. Compound VLPs may be manufactured by methods such as chemical crosslinking, reactive unnatural amino acids, or the use of binding proteins such as the SpyTag/SpyCatcher system, to covalently attach the desired agent or epitope to the viral capsid proteins forming the VLP. The latter method allows the attachment of other non-protein epitopes to the VLP, but requires a complicated production process and cannot yet be used commercially for any agent. Some desired proteins are simply too large to attach to the VLP using current attachment means, and some complex epitopes include multimers with numerous components that must be separately linked together, which must be achieved by additional chemical crosslinking. The current binding proteins which are used as attachment means, such as in the SpyTag/SpyCatcher system, have further issues in that the binding between the proteins whilst being strong, does not occur instantly but requires time for the reactants to fuse, and can result in VLP aggregation depending on which agent or epitope is attached to the VLP. Further complexities arise in the production of VLPs used in clinical human or veterinary applications, which regulators classify VLPs as “biological” active drug intermediates (ADI’s). “Biologic” drugs are produced in living cells, followed by purification according to a regulator – approved process. Each cell line (regardless whether bacterial, plant, yeast, insect or mammalian) used for the production process is carefully characterized so as to guarantee long-term stability of the ADI and stored under highly specified conditions as a “Master Cell Bank” (MCB). If a VLP requires two (or even more) proteins to be assembled, for example where binding proteins are used to attach an epitope to the VLP shell, then currently one MCB is required for each protein component of the drug, and both require a separate purification process, each requiring separate characterisation procedures. In addition a separate quality- control release is required for each critical drug intermediate and the final ADI, multiplying manufacturing costs. Further to these regulatory complexities, the production of the agent/epitope must be established from scratch for each agent/epitope. The most efficient type of production cell is bacteria (specifically: E.coli). However, many proteins do not assume their native shape when produced in E.coli but must be re-folded into their proper form from a denatured state as part of the purification process, which results in huge drop of overall yield and significantly adds to the complexity of the production process As a result of these difficulties, the production process of compound VLP-type drugs which attempt to attach agents such as epitopes to the viral capsid proteins is complex and expensive. This has limited the wide-spread exploration of compound VLP applications to fields where inexpensive mass production could make them more competitive. A technology which simplifies the process of making compound VLPs has recently been described which uses the Hepatitis B virus capsid, HBc. In essence, this technology is based on a pair of binding proteins positioned on the surface tip of each monomer forming each homodimer of the VLP, as shown in Figure 2B herein. These binding proteins can in turn act as a docking point to allow other ‘epitope’ proteins to be positioned on the outside of the VLP. However, it is possible that the effectiveness of vaccines made with this technology may be impacted by “crowding” of too many ‘epitope’ proteins being presented on the surface of the VLP depending on the size and shape of the protein being presented. Another potential limitation, as with all HBc VLP vaccines may be that industrial scale manufacture, stability, and storage could be temperature-dependent, posing practical limitations. It is the aim of the present invention to provide a VLP for use as a vaccine that overcomes the problem of “crowding” of proteins presented on the surface by using heterodimeric capsid subunits which are still able to self-assemble but present a single ‘epitope’ protein for each of the dimeric subunits forming the VLP. In addition, the present invention aims to provide a VLP that has improved stability when manufactured at industrial scale. While other technologies, including mRNA, can generate “conventional” vaccines against infectious diseases, vaccines against self-proteins, such as, for example vaccines to treat asthma or dermatitis, cannot be delivered by mRNA platforms. This is because mRNA translated to self-proteins is not loaded onto the surface of presenting cells (follicular dendritic cells) as a whole intact folded protein, and thus is not able to trigger activation of B-cells. As a result, mRNA vaccines do not generate an antibody response against self-proteins. Therefore, there is a general need for improved vaccine development in the areas of chronic inflammatory diseases, animal health, cancer, dementia, and animal health. One or more aspects of the present invention are aimed at solving one or more of the above- mentioned problems. Statements of Invention According to a first aspect of the present invention, there is provided a virus-like particle (VLP) comprising: - One or more viral capsid protein heterodimer(s) each comprising a first monomer encoded by a first amino acid sequence and a second monomer encoded by a second amino acid sequence, and; - a binding molecule attached exclusively to either the first monomer or the second monomer, and; - wherein the first amino acid sequence and/or the second amino acid sequence comprises at least one mutation which modifies the electrostatic interaction between the first and second monomers to promote association thereof. In one embodiment, the first amino acid sequence and the second amino acid sequence both comprise at least one mutation which modifies the electrostatic interaction between the first and second monomers to promote association thereof. In one embodiment, the at least one mutation of the first amino acid sequence is different to the at least one mutation of the second amino acid sequence. In one embodiment, the binding molecule is operable to be attached to a functional molecule. In some embodiments, the binding molecule is a binding protein. In some embodiments, the binding protein comprises a bacterial toxin inhibitor. In some embodiments, the bacterial toxin inhibitor is selected from Im7, Im8, Im9, Im2, and Barstar. In one embodiment, one of the first or the second amino acid sequences comprises the sequence as set out in SEQ ID NO: 2 or 3. In one embodiment, one of the first or the second amino acid sequences comprises the sequence as set out in SEQ ID NO: 4 or 5. In one embodiment, the first amino acid sequence comprises the sequence as set out in SEQ ID NO:2 and the second amino acid sequence comprises the sequence as set out in SEQ ID NO:4. In one embodiment, the first amino acid sequence comprises the sequence as set out in SEQ ID NO:3 and the second amino acid sequence comprises the sequence as set out in SEQ ID NO:5. In one embodiment, the first amino acid sequence comprises a mutation corresponding to E8K of SEQ ID NO: 1 or 16, and the second amino acid sequence comprises a mutation corresponding to R56D of SEQ ID NO: 1 or 16. In one embodiment, the first amino acid sequence comprises a mutation corresponding to E64K of SEQ ID NO: 1 or 16, and the second amino acid sequence comprises a mutation corresponding to K96D of SEQ ID NO: 1 or 16. In one embodiment, the first amino acid or the second amino acid sequence further comprises a mutation corresponding to K67E; R82D and/or E97K of SEQ ID NO: 16. In one embodiment, the first amino acid sequence further comprises a mutation corresponding to K67E; R82D and/or E97K of SEQ ID NO: 16. Suitably in such an embodiment, the viral capsid protein heterodimer is a woodchuck hepatitis viral capsid protein heterodimer. In any embodiment herein E97K may be replaced with E79K. In one embodiment, the first amino acid sequence comprises a further mutation corresponding to H88K of SEQ ID NO: 16, and the second amino acid sequence comprises a further mutation corresponding to W71D of SEQ ID NO: 16. Suitably in such an embodiment, the viral capsid protein heterodimer is a woodchuck hepatitis viral capsid protein heterodimer. In one embodiment, the second amino acid sequence further comprises a deletion of a serine residue at a position corresponding to residue 78 of SEQ ID NO:16. Suitably in such an embodiment, the viral capsid protein heterodimer is a woodchuck hepatitis viral capsid protein heterodimer. In one embodiment, the binding molecule is attached to the second amino acid sequence. In some embodiments, the viral capsid protein is from any virus having a dimeric capsid protein. In one embodiment, the viral capsid protein is a hepatitis capsid protein. In one embodiment, the viral hepatitis capsid protein is a Woodchuck hepatitis capsid protein. According to a second aspect of the present invention, there is provided a viral capsid protein heterodimer comprising: - a first monomer encoded by a first amino acid sequence and a second monomer encoded by a second amino acid sequence; - a binding molecule attached exclusively to either the first monomer or the second monomer, and; - wherein the first amino acid sequence and/or the second amino acid sequence comprises at least one mutation which modifies the electrostatic interaction between the first and second monomers to promote association thereof. In one embodiment of the second aspect, the first amino acid sequence comprises a least one mutation and the second amino acid sequence comprises at least one mutation. In one embodiment the at least one mutation of the first amino acid sequence is different to the at least one mutation of the second amino acid sequence. According to a third aspect of the present invention, there is provided a viral capsid protein monomer encoded by an amino acid sequence - wherein the amino acid sequence comprises at least one mutation and, - the at least one mutation modifies the electrostatic interaction between the viral capsid protein monomer and other viral capsid protein monomers to promote heterodimeric association thereof, - wherein optionally the viral capsid protein monomer comprises a binding molecule attached thereto. According to a fourth aspect of the present invention, there is provided a first or second viral capsid protein monomer encoded by: - a first amino acid sequence comprising at least one mutation, or - a second amino acid sequence comprising at least one mutation respectively; - wherein the at least one mutation in the first and second amino acid sequences are different, and - wherein the mutations in the first or second amino acid sequences promote association of the first monomer comprising the first amino acid sequence with the second monomer comprising the second amino acid sequence, - wherein optionally one of the first or second monomers exclusively comprises a binding molecule attached thereto. According to a fifth aspect of the present invention, there is provided a nucleic acid encoding the viral capsid protein heterodimer according to the second aspect or a viral capsid protein monomer according to the third or fourth aspect of the invention. According to a sixth aspect of the present invention, there is provided a nucleic acid construct encoding the viral capsid protein heterodimer according to the second aspect, the construct comprising: - a first nucleic acid sequence encoding a first viral capsid protein monomer according to the third or fourth aspect; - a second nucleic acid sequence encoding a second viral capsid protein monomer attached to a binding molecule according to the third or fourth aspect. According to a seventh aspect of the present invention, there is provided a vector comprising one or more of the nucleic acids according to the fifth aspect or the construct according to the sixth aspect of the invention. According to an eighth aspect of the present invention, there is provided a host cell comprising one or more of the nucleic acids according to the fifth aspect, the construct according to the sixth aspect, or the vector according to the seventh aspect. According to a ninth aspect of the present invention, there is provided a process of producing a virus-like particle (VLP) in a single host cell comprising: a) Providing a host cell comprising i. a first nucleic acid encoding a first viral capsid protein monomer according to the third or fourth aspects, ii. a second nucleic acid encoding a second viral capsid protein monomer attached to a binding molecule according to the third or fourth aspects, iii. a third nucleic acid encoding a functional molecule operable to bind to the binding molecule; b) Culturing the host cell under conditions to express the proteins from the nucleic acids; c) Forming functionalised viral capsid protein heterodimers; d) Forming virus-like particles from the functionalised viral capsid protein heterodimers. In some embodiments of the ninth aspect of the invention, the nucleic acids are comprised on one or more vectors. In one embodiment, the first, second and third nucleic acids are comprised on one vector, suitably a vector according to the seventh aspect. According to a tenth aspect of the present invention, there is provided a process of producing a virus-like particle (VLP), comprising; (a) Providing a first host cell comprising: (i) a first nucleic acid encoding a first viral capsid protein monomer according to the third or fourth aspects, (ii) a second nucleic acid encoding a second viral capsid protein monomer attached to a binding molecule according to the third or fourth aspects, (b) Providing a second host cell comprising: (i) a third nucleic acid encoding a functional molecule operable to bind to the binding molecule; (c) Culturing the first and second host cells under conditions to express the proteins from the first, second, and third nucleic acids respectively; (d) Recovering the proteins; (e) Mixing the proteins to (i) form functionalised viral capsid protein heterodimers and (ii) form virus-like particles from the functionalised viral capsid protein heterodimers. In some embodiments of the tenth aspect of the invention, the first nucleic acid encoding the first viral capsid protein monomer and the second nucleic acid encoding a second viral capsid protein monomer attached to a binding molecule are comprised on a first vector. In one embodiment, the third nucleic acid is comprised on a second vector. In some embodiments of any of the above aspects, the or each viral capsid protein monomer is from any virus having a dimeric capsid protein. In one embodiment, the or each viral capsid protein monomer is a hepatitis capsid protein monomer. In one embodiment, the or each viral hepatitis capsid protein monomer is a Woodchuck hepatitis capsid protein monomer. According to an eleventh aspect of the present invention, there is provided a cell culture comprising one or more host cells according to the eighth aspect of the invention. According to a twelfth aspect of the present invention, there is provided an immunogenic composition comprising the virus-like particle according to the first aspect. According to a thirteenth aspect of the present invention, there is provided a virus-like particle (VLP) according to the first aspect, an immunogenic composition according to the twelfth aspect of the invention for use as a medicament. According to a fourteenth aspect of the present invention, there is provided a virus-like particle (VLP) according to the first aspect, or an immunogenic composition according to the twelfth aspect for use in the prevention and/or treatment of infectious diseases, cardiovascular diseases, cancer, inflammatory diseases, autoimmune diseases, neurological disease, rheumatological degenerative disease, or addiction. According to a fifteenth aspect of the present invention, there is provided use of a virus-like particle (VLP) according to the first aspect of the invention in research, or in the diagnosis of a disease. According to a sixteenth aspect of the present invention, there is provided a method of diagnosing a disease in a subject comprising: (a) Providing a virus like particle according to the first aspect of the invention, wherein the binding molecule is attached to a functional molecule and, wherein the functional molecule is an antibody directed towards an antigen derived from a disease causing agent; (b) Mixing the virus like particle with a suitable sample from the subject; (c) Detecting whether the virus like particle precipitates; (d) Diagnosing the presence of a disease if the virus like particle precipitates. The present invention relates to VLPs comprising one or more viral capsid protein heterodimer(s). The Heterodimer(s) each comprise a first monomer encoded by a first amino acid sequence and a second monomer encoded by a second amino acid sequence. The first or the second monomer having a binding molecule attached, exclusively to the first or the second monomer. The first and/or second amino acid sequences comprise at least one mutation as compare to the wild-type sequence, such that, the mutation modifies the electrostatic interaction between the first and the second monomers as compared to wild-type sequences. This modification in the electrostatic interaction promotes the formation of a heterodimer comprising the first monomer and the second monomer, and a binding molecule attached exclusively to either the first or the second monomer of the capsid protein heterodimer. Many wild-type viral capsid proteins are made up of dimers formed from identical proteins, that is, the monomeric subunits of the homodimers are identical, such as hepatitis capsid proteins. These homodimers self-assemble to form VLPs. The inventors have found that even if one of the monomers of the dimer has a binding molecule attached, homodimers are still formed. This results in homodimers that have a binding molecule attached to each monomer, or a homodimer having no binding molecules attached. This does not solve the problems in the art discussed above in which crowding of functional molecules on the VLP surface inhibits VLP formation and activity. The inventors have now found that certain mutations in the amino acid sequences encoding the monomers can overcome the usual formation of homodimers and promote association of monomers wherein a binding molecule is attached to only one of the monomers, thus forming a heterodimer. The inventors have achieved this by making targeted mutations in each of the two monomers in order to influence the electrostatic attraction of the monomers, such that they instead preferentially form heterodimers. Each heterodimer having only one binding molecule attached exclusively to either the first monomer or the second monomer which may then be functionalised, allows for larger functional molecules to be attached to the VLP surface without steric hindrance. If the functional molecule is a relatively large molecule, more space per molecule is needed to avoid “crowding” of molecules presented on the surface of the VLP. According to any aspect of the present invention, the viral capsid protein may be a hepatitis B capsid protein (HBc). Suitably the viral capsid protein may be a human hepatitis B capsid protein. Alternatively, the viral capsid protein may be a Woodchuck hepatitis virus capsid protein (wHv). Suitably, use of wHv capsid protein confers particular advantages over that of human hepatitis capsid protein. For example, wHv can form capsids at cold temperatures (> 60% capsid formation occurs at temperatures as low as 4°C, Kukreja 2014). This can result in an increased yield of VLPs in low temperature and allows the use of bacterial fermentation at lower temperatures which is preferable for production of complex proteins. Features and embodiments of the above aspects are described further under headed sections below. Any feature or embodiment may be combined with any aspect in any workable combination. While the making and using of various embodiments of the present invention are discussed in detail below, it should be appreciated that the present invention provides many applicable inventive concepts that can be embodied in a wide variety of specific contexts. The specific embodiments discussed herein are merely illustrative of specific ways to make and use the invention and do not delimit the scope of the invention. To facilitate the understanding of this invention, a number of terms are defined below. Terms defined herein have meanings as commonly understood by a person of ordinary skill in the areas relevant to the present invention. Terms such as "a", "an" and "the" are not intended to refer to only a singular entity, but include the general class of which a specific example may be used for illustration. The terminology herein is used to describe specific embodiments of the invention, but their usage does not delimit the invention, except as outlined in the claims. The discussion of the background to the invention herein is included to explain the context of the invention. This is not to be taken as an admission that any of the material referred to was published, known, or part of the common general knowledge in any country as of the priority date of any of the claims. The present invention will employ, unless otherwise indicated, conventional techniques of cell biology, cell culture, molecular biology, transgenic biology, microbiology, recombinant DNA, and immunology, which are within the skill of the art. Such techniques are explained fully in the literature. See, for example, Current Protocols in Molecular Biology (Ausubel, 2000, Wiley and son Inc, Library of Congress, USA); Molecular Cloning: A Laboratory Manual, Third Edition, (Sambrook et al, 2001, Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press); Oligonucleotide Synthesis (M. J. Gait ed., 1984); U.S. Pat. No.4,683,195; Nucleic Acid Hybridization (Harries and Higgins eds. 1984); Transcription and Translation (Hames and Higgins eds.1984); Culture of Animal Cells (Freshney, Alan R. Liss, Inc., 1987); Immobilized Cells and Enzymes (IRL Press, 1986); Perbal, A Practical Guide to Molecular Cloning (1984); the series, Methods in Enzymology (Abelson and Simon, eds. -in-chief, Academic Press, Inc., New York), specifically, Vols.154 and 155 (Wu et al. eds.) and Vol.185, "Gene Expression Technology" (Goeddel, ed.); Gene Transfer Vectors For Mammalian Cells (Miller and Calos eds., 1987, Cold Spring Harbor Laboratory); Immunochemical Methods in Cell and Molecular Biology (Mayer and Walker, eds., Academic Press, London, 1987); Handbook of Experimental Immunology, Vols. I-IV (Weir and Blackwell, eds., 1986); and Manipulating the Mouse Embryo, (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1986). The terms "identity" and "identical" and the like refer to the sequence similarity between two polymeric molecules, e.g., between two nucleic acid molecules, such as between two DNA molecules, or between two protein molecules. Sequence alignments and determination of sequence identity can be done, e.g., using the Basic Local Alignment Search Tool (BLAST) originally described by Altschul et al. 1990 (J Mol Biol 215: 403-10), such as the "Blast 2 sequences" algorithm described by Tatusova and Madden 1999 (FEMS Microbiol Lett 174: 247-250). Methods for aligning sequences for comparison are well-known in the art. Various programs and alignment algorithms are described in, for example: Smith and Waterman (1981) Adv. Appl. Math.2:482; Needleman and Wunsch (1970) J. Mol. Biol.48:443; Pearson and Lipman (1988) Proc. Natl. Acad. Sci. U.S.A. 85:2444; Higgins and Sharp (1988) Gene 73:237-44; Higgins and Sharp (1989) CABIOS 5:151-3; Corpet et al. (1988) Nucleic Acids Res.16:10881- 90; Huang et al. (1992) Comp. Appl. Biosci. 8:155-65; Pearson et al. (1994) Methods Mol. Biol. 24:307-31; Tatiana et al. (1999) FEMS Microbiol. Lett. 174:247-50. A detailed consideration of sequence alignment methods and homology calculations can be found in, e.g., Altschul et al. (1990) J. Mol. Biol.215:403-10. The National Center for Biotechnology Information (NCBI) Basic Local Alignment Search Tool (BLAST™; Altschul et al. (1990)) is available from several sources, including the National Center for Biotechnology Information (Bethesda, MD), and on the internet, for use in connection with several sequence analysis programs. A description of how to determine sequence identity using this program is available on the internet under the "help" section for BLAST™. For comparisons of nucleic acid sequences, the "Blast 2 sequences" function of the BLAST™ (Blastn) program may be employed using the default parameters. Nucleic acid sequences with even greater similarity to the reference sequences will show increasing percentage identity when assessed by this method. Typically, the percentage sequence identity is calculated over the entire length of the sequence. For example, a global optimal alignment is suitably found by the Needleman-Wunsch algorithm with the following scoring parameters: Match score: +2, Mismatch score: -3; Gap penalties: gap open 5, gap extension 2. The percentage identity of the resulting optimal global alignment is suitably calculated by the ratio of the number of aligned bases to the total length of the alignment, where the alignment length includes both matches and mismatches, multiplied by 100. The term “vector” is well known in the art, and as used herein refers to a nucleic acid molecule, e.g. double-stranded DNA, which may have inserted into it a nucleic acid sequence according to the present invention. A vector is suitably used to transport an inserted nucleic acid molecule into a suitable host cell. A vector typically contains all of the necessary elements that permit transcribing the insert nucleic acid molecule, and, preferably, translating the transcript into a polypeptide. A vector typically contains all of the necessary elements such that, once the vector is in a host cell, the vector can replicate independently of, or coincidental with, the host chromosomal DNA; several copies of the vector and its inserted nucleic acid molecule may be generated. The term “operably linked”, “operably connected” or equivalent expressions as used herein refer to the arrangement of various nucleic acid elements relative to each other such that the elements are functionally connected and are able to interact with each other in the manner intended. The terms “therapy” “therapeutic” “treatment” or “treating” refer to reducing, ameliorating or eliminating one or more signs, symptoms, or effects of a disease or condition. "Treatment," or “therapy” as used herein thus includes any treatment of a disease in a mammal, particularly in a human, and includes: (a) preventing the disease from occurring in a subject predisposed to the disease or at risk of acquiring the disease but has not yet been diagnosed as having it; (b) inhibiting the disease, i.e., arresting its development; and (c) relieving the disease, i.e., causing regression of the disease. The “administration” of an agent to a subject includes any route of introducing or delivering to a subject the agent to perform its intended function. Administration can be carried out by any suitable route, including orally, intranasally, intraocularly, ophthalmically, parenterally (intravascularly, intramuscularly, intraperitoneally, or subcutaneously), or topically. Administration includes self-administration and the administration by another. The terms “individual,” “subject,” and “patient” are used interchangeably, and refer to any individual subject with a disease or condition in need of therapy, suitably in need of therapy by treatment with the present invention. For the purposes of the present disclosure, the subject may be a human or animal, for example primate, preferably a human, or another mammal, such as a dog, cat, horse, pig, goat, or bovine, and the like. Figures The invention may be described with reference to the following figures in which: Figure 1 shows: a cartoon diagram representing a VLP capsid and subunits. On the top left, the overall structure of the Woodchuck hepatitis virus (wHv) capsid. On the top right: close up (side view and ‘top’ view, respectively) of one so-called “asymmetric unit” composed of two homodimers which in turn are formed each by joining together of one single capsid protein. At the bottom of the figure, a ribbon diagram of one single “homodimer” composed of two identical monomer protein subunits is shown (side view and ‘top’ view, respectively). In this way, the entire capsid is formed from ordered assembly of a single protein where the central building block is a homodimer. For clarity, the single wHv capsid protein is shown without the C- terminal domain which conveys binding to RNA in the wild type virus. Only the N-terminal portion, truncated after aa149, is required for the formation of the capsid. Therefore, “wHv” designation of the capsid protein in the following figure legends, and elsewhere herein, refers to this truncated protein, also designated herein as “wHv149”. Figure 2 shows: a cartoon representation of the present invention. From top to bottom (A) shows a wild type homodimeric capsid subunit (as in Figure 1, but here shown as space-filling model), (B) shows a prior art homodimeric capsid subunit which has been modified to allow two functional molecules (dark grey, on top, facing the surface of the capsid) to be presented by each dimeric subunit on the VLP surface. (C) shows the heterodimeric subunit of the present invention, which allows only one single functional molecule (dark grey, on top, facing the surface of the capsid) to be presented by each heterodimeric subunit on the surface of the VLP. This allows the production of VLP vaccines where only one protein is presented for each of the dimeric capsid subunits. Figure 3 shows: a diagrammatic representation of an approach to creating a mutant wHv capsid where one dimer displays a binding protein such as an integrated Im7 protein toward the VLP surface. Panel A shows an expression vector that allows simultaneous expression of a wild type wHv protein (ORF2) and a wHv protein carrying the binding protein (an integrated Im7 protein, ORF1), driven by an independent second promoter or through an internal ribosome binding site (RBS). This construct can result in either formation of homodimers (ORF2 + ORF2, as shown, or ORF1 + ORF1, which is not illustrated here) or heterodimers (ORF1 + ORF2). Panel B shows a close up of the central ‘tip’ of the wHv dimer (dashed boxed in Panel A). Highlighted are negatively charged (E64) and positively charged (K96) amino acids, respectively, which create electrostatic attraction, contributing to dimer formation of two subunits. Figure 4 shows: a preliminary approach to create asymmetrical interaction between two wHv monomers in order to favour formation of heterodimers over homodimer formation. Panel A shows a schematic of an exemplary expression vector. Complementary mutations are introduced into the two different monomers: K96E in wHv-Im7 and E64K into wHv, respectively. Below shown is a schematic showing how exemplary complementary mutations generate local electrostatic repulsion whenever two wHv monomers interact, while creating electrostatic attraction whenever a wHv and a modified-wHv monomer interact. In this example, the modified-wHv is modified with an integrated Im7 protein. Panel B shows structural prediction using Alphafold2 database (Jumper, J et al. (2021) and Varadi, M et al. (2021), showing that formation of homodimers composed of wHv/wHv and wHv-Im7/wHv-Im7, respectively, is still favoured despite the mutations introduced (shown is the top-ranked of five models, all of which show homodimer formation). Figure 5 shows: mutational refinement in the wHv monomers. In this example, lysine96 (K96) in wHv is replaced by aspartate (D96), instead of glutamate (E96), in contrast to the model shown in figure 4. Panel A shows a schematic of an exemplary expression vector showing that complementary mutations are introduced into the two different monomers: K96D in wHv- Im7 and E64K into wHv, respectively. The mutation of K96 to D96 reduces side-chain bulkiness, shown on the left of panel B. The resulting structural prediction using Alphafold2 database (right) shows a predicted mixture between heterodimer and homodimer formation. Figure 6 shows: Additional intra-chain ionic stabilization by added mutation of Lysine 67 (K67) to glutamate (E67) in the wHv149 subunit. Panel A shows a schematic of an exemplary expression vector showing that, in contrast to figure 5, an additional mutation is introduced into the wHv monomer (ORF2). In this example, an additional mutation K67E is introduced to the wHv149 subunit. This added mutation results in increased heterodimer formation since now E67 interacts with K64 and no longer with D63 within the same protein chain. This, in turn stabilizes the interaction of K64 with D96 of the heterodimeric partner monomer (ORF1). Nonetheless, still a mix of hetero- and homodimer structures is predicted by Alphafold2 (shown in panel B). This figure shows that exclusive formation of heterodimers is difficult to achieve. Figure 7 shows: a ribbon diagram of the top rated (by Alphafold2 database) heterodimeric capsid subunit structures obtained with the optimized engineered combination of mutations (wHv149: E8K, E64K, K67E, R82D, E79K, H88K; wHv149-Im7/Bs: R56D, K96D, W71D, summarized in table 2 of the examples), generated using Alphafold2 software, for heterodimers consisting of wHv149/wHv-Im7 (top) and wHv149/wHv-Bs (bottom). Figure 8 shows: an overlay of ribbon-diagram structures of wild type wHv with the combination of mutants listed in table 2, generated using the icn3d web-app (NCBI/structure; PDB: 6edj) and Alphafold2 database, respectively. Left: the wHv149 subunit, right: the wHv- Im7 subunit. The Im7-domain on top of the tip of wHv-Im7 is not shown, as it does not align with wild type wHv. The figure illustrates that the enacted mutations to not impact on the backbone structure of the mutated monomer proteins. Figure 9 shows: Space filling model generated using icn3d (NCBI/structure; PDB: 6edj), showing the wild type wHv (left) and the modified wHv149/wHv-Im7 (centre) and wHv149/wHv-Barstar (right) heterodimers, respectively, from the front (top) and from the surface (bottom) of the capsid. The dashed line (top) indicates the plane of subunit interaction leading to VLP assembly, which remains undisturbed by the integration of binding proteins (Im7 or Barstar). The bottom illustration shows that, compared to the wild type (left) the space occupancy of the heterodimers remains essentially unchanged. Figure 10 shows: (A) view from the side showing “spike” made from two helices from each monomer protruding to the outside (top arrow) and bottom part mediating interaction with other dimers in the capsid (bottom arrow). Panel (B) shows the wild-type amino acid sequences of both the Woodchuck (wild type wHv )(SEQ ID NO: 16) and Human hepatitis B capsid protein (SEQ ID NO: 1) monomers (subunit). The bold residues show differences in the amino acid sequences between Woodchuck and Human hepatitis capsid protein monomers and the highlighted amino acids relate to amino acids capable of forming inter-molecular electrostatic bonds. Figure 11 shows: the electrostatic interactions occurring between to wild type monomers forming a homodimer in the human hepatitis B virus capsid. Left: a ribbon diagram of the homodimer where dark circles and light circles highlight the position of electrostatic interactions between subunits in the ‘tip’ (dark) and in the ‘base’ (light) of the homodimer, respectively. Right: the encircled regions from the left side of the panel are shown at close up (‘tip’ region: top; ‘base’ region’: bottom) in a side-view, and 90 degrees rotated, respectively. The diagram shows that in the wild type HBc dimer E64 of each monomer interacts with K96 of the other monomer (top) and that E8 of each monomer interacts with R56 of the other monomer (bottom). The figure shows that complementary mutations in the human HBc virus capsid can be enacted analogous to the mutations illustrated for the wHv capsid in order to drive assembly of heterodimers, when one of the monomers has been altered, for example by in-frame fusion of Im7 or Bs (or any other change only implemented in one of the monomers). Figure 12 shows: panel A shows a diagram of an exemplary plasmid to produce the monomeric subunits of the VLP capsid. wHv capsid heterodimer components are soluble and evenly expressed in E.coli. Panel B shows SDS-PAGE gel of showing that both wHv_Im7 and wHv proteins, when driven by individual T7 promoters, can be expressed as soluble proteins in E.coli and are synthesized at approximately even stoichiometric ratios ( black arrows). Figure 13 shows: purification of a human Hepatitis B capsid dimer linked to a binding protein via IMAC. Left lane is the soluble cytosolic fraction of E.coli lysates where expression of the three proteins HBc-Im7 (white arrow), HBc-wt (dark grey arrow), ColE7-IL31 (light grey arrow) had been induced. This was applied to a Ni-NTA column. Lanes 2 and 3 show the flow-through and wash fraction (washed with 40mM imidazole, respectively). Lane 4 shows the fraction eluted with 200 mM imidazole. The relative band density between ColE7-IL31 and HBc-Im7 is approximately even, in keeping with a stoichiometric ratio of 1:1. The band of HBc-wt (light grey) is slightly weaker, owing to reduced molecular weight, but consistent with a 1:1 stoichiometric ratio between HBc-Im7 and HBc-wt. These data illustrate that all three proteins exist in complex and co-purify. Figure 14 shows: SDS PAGE analysis of a discontinuous density gradient run on a heterodimeric VLP decorated with a surface epitope protein (functional molecule). After 6h of 120,000g in the ultracentrifuge, all of the epitope, as well as the two heterodimeric VLP scaffold proteins partition to the 50% and 60% cushion, indicating high – density nanoparticle formation. Furthermore, the staining density of the epitope protein (white arrow) and the Im7- incorporating WHc protein (grey arrow) are approximately even. This indicates that most or all of the WHcIm7 moieties are loaded with epitope protein. Figure 15 shows: SDS PAGE analysis of heterodimeric WHcIm7/WHc VLPs decorated with an epitope protein. The middle lane shows a cytosolic fraction. The right lane shows the same preparation after purification via immobilized metal affinity chromatography (IMAC). The metal-binding tag is located on the epitope protein (white arrow). The data show that both the WHcIm7 (grey arrow) and the WHc protein (black arrow) co-purify, confirming that they are both bound to the epitope. The density of epitope and WHcIm7 is approximately even, indicating that the VLPs are fully decorated with epitope protein. Figure 16 shows: Dynamic Light Scatter (DLS) Analysis of the VLP particles analysed in Figure 15. The light scattering profile confirms uniform size distribution of particles at the expected size range (approximately 32 nm diameter). Figure 17 shows: Transmission Electron Microscopy (TEM) close-up of WHcIm7/WHc heterodimeric VLPs decorated with a surface epitope. Analysis done with 80 kV at 30,000x magnification. Scale bar 50 nm. The images confirm the size of VLPs determined by DLS analysis in Figure 16. The thickened rim structure and fuzzy outer rim appearance is consistent with decoration of an epitope localized to the surface. Description Viral Capsid Protein The present invention relates to VLPs which comprise one or more viral capsid proteins, the viral capsid proteins self-assemble into the VLP, to which functional molecules can then be attached through a binding molecule which may be a binding protein and/or chemical modification as discussed elsewhere herein. In accordance with any aspect, the viral capsid protein is from any virus having a dimeric capsid protein, suitably from any virus having a dimeric capsid protein formed from identical monomers. In one embodiment, the viral capsid protein is a hepatitis capsid protein, which may be selected from Hepatitis A, B, C or D. In one embodiment, the viral capsid protein is a Hepatitis B viral capsid protein (HBc). Suitably, the viral capsid protein is a mammalian Hepatitis viral capsid protein. Suitably, the viral capsid protein is a human Hepatitis B viral capsid protein. In a preferred embodiment, the viral capsid protein is a Woodchuck (Marmota monax) Hepatitis viral capsid protein (wHv). In one embodiment of any of the aspects, the viral capsid protein is a heterodimer, suitably therefore a heterodimeric viral capsid protein. Suitably, each heterodimeric viral capsid protein is made up of a first monomer and a second monomer. Suitably each heterodimeric viral capsid protein is attached to a binding molecule. Suitably therefore each heterodimeric viral capsid protein displays a binding molecule. Suitably each heterodimeric viral capsid protein is attached to a single binding molecule, suitably therefore one of the monomers of each heterodimeric capsid protein is attached to a binding molecule. Suitably the first or second monomer that forms the heterodimeric viral capsid protein is modified to display a binding molecule. Suitably the first or second monomer of the heterodimeric viral capsid protein is fused to binding molecule. Suitably the first or second monomer of the heterodimeric viral capsid protein is modified to display a binding molecule by fusing the binding molecule to the monomer of the heterodimeric viral capsid protein. Suitably the first or second monomer of the heterodimeric viral capsid protein is modified to display a binding molecule by inserting the amino acid sequence of the binding molecule into the amino acid sequence of the relevant monomer of the heterodimeric viral capsid protein. Suitably the amino acid sequence of the binding molecule is inserted into the major immunodominant region of the monomer of the heterodimeric viral capsid protein. Suitably the binding molecule is fused to the major immunodominant region of the monomer of the heterodimeric viral capsid protein. In an embodiment of the invention, the binding molecule is inserted between amino acids corresponding to residues 76 and 80 of the major immunodominant region of the monomer of the heterodimeric viral capsid protein. Suitably the binding molecule is inserted between amino acid residues corresponding to 77 and 79 of the major immunodominant region of the monomer of the heterodimeric viral capsid protein. Suitably the binding molecule is inserted between amino acid residues corresponding to 77 and 78 of the major immunodominant region of the monomer of the heterodimeric viral capsid protein. Suitably, the VLP of the invention comprises one or more linkers. Suitably the linkers join the amino acid sequence of the monomer in accordance with the third or fourth aspect with the binding molecule. Suitably, the linkers are located between the protein coding sequences of the monomer and the binding molecule. In one embodiment, the binding molecule is a binding protein and a linker is located at the N and C terminus of the binding protein, suitably to link to the heterodimeric viral capsid protein. Suitably a further linker may also be located between the functional molecule and the binding protein. Suitably the further linker may comprise an alpha helix. Suitably the further linker may comprise or consist of the sequence of LAEAAAKEAAAKEAAKAA (SEQ ID NO: 33). Suitably a further linker may also be located between the binding molecule and a further binding molecule. Suitably each linker is between 5 to 50 amino acids in length. Suitably each linker is 5, 10, 15, 20, 21, 25, 30, 35, 40 amino acids in length. Suitably each linker is 9, 10 or 11 amino acids in length. Suitably each linker comprises the sequence: GGGGSGGGGS (SEQ ID NO:9) or GGGGGSGGGGS (SEQ ID NO: 10), SGGGSSGSG (SEQ ID NO: 11), KAAAEKAAAE (SEQ ID NO: 14), GGKAAAE (SEQ ID NO:15) or LAEAAAKEAAAKEAAKAA (SEQ ID NO: 33). In one embodiment, the linkers used to link the amino acid sequence of the monomer in accordance with the third or fourth aspect with the binding molecule comprise either KAAAEKAAAE (SEQ ID NO: 14) or GGKAAAE (SEQ ID NO:15). Suitably, the first linker is KAAAEKAAAE (SEQ ID NO: 14) which links the N terminus of the binding protein to the heterodimeric viral capsid protein. Suitably the second linker is GGKAAAE (SEQ ID NO:15) which links the C terminus of the binding protein to the heterodimeric viral capsid protein. Suitably, as explained elsewhere herein, the binding molecule is a binding protein. Suitably, the viral capsid protein is a hepatitis B capsid protein and may comprise the amino acid sequence of SEQ ID NO: 2, suitably forming the first monomer. Suitably, the viral capsid protein is a hepatitis B capsid protein and may comprise the amino acid sequence of SEQ ID NO: 4, suitably forming the second monomer. In one embodiment, therefore, the heterodimeric viral capsid protein is a heterodimeric hepatitis B capsid protein and comprises the amino acid sequence of SEQ ID NO:2, and the amino acid sequence of SEQ ID NO:4. Suitably, the viral capsid protein is a woodchuck hepatitis capsid protein and may comprise a truncated viral capsid protein. Suitably one or both monomers of the woodchuck hepatitis capsid protein are truncated. Suitably both monomers of the woodchuck hepatitis capsid protein are truncated, suitably comprising a truncation of the C terminus. Suitably the C- terminus is removed from the or each monomer of the woodchuck hepatitis capsid protein. Suitably therefore the or each woodchuck hepatitis capsid protein monomer comprises amino acids 1 to 149 of the wild type woodchuck hepatitis capsid protein monomer sequence. Suitably references herein to woodchuck hepatitis capsid protein, wHv capsid protein, or wHv149 capsid protein are to the truncated form. Suitably such a truncated monomer sequence is shown in SEQ ID NO:16, and is additionally shown in SEQ ID NO:3 and 5 with the mutations described herein. Suitably, the viral capsid protein is a woodchuck hepatitis capsid protein and may comprise the amino acid sequence of SEQ ID NO: 3, suitably forming the first monomer. Optionally the sequence may comprise mutations at positions K67, R82, E97, and/or H88, which are described further herein. Suitably E97 may be replaced with E79. Suitably, the viral capsid protein is a woodchuck hepatitis capsid protein and may comprise the amino acid sequence of SEQ ID NO: 5, suitably forming the second monomer. Optionally the sequence may further comprise mutation at position W71 and/or a deletion at S78, which are described further herein. In one embodiment, therefore, the heterodimeric viral capsid protein is a heterodimeric woodchuck hepatitis capsid protein and comprises the amino acid sequence of SEQ ID NO:3, and the amino acid sequence of SEQ ID NO:5. Optionally wherein the SEQ ID NO:3 further comprises the additional mutations at positions K67, R82, E97, and/or H88, which are described further herein, and SEQ ID NO:5 further comprises the additional mutation at position W71 and/or a deletion at S78, which are described further herein. Suitably E97 may be replaced with E79. Modified Monomers and Heterodimers Suitably the first amino acid sequence encoding the first monomer and/or the second amino acid sequence encoding the second monomer comprises a mutation as compared to the wild- type sequence. Suitably, a mutation may be an insertion, deletion or substitution. Suitably the first amino acid sequence encoding the first monomer and the second amino acid sequence encoding the second monomer each comprise at least one mutation as compared to the wild-type sequence. Suitably, the or each mutation in the first amino acid sequence is different to the or each mutation in the second amino acid sequence. Suitably therefore the amino acid sequence of the first monomer is different to the amino acid sequence of the second monomer. Suitably, a mutation in the first amino acid sequence encoding the first monomer and/or the second amino acid sequence encoding the second monomer modifies the electrostatic interactions between the monomers as compared to the wild type sequences. Suitably the or each mutation modifies the electrostatic interaction between the monomers to promote association of the monomers to form heterodimers. Suitably the viral capsid protein may comprise further modifications. Suitable modifications may include: insertions, deletions, substituents, truncations, reversals, repeats, or the like in the amino acid sequence encoding the protein. Suitably the viral capsid protein may comprise further modifications in the major immunodominant region. Suitably such modifications aid the insertion of the binding molecule into the viral capsid protein. Suitably the viral capsid protein may comprise amino acid deletions. Suitably the viral capsid protein may comprise amino acid deletions in the major immunodominant region. Suitably the viral capsid protein may comprise amino acid deletions in the major immunodominant region which remove negatively charged amino acids. Suitably, the first amino acid sequence encoding the first monomer or the second amino acid sequence encoding the second monomer comprise at least one mutation. Suitably the first amino acid sequence encoding the first monomer and the second amino acid sequence encoding the second monomer each comprise at least one mutation. Suitably the at least one mutation of the first amino acid sequence is different to the at least one mutation of the second amino acid sequence. The person skilled in the art would understand that a mutation to an amino acid sequence can include insertions, deletions or substitutions. Suitably, the first and/or second amino acid sequences may include further modifications such as truncations, reversals, repeats, or the like. In a suitable embodiment, the first and/or second amino acid sequences include at least one mutation (for example, a substitution, addition, or deletion) as compared to the wild type sequence. Suitably, the first and/or second amino acid sequences include at least 2 mutations, at least 3 mutations, at least 4 mutations, at least 5 mutations, at least 6 mutations, at least 7 mutations, at least 8 mutations, at least 9 mutations, at least 10 mutations, at least 11 mutations, at least 12 mutations, at least 13 mutations, at least 14 mutations, at least 15 mutations, at least 16 mutations, at least 17 mutations, at least 18 mutations, at least 19 mutations, at least 20 mutations, at least 21 mutations, at least 22 mutations, at least 23 mutations, at least 24 mutations, at least 25 mutations, at least 26 mutations, at least 27 mutations, at least 28 mutations, at least 29 mutations or at least 30 mutations as compared to the wild type sequence. Suitably the or each mutation is present in the alpha helices of the first or second monomers. Suitably the or each mutation may be an amino acid substitution. Suitably the or each mutation may be an amino acid deletion. Suitably the amino acid substitution(s) modify the electrostatic interactions between the first and second monomers to promote association of the first and second monomers. Suitably, a substitution in the first and/or second amino acid sequence may be a substitution of a negatively charged amino acid with a positively charged amino acid. Suitably, a substitution in the first and/or second amino acid sequence may be a substitution of a positively charged amino acid with a negatively charged amino acid. Suitably a mutation in the first amino acid sequence may be complementary to a mutation of the second amino acid sequence. Suitably therefore the mutations in the first and second amino acid sequences may be regarded as pairs, suitably as complementary pairs. Suitably therefore the first and second amino acid sequences may comprise at least one pair of complementary mutations. Suitably, a pair of complementary mutations may comprise at least one positively charged amino acid and at least one negatively charged amino acid. Suitably the electrostatic interaction may be an electrostatic attraction or repulsion. In the context of the present invention, an electrostatic attraction is an interaction that occurs between molecules that have opposite partial charges. Suitably, these molecules do not form a covalent bond, but interact with each other if they are in close proximity to their opposite partial charge. In the case of an electrostatic attraction, the molecules are pulled together by the attraction between the opposite partial charges. Suitably, an electrostatic repulsion is an interaction that occurs between molecules that have the same partial charge. These molecules do not form a covalent bond but interact with each other if they are in close proximity to the same partial charge. In the case of electrostatic repulsion, the molecules are pushed away from each other by the repulsion of the same partial charge. Suitably, in the context of the present invention, the molecules described above relate to monomers of the present invention. Suitably a mutation of the first amino acid sequence may form an electrostatic interaction with a mutation in the second amino acid sequence. Alternatively, a mutation of the first amino acid sequence may form an electrostatic interaction with a non-mutated residue of the second amino acid sequence. Alternatively a mutation of the second amino acid sequence may form an electrostatic interaction with a non-mutated residue of the first amino acid sequence. Suitably an electrostatic interaction may be formed between a positively charged amino acid and a negatively charged amino acid. Suitably the electrostatic interaction may be an attraction. In a suitable embodiment, the first and second amino acid sequences may form an electrostatic attraction between a positively charged amino acid and a negatively charged amino acid. Suitably the positively charged amino acid is comprised on the first amino acid sequence and the negatively charged amino acid is comprised on the second amino acid sequence. Suitably, an electrostatic interaction may be a repulsion. Suitably, an electrostatic repulsion may be formed between two or more amino acids having a similar charge. Suitably, an electrostatic repulsion may be formed between two or more amino acids having a positive charge. Suitably, an electrostatic repulsion may be formed between two or more amino acids having a negative charge. In one embodiment, the heterodimer comprises a binding molecule attached to either the first or second monomer. Suitably, the heterodimer comprises a mutation in the first amino acid sequence encoding the first monomer and a different mutation in the second amino acid sequence encoding the second monomer and a binding molecule attached to either the first or second monomer. In one embodiment, the first amino acid sequence encoding the first monomer and/or the second amino acid sequence encoding the second monomer comprises an amino acid mutation at residue 8 of SEQ ID NO: 1 or 16, or a position corresponding thereto. Suitably, the mutation may be an amino acid substitution at residue 8 of SEQ ID NO: 1 or 16, or a position corresponding thereto. Suitably, the amino acid substitution may be from a glutamate to a lysine at residue 8 (E8K) of SEQ ID NO:1 or 16, or a position corresponding thereto. In another embodiment the first amino acid sequence encoding the first monomer or the second amino acid sequence encoding the second monomer comprises an amino acid mutation at residue 64 of SEQ ID NO: 1 or 16 or a position corresponding thereto. Suitably, the mutation may be an amino acid substitution at residue 64 of SEQ ID NO: 1 or 16 or a position corresponding thereto. Suitably, the amino acid substitution may be from a glutamate to a lysine at residue 64 (E64K) of SEQ ID NO: 1 or 16 or a position corresponding thereto. In another embodiment, the first amino acid sequence encoding the first monomer and/or the second amino acid sequence encoding the second monomer comprises an amino acid comprise an amino acid substitution from a glutamate to a lysine at residue 8 (E8K) and an amino acid substitution from a glutamate to a lysine at residue 64 (E64K) of SEQ ID NO:1 or 16, or positions corresponding thereto. Suitably, therefore the first or second monomer may be encoded by an amino acid sequence comprising a sequence set out in SEQ ID NO: 2 or SEQ ID NO: 3, or a sequence having at least 60 %, at least 70%, at least 80%, at least 90%, at least 95 %, at least 96%, at least 97%, at least 98%, at least 99% sequence identity thereto and comprising the mutations defined above. In one embodiment, the first amino acid sequence encoding the first monomer and/or the second amino acid sequence encoding the second monomer comprises an amino acid mutation at residue 56 of SEQ ID NO: 1 or 16 or a position corresponding thereto. Suitably, the mutation may be an amino acid substitution at residue 56 of SEQ ID NO: 1 or 16 or a position corresponding thereto. Suitably, the amino acid substitution may be from an arginine to an aspartate at residue 56 (R56D) of SEQ ID NO:1 or 16 or a position corresponding thereto. In another embodiment the first amino acid sequence encoding the first monomer and/or the second amino acid sequence encoding the second monomer comprises an amino acid mutation at residue 96 of SEQ ID NO: 1 or 16 or a position corresponding thereto. Suitably, the mutation may be an amino acid substitution at residue 96 of SEQ ID NO: 1 or 16 or a position corresponding thereto. Suitably, the amino acid substitution may be from a lysine to an aspartate at residue 96(K96D) of SEQ ID NO:1 or 16 or a position corresponding thereto. In another embodiment, the first amino acid sequence encoding the first monomer and/or the second amino acid sequence encoding the second monomer comprises an amino acid comprise an amino acid substitution from an arginine to an aspartate at residue 56 (R56D) and an amino acid substitution from a lysine to an aspartate at residue 96 (K96D) of SEQ ID NO:1 or 16 or positions corresponding thereto. Suitably, the first amino acid sequence encoding the first monomer or the second amino acid sequence encoding the second monomer comprises amino acid substitutions R56D and K96D in SEQ ID NO:1 or 16, or substitutions corresponding thereto, and further comprises a binding molecule attached to the monomer. Suitably, therefore the first or second monomer may be encoded by an amino acid sequence comprising a sequence set out in SEQ ID NO: 4 or SEQ ID NO: 5 or a sequence having at least at least 60 %, at least 70%, at least 80%, at least 90%, at least 95 %, at least 96%, at least 97%, at least 98%, at least 99% sequence identity thereto and comprising the mutations defined above. In one embodiment, a capsid protein heterodimer comprises a first monomer comprising amino acid substitutions E8K and E64K in SEQ ID NO:1 or 16, or substitutions corresponding thereto, and a second monomer comprising amino acid substitutions corresponding to R56D and K96D in SEQ ID NO:1 or 16, or substitutions corresponding thereto, and further comprising a binding molecule attached to the second monomer. In one embodiment, the capsid protein heterodimer comprises a monomer encoded by an amino acid sequence comprising the amino acid sequence set out in SEQ ID NO: 2. In one embodiment, the capsid protein heterodimer comprises a monomer encoded by an amino acid sequence comprising the amino acid sequence set out in SEQ ID NO: 4. In one embodiment, the capsid protein heterodimer comprises a first monomer encoded by an amino acid sequence comprising the amino acid sequence set out in SEQ ID NO: 2 and a second monomer encoded by an amino acid sequence comprising the amino acid sequence set out in SEQ ID NO: 4. In one embodiment, the capsid protein heterodimer comprises a monomer encoded by an amino acid sequence comprising the amino acid sequence set out in SEQ ID NO: 3. In one embodiment, the capsid protein heterodimer comprises a monomer encoded by an amino acid sequence comprising the amino acid sequence set out in SEQ ID NO: 5. In one embodiment, the capsid protein heterodimer comprises a first monomer encoded by an amino acid sequence comprising the amino acid sequence set out in SEQ ID NO: 3 and a second monomer encoded by an amino acid sequence comprising the amino acid sequence set out in SEQ ID NO: 5. In one embodiment, the capsid protein heterodimer comprises a first or second monomer encoded by an amino acid sequence comprising one or more mutations selected from the list consisting of: E64K, K67E, R56D, H88W, K96D, W71H, W71D, E8K, E8R, K96E, S78E, S78R, D64K, R82D, E67K, H88K, and E97K, and/or optionally a deletion at S78 of SEQ ID NO:1 or 16, or at a position corresponding thereto, or combinations thereof. Suitably E97K may be replaced with E79K. Suitably the one or more mutations may be selected from the list consisting of: E8K; E64K; K67E; R82D;E97K; and H88K of SEQ ID NO:1 or 16, or at a position corresponding thereto. Suitably the one or more mutations may be selected from the list: E8K and E64K of SEQ ID NO:1 or at a position corresponding thereto. Suitably the one or more mutations may be selected from the list: E8K; E64K; K67E; R82D;E97K; and H88K of SEQ ID NO:16, or at a position corresponding thereto. Suitably E97K may be replaced with E79K. Suitably the mutations may be selected from one or more of the following groups: (i) E8K and E64K and K67E; (ii) E8K and R82D and E97K; (iii) E8K and H88K; (iv) E64K and K67E; and R82D and E97K; (v) E64K and K67E; and H88K; (vi) R82D and E97K; and H88K; (vii) E8K; E64K and K67E; and R82D and E97K; (viii) E8K; E64K and K67E; and H88K; (ix) E8K; R82D and E97K; and H88K; (x) E64K and K67E; R82D and E97K; and H88K; or (xi) E8K; E64K and K67E; R82D and E97K; and H88K; Of SEQ ID NO:1 or 16, or at positions corresponding thereto. Suitably E97K may be replaced with E79K. Suitably such mutations are present in the first monomer. Suitably the one or more mutations may be selected from the list consisting of: R56D; K96D; W71D and a deletion at S78 of SEQ ID NO:1 or 16, or at a position corresponding thereto. Suitably the one or more mutations may be selected from the list: R56D and K96D of SEQ ID NO:1 or at a position corresponding thereto. Suitably the one or more mutations may be selected from the list: R56D; K96D; W71D; and a deletion of S78 of SEQ ID NO:16 or at a position corresponding thereto. Suitably the mutations may be selected from: (i) R56D and K96D; (ii) R56D and W71D; (iii) R56D and a deletion at S78; (iv) K96D and W71D; (v) K96D and a deletion at S78; (vi) W71D and a deletion at S78; (vii) R56D and K96D and W71D; (viii) R56D and K96D and a deletion at S78; (ix) R56D and W71D and a deletion at S78; (x) K96D and W71D and a deletion at S78; (xi) R56D and K96D and W71D and a deletion at S78; Of SEQ ID NO:1 or 16, or at positions corresponding thereto. Suitably such mutations are present in the second monomer. In one embodiment, the heterodimer comprises a first monomer encoded by an amino acid sequence comprising a substitution at E8K of SEQ ID NO:1 or 16, or at a position corresponding thereto, and a second monomer encoded by an amino acid sequence comprising a substitution at R56D of SEQ ID NO:1 or 16 or at a position corresponding thereto, the second monomer having a binding molecule attached. In one embodiment, the heterodimer comprises a first monomer encoded by an amino acid sequence comprising a substitution at E64K of SEQ ID NO:1 or 16, or at a position corresponding thereto, and a second monomer encoded by an amino acid sequence comprising a substitution at K96D of SEQ ID NO:1 or 16, or at a position corresponding thereto, the second monomer having a binding molecule attached. In one embodiment, the heterodimer comprises a first monomer encoded by an amino acid sequence comprising a substitution at H88K of SEQ ID NO:16 or at a position corresponding thereto and a second monomer encoded by an amino acid sequence comprising a substitution at W71D of SEQ ID NO:16 or at a position corresponding thereto, the second monomer having a binding molecule attached. In one embodiment, the heterodimer comprises a first monomer encoded by an amino acid sequence comprising a substitution corresponding to K67E of SEQ ID NO:16 or at a position corresponding thereto, and a second monomer encoded by an amino acid sequence comprising a wild type sequence (corresponding to SEQ ID NO:16), the second monomer having a binding molecule attached. In one embodiment, the heterodimer comprises a first monomer encoded by an amino acid sequence comprising a substitution corresponding to R82D and E97K of SEQ ID NO:16 or at a position corresponding thereto, and a second monomer encoded by an amino acid sequence comprising a wild type sequence (corresponding to SEQ ID NO:16), the second monomer having a binding molecule attached. Suitably E97K may be replaced with E79K. Suitably, the substitutions corresponding to R82D and E97K result in an Alpha-helix charge inversion. In one embodiment, the heterodimer comprises a first monomer encoded by a wild type amino acid sequence (corresponding to SEQ ID NO:1 or 16) and a second monomer encoded by an amino acid sequence comprising a deletion of a serine residue at a position corresponding to residue 78 of SEQ ID NO:16 or at a position corresponding thereto, the second monomer having a binding molecule attached. In a suitable embodiment, the heterodimer comprises a first monomer encoded by an amino acid sequence comprising one or more mutations selected from: E8K; E64K; K67E; R82D; E97K; and H88K of SEQ ID NO:1 or 16, or at positions corresponding thereto; and a second monomer encoded by an amino acid sequence comprising one or more mutations selected from: R56D; K96D; W71D; and a deletion at S78 of SEQ ID NO:1 or 16, or at positions corresponding thereto. Suitably, the second monomer having a binding molecule attached thereto. Suitably E97K may be replaced with E79K. In a suitable embodiment, the heterodimer comprises a first monomer encoded by an amino acid sequence comprising one or more mutations selected from: E8K and E64K of SEQ ID NO:1 or 16, or at positions corresponding thereto; and a second monomer encoded by an amino acid sequence comprising one or more mutations selected from: R56D and K96D of SEQ ID NO:1 or 16, or at positions corresponding thereto. Suitably, the second monomer having a binding molecule attached thereto. Suitably, in such cases, the heterodimer may be a hepatitis B heterodimer or a woodchuck hepatitis heterodimer. Suitably, when the heterodimeric viral capsid protein is from a woodchuck hepatitis virus, one or more further mutations may be present in the first and/or second monomers. Suitably, the first monomer further comprises one or more further mutations selected from: K67E; R82D; E97K; and H88K of SEQ ID NO:16, or at positions corresponding thereto. Suitably E97K may be replaced with E79K. Preferably the first monomer comprises the further mutation K67E, and optionally the further mutations R82D; E97K; and H88K of SEQ ID NO:16, or at positions corresponding thereto. Suitably E97K may be replaced with E79K. Suitably the second monomer further comprises one or more further mutations selected from: W71D and a deletion of residue S78 of SEQ ID NO:16, or at positions corresponding thereto. In a suitable embodiment, therefore, the heterodimer comprises a first monomer encoded by an amino acid sequence comprising one or more mutations selected from: E8K; E64K; K67E; R82D; E97K; and H88K of SEQ ID NO:16, or at positions corresponding thereto; and a second monomer encoded by an amino acid sequence comprising one or more mutations selected from: R56D; K96D; W71D; and a deletion of S78 of SEQ ID NO:16, or at positions corresponding thereto. Suitably E97K may be replaced with E79K. Suitably, the second monomer having a binding molecule attached thereto. Suitably in such cases, the heterodimer is a woodchuck hepatitis heterodimer. In one embodiment, the heterodimer is a hepatitis B capsid heterodimer and comprises a first monomer encoded by an amino acid sequence according to SEQ ID NO:1 and comprising mutations E8K and E64K; and a second monomer according to SEQ ID NO:1 and comprising mutations R56D and K96D. Suitably, the second monomer having a binding molecule attached thereto. In one embodiment, the heterodimer is a woodchuck hepatitis capsid heterodimer and comprises a first monomer encoded by an amino acid sequence according to SEQ ID NO:16 and comprising mutations E8K; E64K; and K67E, and a second monomer according to SEQ ID NO:16 and comprising mutations R56D; and K96D. Suitably, the second monomer having a binding molecule attached thereto. In another embodiment, the heterodimer is a woodchuck hepatitis capsid heterodimer and comprises a first monomer encoded by an amino acid sequence according to SEQ ID NO:16 and comprising mutations E8K; E64K; K67E; R82D; E97K; and H88K, and a second monomer according to SEQ ID NO:16 and comprising mutations R56D; K96D; W71D and a deletion of S78. Suitably E97K may be replaced with E79K. Suitably, the second monomer having a binding molecule attached thereto. Suitably, the heterodimer may comprise any combination of mutations described above. Suitably, a mutation to the first and/or second amino acid sequence may modify the electrostatic interactions between the first monomer an the second monomer. Suitably, the electrostatic interactions between the first monomer and the second monomer may be modified to increase repulsions and/or attractions between the monomers. Suitably, a mutation of the first and/or second amino acid sequence may modify electrostatic interactions to increase repulsion between the first and the second amino acid sequences. Suitably, a mutation of the first and/or second amino acid sequence may modify electrostatic interactions to increase attraction between the first and the second amino acid sequences. Suitably, the mutations described on any one of the embodiments of the present invention modify the electrostatic interactions between the first and the second monomers to promote association thereof. Suitably, this association results in the formation of heterodimers. Suitably, the heterodimer comprises a single binding molecule attached exclusively to either the first or the second monomer. Suitably, the binding molecule is a binding protein. Suitably, any of the embodiments described herein may comprise further mutations or modifications to the amino acid sequences encoding the first and/or the second monomers. Binding molecule The present invention is based on the use of VLPs to present a functional molecule on its surface, for example to the immune system. Suitably, the invention relates to VLPs which make use of a binding molecule which can attach a functional molecule, typically an antigen, to the viral capsid proteins forming the VLP. In accordance with the invention, there is provided an a first capsid protein monomer encoded by a first amino acid sequence and a second capsid protein monomer encoded by a second amino acid sequence. Suitably, the first or second monomer comprises a binding molecule attached thereto. Suitably, each capsid protein heterodimer comprises a binding molecule attached exclusively to either the first or the second monomer. Suitably, each capsid protein heterodimer is able to attach a functional molecule via the binding molecule. Suitably therefore the binding molecule is operable to bind to a functional molecule. Suitably, the binding molecule may be any molecule that can be attached to the first or second monomer for the purposes of attaching to a functional molecule, such as an antigen. In one embodiment the binding molecule is a binding protein. Suitably the binding protein has low homology to proteins of the subjects which may be treated with the VLP. Suitably the binding protein has low homology to human proteins. Suitably the binding protein has low homology with the tertiary structure of any human proteins. Advantageously, low homology with human proteins means that the binding protein itself is less likely to stimulate an off-target immune reaction. Suitably the binding protein does not contain any disulphide bonds. Suitably the binding protein is not glycosylated. Suitably the binding protein is relatively small in size. Suitably the binding protein comprises a relatively short sequence length. Suitably the binding protein comprises a length of between 84 – 134 amino acids. Suitably the binding protein comprises a length of less than 135 amino acids. Advantageously, the lack of disulphide bonds, lack of glycosylation, and small size means that the binding protein is easier to produce in bacterial cells such as E.coli. Suitably the binding protein comprises a bacterial toxin or a bacterial toxin inhibitor or antitoxin. Suitably the binding protein of the VLP is a bacterial toxin inhibitor. Suitably, the binding protein is a bacterial toxin inhibitor called Im7. Suitably, the binding protein is a bacterial toxin inhibitor called Barstar. Suitably the binding protein is part of a pair of binding proteins. Suitably therefore the binding protein attached to the first or second monomer is a first binding protein operable to bind to a second binding protein. Suitably the second binding protein is attached to the functional molecule. Optionally via a linker, as explained hereinabove, which may be an alpha helix linker. Suitably comprising or consisting of a sequence according to ID NO:33. Suitably the first binding protein is a bacterial toxin or a bacterial toxin inhibitor or antitoxin. Suitably the first binding protein of the VLP is a bacterial toxin inhibitor which may be selected from Im7 or Barstar. Alternatively the first binding protein may be SpyCatcher. Alternatively, the first binding protein may be a nanobody. Suitably the second binding protein is a bacterial toxin which may be selected from ColE7, or Barnase. Alternatively the second binding protein may be SpyTag. Alternatively the second binding protein may be a cognate target protein. In one embodiment, the first binding protein is Barstar and the second binding protein is Barnase. In an alternative embodiment, the first binding protein is Im7 and the second binding protein is ColE7. Preferably the first binding protein is Im7 and the second binding protein is ColE7. Advantageously, this pair of binding proteins allows purification of VLPs by anion chromatography. In an alternative embodiment, the first binding protein is a nanobody and the second binding protein is a cognate target protein. In a suitable embodiment, the first binding protein is attached exclusively to either the first or second monomer of the invention and the second binding protein is attached to a functional molecule. Suitably, the first binding protein binds to the second binding protein. Suitably, a binding molecule may comprise the SpyTag/SpyCatcher system. Suitably the binding protein may be the wild-type protein, or it may be modified. Suitably the binding protein may be modified to improve its function as a binding protein in the context of the VLP of the invention. Suitable modifications may include: insertions, deletions, substituents, truncations, reversals, repeats, or the like in the amino acid sequence encoding the protein. Suitably, any property of the bacterial toxin binding protein detrimental to either the host cell and / or the recipient organism intended for VLP administration is neutralized by targeted modifications. Suitably the or each binding protein may comprise one or more amino acid substitutions. Suitably the amino acid substitutions may increase the binding affinity between the or each binding protein and the functional molecule . Suitably the amino acid substitutions may remove undesirable disulphide bonds from a given binding protein. Suitably the or each binding protein may comprise one or more amino acid substitutions. In an embodiment where the first binding protein is Barstar, suitably the amino acid sequence of Barstar comprises one or more of the following substitutions: C40A, C82A, and I87E. Suitably the amino acid sequence of Barstar may comprise all of the following substitutions: C40A, C82A, and I87E. Suitably the amino acid sequence of Barstar comprises: KKAVINGEQIRSISDLHQTLKKELALPEYYGENLDALWDALTGWVEYPLVLEWRQFEQSK Q LTENGAESVLQVFREAKAEGADITIELS (SEQ ID NO: 6) In an embodiment where the first binding protein is Im7, suitably the amino acid sequence of Im7 comprises the following substitution: F41L. Suitably the amino acid sequence of Im7 comprises: ELKNSISDYTEAEFVQLLKEIEKENVAATDDVLDVLLEHFVKITEHPDGTDLIYYPSDNR DDS PEGIVKEIKEWRAANGKPGFKQ (SEQ ID NO: 7). Suitably the second binding protein may also comprise one or more amino acid substitutions. Suitably the amino acid substitutions in the amino acid sequence of the second binding protein may increase the negative charge of the second binding protein. In an embodiment where the second binding protein is Barnase, suitably the amino acid sequence of Barnase comprises the following substitution: E73W. Suitably the amino acid sequence of Barnase comprises: AQVINTFDGVADYLQTYHKLPDNYITKSEAQALGWVASKGNLADVAPGKSIGGDIFSNRE G KLPGKSGRTWRWADINYTSGFRNSDRILYSSDWLIYKTTDHYQTFTKIR (SEQ ID NO: 12). In an embodiment where the second binding protein is ColE7, suitably the amino acid sequence of ColE7 comprises one or more of the following substitutions: Arg538Ala, Glu542Ala, and His569Ala. Suitably the amino acid sequence of ColE7 may comprise all of the following substitutions: Arg538Ala, Glu542Ala, and His569Ala. Suitably the amino acid sequence of ColE7 comprises: ESKRNKPGKATGKGKPVNNKWLNNAGKDLGSPVPDRIANKLRDKEFKSFDDFRKKFWEEV SKDPELSKQFSRNNNDRMKVGKAPKTRTQDVSGKATSFALHHEKPISQNGGVYDMDNISV VTPKRAIDIHRGKS (SEQ ID NO: 13). Suitably the first or second binding proteins may be truncated. Suitably the second binding protein is truncated. In an embodiment where the second binding protein is ColE7, suitably the whole or a part of the ColE7 protein may be used as the second binding protein. Suitably only a part of the ColE7 protein is used as the second binding protein. Suitably the ColE7 protein is truncated, suitably so that it only comprises the catalytic domain of ColE7. Suitably the second binding protein comprises the catalytic domain of ColE7. In an embodiment where the second binding protein is Barnase, suitably the whole or a part of the Barnase protein may be used as the second binding protein. Suitably only a part of the Barnase protein is used as the second binding protein. Suitably the Barnase protein is truncated, suitably so that it only comprises the catalytic domain of Barnase. Suitably the second binding protein comprises the catalytic domain of Barnase. Suitably the binding molecule may comprise additional modifications. Suitably the binding molecule may comprise chemical modification. Suitably Im7 may comprise chemical modification. Suitably the chemical modification is capable of binding to a functional molecule. Suitably the chemical modification is capable of covalently binding to a functional molecule. In one example, the functional molecule bound to the chemical modification may be a fluorescent molecule. Other suitable functional molecules are described elsewhere herein. Suitably the chemical is attached to the first binding protein by non-covalent binding. Suitably the chemical is attached to the first binding protein by electrostatic and/or hydrophobic bonding. Suitably chemical modifications include alkanes having an amine group. Suitably the alkane may have any chain length. Suitably the alkane is a lower alkane. Suitably the alkane may have a chain length of between 1 and 10 carbons. Suitably the alkane may have a chain length of between 4 and 8 carbons. Suitably the alkane may be branched. Suitably, the length of the carbon chain and the length of branched substitutions on the amine group are chosen such as to allow either irreversible attachment to the protein or reversible attachment, dependent on the desired application. In one embodiment, the chemical is attached irreversibly to the first binding protein. Suitably, in such an embodiment, conferring irreversible binding, the alkane has eight carbon atoms and a terminal nitrogen (octylamine). In another embodiment, the chemical is attached reversibly to the first binding protein. Suitably, in such an embodiment, allowing reversible binding the alkane has 4 carbon atoms in a branched structure (diethylethanolamine). Suitably the first binding protein may be chemically modified at one or more sites, suitably at one or more amino acids. Suitably the first binding protein is chemically modified at one amino acid. In one embodiment, the first binding protein is chemically modified with DEAE. In one embodiment, the first binding protein is chemically modified with octylamine. Suitably, in such embodiments, the first binding protein may be Im7. Suitably, modification with DEAE allows the first binding protein to be purified. Suitably purification by chromatography. Suitably modification with octylamine allows the first binding protein to directly bind to a functional molecule. In one embodiment, the chemical modification of the binding protein occurs within the host cell. Suitably by post-translational modification. In another embodiment, the chemical modification of the binding protein occurs outside of the host cell. Suitably by means of a chemical reaction. Suitably by means of a non-enzymatically catalyzed non-covalent attachment. Functional Molecule The present invention relates to VLPs which are able to display various functional molecules on their surface by virtue of a binding molecule which may be a binding protein attached exclusively to the first or second monomer of the heterodimeric capsid proteins. Suitably, each heterodimer has a single binding molecule attached. Suitably the binding molecule is a binding protein. Suitably the binding molecule is attached to at least one functional molecule. Suitably the binding molecule may be attached to more than one functional molecule. Suitably the functional molecule(s) may be of the same type or different types. For example, the binding molecule may be attached to any combination of one or more antigens, antigen binding proteins, or fluorescent molecules. Suitably the binding protein is attached to one functional molecule. Suitably the binding protein may be attached to a functional molecule by a chemical modification, or alternatively via a second binding protein wherein in such an embodiment the binding protein attached to the capsid protein is the first binding protein. In one embodiment, the binding protein may comprise a chemical modification. Suitably, a chemical modification may be attached to a functional molecule. Suitably, in such an embodiment, the functional molecule is attached to the binding protein via the chemical modification. Suitably in such embodiments, the functional molecule is a non- protein antigen or epitope thereof, or a fluorescent molecule. Suitably, wherein each viral capsid protein is attached to a binding protein, and each chemical modification is attached to a functional molecule. In another embodiment, the functional molecule may be attached to the second binding protein. Suitably, the second binding protein is Barnase. Suitably, the second binding protein is ColE7. Suitably, the second binding protein may be attached to the first binding protein, the first binding protein being exclusively attached to either the first or the second monomer of the invention. Suitably the first binding protein is Barstar. Suitably, the first binding protein is Im7. In one embodiment of the present invention, the functional molecule is attached to Barnase. Suitably, Barnase may be bound to Barstar. In another embodiment, the functional molecule is attached to ColE7. Suitably, ColE7 may be bound to Im7. Suitably the binding proteins are directly or indirectly attached to the viral capsid protein and to the functional molecule. Suitably the binding proteins are directly attached to the viral capsid protein and in some cases directly attached to the functional molecule. Suitably, the binding protein may be fused to the first or second monomer of the viral capsid protein heterodimer as described hereinabove. Suitably, the functional molecule may be fused to the binding protein. In some embodiments, the binding protein may be indirectly attached to the functional molecule via a second binding protein attached to the first binding protein. Alternatively , the binding protein may be indirectly attached to the functional molecule. Suitably via chemical modification. Suitable functional molecules may include: protein or non-protein antigens; antigen binding proteins such as antibodies or binding fragments thereof, antibody mimetics, and aptamers; fluorescent molecules. Suitably the functional molecule may be modified, suitably by the introduction of one or more mutations to change its characteristics, properties or biological effect. Sutiably the functional molecule many comprise one or more substitution mutations for example. Suitably the functional molecule is an antigen binding molecule such as an antibody. Suitably the second binding protein is a generic antibody binding protein. Suitably the antibody binding protein is selected from protein G, protein A, protein AG, and streptavidin. Suitably, an antigen binding protein such as an antibody for use as a functional molecule is capable of binding an antigen of interest. Suitably the use of an antigen binding protein such as an antibody as a functional molecule produces a VLP which is capable of binding to an antigen. Suitably this is useful for detecting an antigen, or for targeting the VLP to an antigen. Suitable antigens may include the whole or part of an antigen. Suitably the antigen may be a subunit or monomer of an antigen. Suitably the functional molecule may be an epitope of an antigen. Suitably the use of an antigen as a functional molecule produces a VLP which is capable of stimulating an immune response to the antigen. Suitably this is useful as a vaccine. Suitably the antigen may be a protein or non-protein antigen. Suitable non-protein antigens may include sugars, lipids or carbohydrates, or small molecule chemicals to which an immune response is desired, or who need to be detected, such as nicotine, cocaine, or other exogenous toxins. Suitably the antigen may be a self or non-self antigen relative to the subject intended to be treated with the VLP. Suitably the antigen may be a human or non-human antigen. Suitably the antigen may be derived from the causative agent in a disease or disorder. Suitably the causative agent may be self or non-self. Suitably a non-self causative agent may be an infectious agent. Suitably therefore the antigen may be derived from an infectious agent such as a virus, bacterium, fungus, protozoan, archaeon. Suitably the antigen may be derived from a virus selected from: Adeno-associated virus, Chikungunya virus, Crimean-Congo hemorrhagic fever virus, Dengue virus, Ebolavirus, Echovirus, Encephalomyocarditis virus, Epstein-Barr virus, Hantaan virus, Hepatitis A virus, Hepatitis B virus, Hepatitis C virus, Hepatitis D virus, Hepatitis E virus, Human adenovirus, Human astrovirus, Human coronavirus, Human cytomegalovirus, Human enterovirus, Human herpesvirus, Human immunodeficiency virus, Human papillomavirus, Human parainfluenza, Human respiratory syncytial virus, Human rhinovirus, Human torovirus, Influenza A virus, Influenza B virus, Influenza C virus, Japanese encephalitis virus, Polyomavirus, Kunjin virus, Lassa virus, Measles virus, Molluscum contagiosum virus, Mumps virus, Nipah virus, Poliovirus, Rabies virus, Rotavirus A, Rotavirus B, Rotavirus C, Rubella virus, Sagiyama virus, Salivirus A, Sapporo virus, Sindbis virus, Toscana virus, Uukuniemi virus, Varicella-zoster virus, Venezuelan equine encephalitis virus, Vesicular stomatitis virus, Western equine encephalitis virus, West Nile virus, Yellow fever virus, Zika virus. Suitably the antigen may be derived from a bacterium selected from: Actinomyces israelii, Bacillus anthracis, Bacillus cereus, Bartonella henselae, Bartonella quintana, Bacteroides fragilis, Bordetella pertussis, Borrelia burgdorferi, Borrelia garinii, Borrelia afzelii, Borrelia recurrentis, Brucella abortus, Brucella canis, Brucella melitensis, Brucella suis, Campylobacter jejuni, Chlamydia pneumoniae, Chlamydia trachomatis, Chlamydophila psittaci, Clostridium botulinum, Clostridium difficile, Clostridium perfringens, Clostridium tetani, Corynebacterium diphtheriae, Enterococcus faecalis, Enterococcus faecium, Escherichia coli, Francisella tularensis, Haemophilus influenzae , Helicobacter pylori, Klebsiella pneumoniae, Legionella pneumophila, Leptospira interrogans, Leptospira santarosai, Leptospira weilii, Leptospira noguchii, Listeria monocytogenes , Mycobacterium leprae, Mycobacterium tuberculosis, Mycobacterium ulcerans, Mycoplasma pneumoniae, Neisseria gonorrhoeae, Neisseria meningitidis, Nocardia asteroides, Pseudomonas aeruginosa, Rickettsia rickettsia, Salmonella enterica subsp. enterica , Salmonella typhi, Shigella sonnei, Shigella dysenteriae, Staphylococcus aureus, Staphylococcus epidermidis, Staphylococcus saprophyticus, Streptococcus agalactiae, Streptococcus pneumoniae, Streptococcus pyogenes, Streptococcus viridans, Treponema pallidum, Ureaplasma urealyticum, Vibrio cholerae, Yersinia pestis, Yersinia enterocolitica, Yersinia pseudotuberculosis . In one embodiment the antigen is derived from a coronavirus, suitably from SARS-CoV-2. Suitably the antigen is the whole or part of a spike protein derived from SARS-CoV-2, or the whole or part of a nucleocapsid protein derived from SARS-CoV-2. In one embodiment, therefore, the functional molecule is part of a spike protein derived from SARS-CoV-2. Suitably the receptor binding domain. In another embodiment, therefore, the functional molecule is part of a nucleocapsid protein derived from SARS-CoV-2. Suitably the C-terminus. Suitably a self-causative agent may be a non-infectious agent. Suitably therefore the antigen may be derived from a non-infectious agent such as an inflammatory molecule, or a molecule causing degenerative changes in nervous (such as beta-amyloid), cartilage or bone tissue, or a molecule causing worsening of a neoplastic disease. Suitably the antigen may be an inflammatory molecule or a molecule causing degenerative changes or a molecule conducive to a neoplastic disease which is a causative agent in a disease or disorder. Suitably the molecule may operate in humans or in non-human mammals. Suitably the molecule may cause a disease or disorder in a specific species. Suitable inflammatory molecules may include chemokines or cytokines, or proteases. Suitable chemokines or cytokines may include: interleukins, tumour necrosis factors, interferons, and colony stimulating factors. Suitable chemokines or cytokines may include: IL1, IL2, Il3, Il4, IL5, Il6, Il7, IL8, IL9, IL10, IL11, IL12, IL13, IL17, IL33, TNFα, TNFβ, IFNα, IFNβ, IFNγ, G-CSF, GM-CSF, M-CSF, erythropoietin, and TGFβ. Suitable proteases may include ADAMTS4, ADAMTS5. Suitably the antigen is an interleukin or a protease. Suitably the antigen is IL13, IL17 or IL33 or a fragment thereof. In one embodiment, therefore, the functional molecule is IL13, IL17 or IL33. In one embodiment the IL13 is modified. In one embodiment the IL13 may comprise one or more substitution mutations. Suitably the or each modification may reduce, limit, or change the effect of IL3, suitably it may reduce the transactivation of receptors. Suitable molecules which case degenerative changes in nervous tissue or worsening of neoplastic diseases may include: ADAMTS4/5, angiogenesis factors, or factors allowing escape of tumours such as galectin proteins. References to any antigens herein may equally refer to an epitope of said antigen. An antigen of interest may be any of those listed above. For example, an antigen of interest may be from a disease causing agent such as a virus, bacterium, fungus, protozoan, or archaeon. Alternatively, an antigen of interest may be from a non-infectious agent, for example, a cell surface receptor. Suitably the antibody may be capable of binding to an antigen from a virus, bacterium, fungus, protozoan, archaeon as listed above. Suitable viruses may be selected from, for example: Adeno-associated virus, Chikungunya virus, Crimean-Congo hemorrhagic fever virus, Dengue virus, Ebolavirus, Echovirus, Encephalomyocarditis virus, Epstein-Barr virus, Hantaan virus, Hepatitis A virus, Hepatitis B virus, Hepatitis C virus, Hepatitis D virus, Hepatitis E virus, Human adenovirus, Human astrovirus, Human coronavirus, Human cytomegalovirus, Human enterovirus, Human herpesvirus, Human immunodeficiency virus, Human papillomavirus, Human parainfluenza, Human respiratory syncytial virus, Human rhinovirus, Human torovirus, Influenza A virus, Influenza B virus, Influenza C virus, Japanese encephalitis virus, Polyomavirus, Kunjin virus, Lassa virus, Measles virus, Molluscum contagiosum virus, Mumps virus, Nipah virus, Poliovirus, Rabies virus, Rotavirus A, Rotavirus B, Rotavirus C, Rubella virus, Sagiyama virus, Salivirus A, Sapporo virus, Sindbis virus, Toscana virus, Uukuniemi virus, Varicella-zoster virus, Venezuelan equine encephalitis virus, Vesicular stomatitis virus, Western equine encephalitis virus, West Nile virus, Yellow fever virus, Zika virus. In one embodiment, the functional molecule is an antibody capable of binding to an antigen from a coronavirus. In one embodiment, the antibody is capable of binding to an antigen from SARS-CoV-2. Suitable bacteria may be selected from: Actinomyces israelii, Bacillus anthracis, Bacillus cereus, Bartonella henselae, Bartonella quintana, Bacteroides fragilis, Bordetella pertussis, Borrelia burgdorferi, Borrelia garinii, Borrelia afzelii, Borrelia recurrentis, Brucella abortus, Brucella canis, Brucella melitensis, Brucella suis, Campylobacter jejuni, Chlamydia pneumoniae, Chlamydia trachomatis, Chlamydophila psittaci, Clostridium botulinum, Clostridium difficile, Clostridium perfringens, Clostridium tetani, Corynebacterium diphtheriae, Enterococcus faecalis, Enterococcus faecium, Escherichia coli, Francisella tularensis, Haemophilus influenzae , Helicobacter pylori, Klebsiella pneumoniae, Legionella pneumophila, Leptospira interrogans, Leptospira santarosai, Leptospira weilii, Leptospira noguchii, Listeria monocytogenes , Mycobacterium leprae, Mycobacterium tuberculosis, Mycobacterium ulcerans, Mycoplasma pneumoniae, Neisseria gonorrhoeae, Neisseria meningitidis, Nocardia asteroides, Pseudomonas aeruginosa, Rickettsia rickettsia, Salmonella enterica subsp. enterica , Salmonella typhi, Shigella sonnei, Shigella dysenteriae, Staphylococcus aureus, Staphylococcus epidermidis, Staphylococcus saprophyticus, Streptococcus agalactiae, Streptococcus pneumoniae, Streptococcus pyogenes, Streptococcus viridans, Treponema pallidum, Ureaplasma urealyticum, Vibrio cholerae, Yersinia pestis, Yersinia enterocolitica, Yersinia pseudotuberculosis. Suitably in such an embodiment, the VLP may be targeted to a particular virus. Suitably targeted to bind to a particular virus. Suitably the VLP may therefore be used for detecting the presence of a virus. Further details on this use are provided elsewhere. Suitably the antigen binding protein such as an antibody may be capable of binding to an antigen from a cell surface receptor. Suitably the cell surface receptor may be an ion-channel linked receptor, a G-protein coupled receptor, or an enzyme-linked receptor. Suitably the cell surface receptor is selected from: 5-HT receptor, nAch-receptor, Zinc-activated ion channel, GABAA receptor, Wnt-family member receptors, co-receptors contained in lipid rafts, T-cell and T-cell co-receptors, B-cell receptors and B-cell costimulatory molecules, Glycine receptor, AMPA receptor, Kainate receptor, NMDA receptor, Glutamate receptor, ATP-gated channel, PIP2 gated channel, Erb receptor, GDNF receptor, NP receptor, trk receptor, toll-like receptor, GABAB receptor, GBPCR class A, B, C, D, E, or F. Suitably in such an embodiment, the VLP may be targeted to a particular cell. Suitably targeted to bind to a particular cell. Suitably the VLP may be used to deliver cargo to a cell. Further details on this use are provided elsewhere. Suitable antibodies may include IgG, IgM, IgE, IgA, IgD antibodies. Suitably, the antibody is an IgG antibody. Suitably IgG subclasses include IgG1, IgG2, IgG3 and IgG4. Suitable further antigen binding proteins may include antibody binding fragments or antibody mimetics which perform the same function as an antibody. Suitably they are also capable of binding an antigen of interest. Suitably the use of an antibody binding fragment or mimetic as a functional molecule also produces a VLP which is capable of binding to an antigen. Suitably this is useful for detecting an antigen, or for targeting the VLP to an antigen as described above. Suitable antibody binding fragments may include: Fab, monospecific or bispecific F(ab)2, F(ab’)2, monospecific or bispecific diabody, nanobody, ScFv, ScFv-Fc, F(ab)3. Suitable antibody mimetics may include affibodies, affilins, affimers, affitins, alphabodies, anticalins, avimers, DARPins, fynomers, Kunitz domain peptides, monobodies, nanCLAMPs. Suitably the use of a fluorescent molecule as a functional molecule produces a VLP which is visible. Suitably this is useful for labelling, especially when combined with a second functional molecule which can bind to an antigen, for example antibodies or binding fragments thereof, antibody mimetics, or aptamers. Suitable fluorescent molecules may include: GFP, EBFP, EBFP2, Azurite, GFPuv, T-saphhire, Cerulean, CFP, mCFP, mTurquoise2, CyPet, mKeima-red, tagCFP, AmCyan1, mTFP1, midoriishi cyan, turboGFP, tagGFP, emerald, azami green, ZsGreen1, YFP, tagYFP, EYFP, topaz, venus, mCtrine, YPet, turboYFP, ZsYellow1, Kusabira Orange, mOrange, allophycocyanin, mkO, RFP, turboRFP, tdTomato, tagRFP, dsRed, mStrawberry, turboFP602, asRed2, J-red, R-phycoerythrin, B-phycoerythrin, mCherry, HcRed, Katusha, P3, peridin chlorophyll, mKate, turboFP635, mPlum, mRaspberry. Suitably the fluorescent molecule is GFP or any modified form of GFP. In one embodiment of the invention, the or each functional molecule is IL13, IL17, IL33, the receptor binding domain of SARS Cov-2 spike protein, or the C-terminus of the SARS Cov-2 nucleocapsid protein. In another embodiment of the invention, the or each functional molecule is an IgG antibody or binding fragment thereof. In one embodiment, the antibody or binding fragment thereof is an antibody or binding fragment thereof directed towards SARS-CoV-2. Suitably the functional molecule is an epitope. Suitably an epitope selected from IL-13, IL-33, IL-31, IL-17, or SARS-Cov2 spike protein receptor binding domain. In one embodiment, the functional molecule is IL-31, suitably according to SEQ ID NO:17. Suitably the functional molecules may comprise one or more epitopes and/or a fluorescent molecule. Suitably the functional molecules may comprise two epitopes. Suitably the functional molecules may comprise an epitope and a fluorescent molecule. Virus-Like Particle (VLP) The present invention relates to VLPs, their uses and methods of manufacture thereof. Suitably the VLP comprises one or more viral capsid protein heterodimers which suitably form a VLP. Suitably the one or more viral capsid proteins self-assemble into the VLP. Suitably the VLP comprises one or more binding molecules, each attached to a viral capsid protein heterodimer. Suitably the VLP comprises one or more functional molecules which are suitably each attached to the binding molecule, and/or chemical modifications present on the binding molecule of the capsid protein heterodimer. Suitably, in such a way, the VLP of the invention stably displays the functional molecules on its surface. Suitably the VLP may comprise a plurality of subunits. Suitably each subunit comprises a complete viral capsid protein heterodimer, one binding molecule and one functional molecule. Suitably the subunits self-assemble into a VLP. Suitably therefore the VLP comprises a plurality of viral capsid protein heterodimers, a plurality of binding molecules (each attached to a capsid protein heterodimer and a plurality of functional molecules, each attached to a binding molecule . Suitably each viral capsid heterodimer comprise a first monomer and a second monomer. The first and/or the second monomer comprising at least one mutation in its amino acid sequences as compared to the wildtype amino acid sequence. Suitably, each capsid protein heterodimer comprises a single binding molecule. Suitably, the binding molecule may be attached to either the first or the second monomer. Suitably, the binding molecule is attached to at least one functional molecule. In an embodiment of the first aspect of the invention, the VLP comprises a plurality of capsid protein heterodimers, each heterodimer comprising a first and a second monomer, a binding molecule attached to either the first or the second monomer, and a functional molecule. In such an embodiment, the amino acid sequence of the first and/or second monomer comprises at least one mutation as compared to the wild-type sequence. Suitably, the mutation in the amino acid sequence promotes association of the monomers to form heterodimers. It will be appreciated to those skilled in the art, that unmodified wild-type Hepatitis B viral capsid proteins favour the formation of homodimers. Suitably, the inventors have found that the introduction of specific mutations in the amino acid sequence of the monomeric subunits of the Hepatitis B viral capsid proteins promotes association of the mutated monomers to form heterodimers. Suitably, the first or second monomer of the heterodimer comprises a binding molecule. Suitable mutations to the amino acid sequences of the monomeric subunits that promote heterodimerisation are discussed elsewhere in the specification. Suitably the VLP comprises a negative surface charge, suitably a homogenous negative surface charge. Suitably the binding molecule may be a binding protein or a pair of binding proteins as discussed hereinabove. Suitably, the VLP may have an average diameter of between 20nm to 100nm, suitably between 25nm and 75nm, suitably between 28nm and 50nm, suitably between 30nm and 40nm, suitably around 32nm. Suitably the size of the VLP may be determined by dynamic light scattering (DLS). For example using a Malvern Zetasizer Ultra. Nucleic Acids and Vectors The present invention relates to nucleic acids encoding component protein parts which form the VLP, and vectors comprising said nucleic acids which may be used in host cells to produce VLPs. Suitably the invention relates to, and makes use of, a first nucleic acid encoding a first viral capsid protein monomer and a second nucleic acid encoding a second viral capsid protein monomer. Suitably, the first or second nucleic acid may encode a capsid protein monomer attached to a binding molecule. Suitably the first or second nucleic acid may encode a fusion protein comprising the viral capsid protein monomer fused to a binding molecule. Suitably the viral capsid protein may be a hepatitis B capsid protein. Suitably the viral capsid protein may be a Woodchuck hepatitis capsid protein. Suitably, the binding molecule may be a binding protein, suitably a first binding protein. Suitably the first or second nucleic acids encoding a fusion protein comprising the viral capsid protein monomer fused to a binding molecule may be known as the ‘capsid fusion protein’. Suitably the first or second nucleic acid sequences may encode a viral capsid protein monomer and may suitably comprise a sequence according to SEQ ID NO: 20 or 23. Suitably the first or second nucleic acid sequences may encode a viral capsid protein monomer and may suitably comprise a sequence having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% identity with SEQ ID NO: 20 or 23. Suitably the first or second nucleic acid sequences may encode a viral capsid protein monomer and may consist of a sequence according to SEQ ID NO: 20 or 23. Suitably any of these monomer sequences may further comprise a sequence encoding a binding molecule, suitably encoding the viral capsid protein monomer fused to a binding molecule, suitably to a first binding protein. Suitably the first and second nucleic acid sequences may encode a heterodimer comprising a binding molecule, suitably a first binding protein, and may suitably comprise a sequence having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% identity with SEQ ID NO: 18, 19, 21, or 22. Suitably therefore a nucleic acid encoding a heterodimer of the invention may comprise a sequence having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% identity with SEQ ID NO: 18, 19, 21, or 22. Suitably the invention relates to, and makes use of, a third nucleic acid encoding a functional molecule. Suitably, the third nucleic acid encoding a functional molecule may be optionally attached to a second binding protein as explained hereinabove. Suitably the third nucleic acid may encode a fusion protein comprising the functional molecule optionally fused to a second binding protein. Suitably this may be known as the ‘functional fusion protein’. In one embodiment, the third nucleic acid encodes only a functional molecule. In one embodiment, the third nucleic acid encodes a functional molecule attached to second binding protein. In one embodiment, the third nucleic acid encodes a functional molecule fused to a second binding protein. In one embodiment the third nucleic acid encodes a functional fusion protein. One example of a third nucleic acid sequence encoding a functional molecule is a sequence having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% at least 96%, at least 97%, at least 98%, at least 99% identity with SEQ ID NO:17. Suitably the third nucleic acid may comprise a sequence encoding a functional molecule attached to a second binding protein, suitably having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% at least 96%, at least 97%, at least 98%, at least 99% identity with SEQ ID NO: 24-25. Suitably the third nucleic acid encoding a functional molecule attached to a second binding protein may consist of a sequence according to SEQ ID NO: 24-25. In embodiments where the third nucleic acid encodes two epitopes, they may be any two epitopes fused to a second binding protein. In one embodiment, the third nucleic acid may encode for example a SARS-Cov2 spike protein receptor binding domain and a C-terminal fragment of the nucleocapsid protein. In embodiments where the third nucleic acid encodes an epitope and a fluorescent molecule fused to a second binding protein, they may be any epitope and any fluorescent molecule. In one embodiment, the third nucleic acid may encode for example a SARS-Cov2 spike protein receptor binding domain and eGFP. In some embodiments, the invention may make use of the first and second nucleic acids. In some embodiments, the invention may make use of the first, second and third nucleic acids. Suitably the first, second, and third nucleic acids described herein may be provided as one contiguous nucleic acid sequence, or may be provided as a plurality of separate nucleic acid sequences. References to the first, second, and third, nucleic acids include embodiments where plurality of nucleic acid sequences may be used to encode the same proteins as the first, second, third, nucleic acids. Suitably, the first and second nucleic acids may comprise a sequence according to SEQ ID NO: 18, 19, 21 or 22. Suitably the third nucleic acid may comprise a sequence according to SEQ ID NO: 24 or 25. Suitably the first and second nucleic acids may comprise a contiguous sequence according to SEQ ID NO:18 or 21, and the third nucleic acid may comprise a sequence according to SEQ ID NO: 24. Suitably in such an embodiment, the first binding protein is lm7 and the second binding protein is Col-E7. Suitably the first and second nucleic acids may comprise a contiguous sequence according to SEQ ID NO:19 or 22, and the third nucleic acid may comprise a sequence according to SEQ ID NO: 25. Suitably in such an embodiment, the first binding protein is Barstar and the second binding protein is Barnase. Suitably the nucleic acids may comprise one or more expression elements to aid in expression of the proteins encoded thereon. Suitable expression elements include promoters, operators, enhancers, activators, repressors, 5’UTRs, 3’UTRs, introns, IRES, etc. Suitably each of the nucleic acids comprises one or more expression elements which ensure equal expression of the proteins encoded thereon. Suitably each of the nucleic acids comprises a promoter which ensures equal expression of the proteins encoded therein. Suitably the promoter may comprise one or more modifications which adapt the level of expression therefrom. Suitably the promoter may comprise one or more mutations. Suitably the or each nucleic acid described herein is operably linked to a promoter. Suitable promoters may be selected from: CMV-IE, EF1a, SV40, PGK1, CAG, human beta actin, T7, TetR/TetA, T7lac, SP6, LP1, TTR, CK8, Synapsin, Glial fibrillary acidic protein (GFAP), CaMKII, TBG, and albumin promoter. Suitably each nucleic acid may be linked to the same promoter or a different promoter. Suitably each nucleic acid may be linked to the same promoter. Suitably therefore each nucleic acid may be expressed at the same time. Suitably each nucleic acid may be linked to a T7 promoter, optionally with one or more modifications to ensure equal expression levels of the proteins encoded by the nucleic acids. Suitably each nucleic acid may be linked to a different promoter. Suitably therefore each nucleic acid may be expressed at different times. Suitably the or each nucleic acid may be independently expressed. Suitably expression of each nucleic acid may be induced at different times. Suitably therefore the or each promoter may be an inducible promoter. Suitably which may be induced by contacting the promoter with a suitable inducer, at a concentration effective to induce expression therefrom. In one embodiment, the first or second nucleic acid sequence may be linked to a first promoter and the first or second nucleic acid may be linked to a second promoter. Suitably the first or second promoter may be a T7 promoter. Suitably, the T7 promoter may comprise the sequence agcataat (SEQ ID NO:8). Suitably the first or second promoter may be a TetR/TetA promoter. Suitably therefore the first or second nucleic acid expresses the viral capsid protein monomers described herein at the same or equal levels. Suitably therefore the heterodimeric capsid protein is expressed at a 1:1 level compared to the functional fusion protein, or the functional molecule. Suitably the nucleic acids may be comprised on one or more vectors. Suitably the first, second and/or third nucleic acids may be comprised on one vector. Alternatively, first, second, and/or third nucleic acids may be comprised on multiple vectors. In one embodiment, the first nucleic acid may be comprised on one vector and the second nucleic acid may be comprised on another vector. Suitably the nucleic acids may be comprised on one or more vectors as constructs. Suitably as expression constructs. Suitably an expression construct in accordance with the invention may comprise a first nucleic acid sequence encoding a first viral capsid protein monomer; and a second nucleic acid sequence encoding a second viral capsid protein monomer attached to a binding molecule. Suitably the expression construct comprises a first promoter operably linked to the first and second nucleic acids. Suitably the expression construct comprises an IRES or ribosome binding site located between the first nucleic acid and the second nucleic acid. Suitably such that the first and second nucleic acids are expressed as separate proteins, suitably as separate monomers. Alternatively, the expression construct comprises a sequence encoding an internal cleavage peptide, suitably a self-cleaving peptide located between the first nucleic acid and the second nucleic acid. Suitably such that once the first and second nucleic acids are expressed as a protein, the protein cleaves into separate monomers. In one embodiment, the first nucleic acid is comprised on a first vector, suitably for example the first vector may comprise a first nucleic acid sequence encoding a woodchuck hepatitis monomer, in such an embodiment, the vector may has a sequence according to SEQ ID NO: 29. In other examples, the first vector may comprise a first nucleic acid encoding a hepatitis B monomer, suitably comprising a sequence according to SEQ ID NO: 20. In one embodiment, the second nucleic acid is comprised on a second vector, suitably for example the second vector may comprise a second nucleic acid sequence encoding a woodchuck hepatitis monomer attached to a binding molecule, suitably a first binding protein, in such an embodiment, the vector has a sequence according to SEQ ID NO:28. .In other examples, the second vector may comprise a second nucleic acid encoding a hepatitis B monomer attached to a binding molecule, suitably a first binding protein. Alternatively, in one embodiment, the first and second nucleic acids may be comprised on the same vector. In one embodiment, the vector has a sequence according to SEQ ID NO: 26. Additionally, the third nucleic acid may be comprises on a second vector. In one embodiment the second vector may comprise a sequence according to SEQ ID NO: 24 or 25. In another embodiment, the first, second and the third nucleic acids may be comprised on the same vector, suitably therefore one vector may encode the VLP of the invention. In one embodiment, the vector may comprise a sequence encoding both woodchuck hepatitis monomers, i.e. a woodchuck hepatitis heterodimer, a first and second binding protein and a functional molecule, suitably the vector has a sequence according to SEQ ID NO: 27. In other examples, the vector may comprise a sequence encoding a both hepatitis B monomers, i.e. a hepatitis B heterodimer, a first and second binding protein and a functional molecule, suitably comprising sequences according to SEQ ID NOs: 18 or 19, and 24 or 25. In one embodiment, the first nucleic acid and the third nucleic acid are comprised on the same vector.. For example, the vector may comprise a nucleic acid sequence according to SEQ ID NO: 20 or 23, and a nucleic acid sequence according to SEQ ID NO: 24 or 25. In one embodiment, the second nucleic acid and the third nucleic acid are comprised on the same vector. In one embodiment, a single vector comprises SEQ ID NO:18 and SEQ ID NO: 24. In one embodiment, a first vector comprises SEQ ID NO:18 and a second vector comprises SEQ ID NO: 24. In one embodiment a single vector copmrpises SEQ ID NO:19 and SEQ ID NO:25. In one embodiment, a first vector comprises SEQ ID NO:19 and a second vector comprises SEQ ID NO: 25. In one embodiment, a single vector comprises SEQ ID NO:21 and SEQ ID NO: 24. In one embodiment, a first vector comprises SEQ ID NO:21 and a second vector comprises SEQ ID NO: 24. In one embodiment, a single vector comprises SEQ ID NO:22 and SEQ ID NO: 25. In one embodiment, a first vector comprises SEQ ID NO:22 and a second vector comprises SEQ ID NO: 25. Suitably the one or more vectors may be comprised in one or more host cells. Suitably the one or more vectors may be comprised in a single host cell. Suitably, for example in the ninth aspect. Alternatively the one or more vectors may be comprised in a two host cells in any combination. Suitably for example in the tenth aspect. Suitably a host cell may comprise any of the above vectors in any combination. Suitably in the process of the ninth aspect, the first, second and/or third nucleic acids may be comprised on one vector or on a first and second vector, or on a first, second and third vector respectively as described above. In one embodiment of the process of the ninth aspect, the first and second nucleic acids are comprised on one vector. Suitably the or each vector is present in the single host cell. In one embodiment of the process of the ninth aspect, the first and second nucleic acids are comprised on a single vector of SEQ ID NO: 26. In one embodiment of the process of the ninth aspect, the first and third nucleic acids are comprised on a single vector. Suitably the single host cell comprises a single vector of SEQ ID NO:26 or 27. In one embodiment of the process of the ninth aspect, the first, second and/or third nucleic acids are comprised on two different vectors. Suitably the first nucleic acid may be comprised on a first vector selected from SEQ ID NO:29. Suitably the second nucleic acid may be comprised on a second vector selected from SEQ ID NO:28. Suitably any workable combination of first and second vectors may be used in the single host cell. For example, the first vector may comprise SEQ ID NO:28 and may be combined with the second vector of SEQ ID NO:29. Suitably in the process of the tenth aspect, the first and second nucleic acids may be comprised on a first vector, or may be comprised on a first and second vector respectively. Suitably the third nucleic acid may be comprised on a third vector. Suitably the first vector and optionally the second vector is present in the first host cell and the third vector is present in a second host cell. In one embodiment of the process of the tenth aspect, suitably the first vector is of SEQ ID NO:29, and the second vector is of SEQ ID NO: 28. Suitably any workable combination of first and second vectors may be used in the host cells. For example, the first host cell may comprise a first vector of SEQ ID NO:28 and may be combined with a second vector of SEQ ID NO: 29. For example, the first host cell may comprise a first vector of SEQ ID NO: 29 and may be combined with a second vector of any of SEQ ID NO: 28. Suitably, the one or more vectors may further comprise the third nucleic acid. Any suitable vector may be used for the chosen host cell/s. Suitable host cells are discussed below. Suitably the vector is selected from: a plasmid, a cosmid, a phage, a virus, an artificial chromosome. Suitably the or each vector is a plasmid. Suitable plasmid vectors for a host E.coli cell may include, for example: pALTER-Ex1, pALTER-Ex2, pBAD/His, pBAD/Myc-His, pBAD/gIII, pCal-n, pCal-n-EK, Cal-c, pCal-Kc, pcDNA 2.1, pDUAL, pET-3a-c, pET-9a-d, pET-11a-d, pET-12a-c, pET-14b, pET-15b, pET- 16b, pET-17b, pET-19b, pET-20b(+), pET-21a-d(+), pET-22b(+),pET-23a-d(+), pET-24a-d(+), pET-25b(+), pET-26b(+), pET-27b(+), pET-28a-c(+), pET-29a-c(+), pET-30a-c(+), pET- 31b(+), pET-32a-c(+), pET-33b(+), pET-34b(+) , pET-35b(+), pET-36b(+), pET-37b(+), pET- 38b(+), pET-39b(+), pET-40b(+), pET-41a-c(+), pET-42a-c(+), pET-43a-c(+), pETBlue-1, pETBlue-2, pETBlue-3, pGEMEX-1, pGEMEX-2, pGEX-1lT, pGEX-2T, pGEX-2TK, pGEX-3X, pGEX-4T, pGEX-5X, pGEX-6P, pHAT10/11/12, pHAT20, pHAT-GFPuv, pKK223-3, pLEX, pMAL-c2X, pMAL-c2E, pMAL-c2G, pMAL-p2X, pMAL-p2E, pMAL-p2G, pProEX HT, pPROLar.A, pPROTet.E, pQE-9, pQE-16, pQE-30/31/32, pQE-40, pQE-60, pQE-70, pQE- 80/81/82L, pQE-100, pRSET, pSE280, pSE380, pSE420, pThioHis, pTrc99A, pTrcHis, pTrcHis2, pTriEx-1, pTriEx-2, pTrxFus. In one embodiment, the vector used is pET-Duet. Suitable plasmid vectors for a host mammalian cell may include: the pSV and the pCMV series of vectors. In one embodiment, the vector used is pcDNA5D. In one embodiment, host mammalian cells are HEK293 cells or CHO cells or derivatives thereof. Suitably if more than one vector is used, it is the same type of vector. Suitably the vector may comprise a variety of other functional nucleic acid sequences, such as one or more selectable markers, one or more origins of replication, multiple cloning sites and the like. Process of Producing a VLP The present invention further relates to processes for the production of VLPs. Two different processes are described herein, one is a single cell process, the other is a process which takes place in two cells and requires mixing of component parts to form the VLP. In accordance with the ninth aspect of the invention, there is provided a single cell process of producing a VLP. In accordance with the tenth aspect of the invention, there is provided a multiple cell process of producing a VLP. Suitably a dual cell process. Suitably the processes may further comprise transfecting the one or more vectors comprising the nucleic acids into the or each host cell. Suitably prior to culturing the or each host cell. Suitably transfection may take place by any suitable method such as electroporation, microinjection, particle delivery, chemical mediated endocytosis, calcium phosphate co- precipitation, or liposome mediated delivery. Suitably culturing the host cells under conditions to express the proteins comprises culturing the host cells under optimum growth conditions. Suitably the optimum growth conditions will vary depending on the host cell being used. Suitably the host cell may be selected from any bacterium, yeast, insect cell or human cell. Suitably the host cell is a bacterial host cell. Suitably the host cell is selected from E.coli, B.subtilis, Caulobacter crescentus, Rodhobacter sphaeroides, Pseudoalteromonas haloplanktis, Shewanella sp. strain Ac10, Pseudomonas fluorescens, Pseudomonas putida, Pseudomonas aeruginosa, Halomonas elongate, Chromohalobacter salexigens, Streptomyces lividans, Streptomyces griseus, Nocardia lactamdurans, Mycobacterium smegmatis, Corynebacterium glutamicum, Corynebacterium ammoniagenes, Brevibacterium lactofermentum, Bacillus brevis, Bacillus megaterium, Bacillus licheniformis, Bacillus amyloliquefacien, Lactococcus lactis, Lactobacillus plantarum, Lactobacillus casei, Lactobacillus reuteri, Lactobacillus gasseri. In one embodiment, the host cell is E.coli. Suitably the E.coli strain is selected from BL21, lemo21, NiCo21, NEB Express, SHuffle, T7 Express, BLR, HMS174, Tuner, Origami2, Rosetta2, m15. In one embodiment, the E.coli strain is BL21(DE3) where the additional genes regulating disulfide formation, dsbC and erv1P, are integrated genomically. Suitably, the genomic integration is within the recAX locus. In an alternative embodiment, the host cell is a human cell, such as a HEK293T cell. Suitably optimum growth conditions comprise culturing at a temperature of 15-25°C. Suitably optimum growth conditions comprise culturing in a medium compatible with bioprocess applications for medicines intended for use in humans, such as chemically defined medium. Suitably optimum growth conditions comprise culturing in an aerated culture medium. Suitably the host cells are cultured to a high density. Suitably to a density OD600 of 4-20. Suitably culturing the host cells under conditions to express the proteins may also comprise inducing the host cells to express the proteins. Suitably inducing the host cells may comprise addition of an inducer into the culture medium, or the creation of certain inducive conditions within the culture medium such as acid/alkali pH, heat shock, hypoxia or the like. Suitably the inducer or inducive condition stimulates transcription of the nucleic acids. Suitably an inducer or inducive condition does so by stimulating an inducible expression control sequence within the nucleic acids. Suitably the inducible expression control sequence may be an inducible promoter. Suitable inducers include isopropyl-β-d-thiogalactoside (IPTG) for lactose driven promoters or tetracycline for tetracycline – regulated promoters. Suitably the host cells are induced to express the proteins once the culture has reached the optimal density described above. Suitably the host cells are induced to express the proteins during logarithmic growth. Suitably the concentration of proteins may be varied by adjusting the concentration of an inducer or altering the inducive conditions to which the host cells are exposed. Suitably the culturing step takes between 4 – 24 hours. Suitably the host cells are induced to express the proteins after 2-6h of culturing or when an OD of 6-8 has been achieved. In a further aspect of the invention, there is provided a cell culture comprising one or more host cells of the ninth or tenth aspects and a culture medium. Suitably a plurality of said cells. Alternatively, the process may not be conducted within one or more cells, and may be conducted in a cell-free system. Suitably in the process of the ninth or tenth aspect, step (a) and/or (b) and/or (c) is conducted within a host cell, to ensure proper production of the VLP. However, suitably steps relating to mixing and forming functionalised viral capsid protein heterodimers; may occur outside of a host cell, in a cell free system. Suitably the processes may further comprise a step of recovering the VLPs. Suitably recovering the VLPs from the host cells. Suitably after the VLPs have been formed. Suitably recovering the VLPs may comprise disrupting the host cells. Alternatively, the host cells may secrete the VLPs into the culture solution. Suitably disrupting the host cells may be carried out by any suitable method such as homogenisation, sonication, or freeze-thaw. Recovery of the VLPs may take place by any suitable method such as filtration, pull-down, centrifugation, or chromatography. Suitably, in an embodiment where the binding molecule comprises a chemical modification, suitably the recovery and purification of VLPs takes place by chromatography. Suitably involving a sequence of steps including mixed mode (hydrophobic interaction and size exclusion) chromatography, anion exchange chromatography, and ultrafiltration. Suitably by anion exchange chromatography. Suitably when anion exchange chromatography is used to recover the VLPs, the VLP may comprise chemical modification, suitably in such an embodiment the first binding protein of the VLP is modified with DEAE. Suitably the DEAE molecules can bind to the chromatography column. Suitably, the recovery and purification of VLPs takes place by affinity chromatography. For example, immobilized metal affinity chromatography (IMAC). Suitably, when affinity chromatography is used to recover the VLPs, the VLP may comprise an affinity tag which is capable of binding to affinity agents used for the affinity chromatography. For example, when immobilized metal affinity chromatography (IMAC) is used the VLP may comprise a metal binding affinity tag, suitably in such an embodiment the first binding protein of the VLP, second binding protein of the VLP and/or a functional protein bound the first and/or second binding protein may comprise an affinity tag. Suitably, the functional protein comprises the affinity tag. Suitably the functional protein is fused to the affinity tag. In such examples, binding of the functional protein to the first and/or second binding proteins can be confirmed by affinity chromatography as the first and/or second binding proteins will be recovered by virtue of binding to the functional protein. “Affinity tag", or “affinity ligand” refers to a short amino acid sequence or peptide enabling a specific interaction with a protein or a ligand, for example in the case of IMAC a metal ion. Examples of affinity tags include biotin, desthiobiotin, histidine, polyhistidine, myc, hemagglutinin (HA), FLAG, fluorescence tag, tandem affinity purification (TAP) tags, FLAG, glutathione S transferase (GST) or derivatives thereof. A suitably affinity tag may comprise or consist of a sequence according to SEQ ID NO: 37. Suitably, in the process of the tenth aspect, step (d) comprises recovering the proteins. Suitably recovering the proteins from the host cells. Suitably recovering the proteins may be performed by similar techniques. Suitably recovering the proteins may comprise disrupting the host cells as above. Alternatively, the host cells may secrete the proteins into the culture solution. Suitably the VLPs form by self-assembly, suitably automatic self-assembly. Suitably once the component proteins are mixed, either within a single host cell as per the ninth aspect or outside of a cell as per the tenth aspect, they will assemble to form VLPs. In respect of the single cell process of the ninth aspect, suitably the step of culturing the host cell further comprises culturing under conditions such that the proteins expressed from the first and second nucleic acids, or from any further nucleic acids, bind to each other. In some embodiments, after the culturing step the binding molecule may be chemically modified. Suitably therefore the method may comprise a step of recovering the proteins, and subsequently chemically modifying the binding molecule. Suitably these steps take place after step (b) but prior to step (c). In some embodiments, the host cell may be cultured under conditions so as to express proteins from the first, second, and third nucleic acids. In one embodiment, the third nucleic acid encodes only a functional molecule. Suitably, in such an embodiment, the binding molecule is chemically modified. In one embodiment, step (c) of the ninth aspect comprises a binding molecule binding to a functional molecule, suitably via a chemical modification. In respect of the two cell process of the tenth aspect, suitably during the culturing step the binding molecule may be chemically modified. Suitably therefore the conditions for culturing the second host cell are such that the binding protein is chemically modified. Suitably such chemical modification of the binding protein may take place post-translationally. Alternatively, the method may comprise a step of chemically modifying the binding protein. Suitably this step takes place after step (d) but prior to step (e). In some embodiments, the host cells may be cultured under conditions so as to express proteins from the first, second, and third nucleic acids. In one embodiment, step (e) comprises each binding protein binding to each functional molecule. Suitably via a chemical modification. In one embodiment, step (e) further comprises mixing under conditions such that the proteins bind to each other. Suitably step (e) comprises mixing host cell supernatants or host cell lysates. Suitably mixing the first host cell supernatant or lysate with the second host cell supernatant or lysate. Suitably the mixing is such that the ratio of first host cell supernatant or lysate to further host cell(s) supernatant or lysate is about 1:1. Suitably the mixing step takes place at room temperature, suitably around 18-22°C. Suitably mixing takes place for between 15 minutes to 2 hours, suitably between 20 minutes and 1 hour, suitably between 25 minutes and 45 minutes, suitably for about 30 minutes. Suitably a functional molecule may be mixed with the VLPs once formed. Immunogenic Composition The present invention further relates to an immunogenic composition comprising the VLP of the invention. Suitably the immunogenic composition may be a vaccine. Suitably the immunogenic composition may further comprise one or more adjuvants. Suitable adjuvants include: mineral salts, emulsions, microorganism derived adjuvants, carbohydrates, cytokines, particulates or tensoactive compounds. Suitable mineral salts include: adjumer, alhydrogel, aluminium hydroxide, aluminum phosphate, aluminium potassium sulphate, amorphous aluminium hydroxyphosphate sulfate (AAHSA), aluminium salts in general, calcium phosphate, Rehydragel HPA, or Rehydragel LV. Suitable emulsions include: Freund’s complete, Freund’s incomplete, montanide ISA720, montanide ISA 51, montanide incomplete, Ribi, TiterMax, AF03, AS03, MF59, specol, SPT, or squalene. Suitable microorganism derived include: cholera toxin or mutants thereof, cholera toxin subunit B, CpG DNA, LTR 192G, MPL, Bordella pertussis components, E.coli heat labile toxin, CTA1-DD gene fusion protein, Etx B subunit, lipopolysaccharides, flagellin, Corynebacterium derived P40, LTK72, MPL-SE, or Ty particles. Suitably the immunogenic composition may further comprise one or more pharmaceutically acceptable excipients. Pharmaceutically acceptable excipients may include stabilizers, fillers, preservatives, diluents, nutrients, antioxidants, antimicrobial agents, buffers, solvents, inactivating agents, purifiers, emulsifiers, surfactants and the like. Suitable excipients may be selected from, for example: monosodium glutamate, sucrose, D- mannose, D-fructose, dextrose, human serum albumin, potassium phosphate, plasdone C, anhydrous lactose, microcrystalline cellulose, polacrilin potassium, magnesium stearate, cellulose acetate phthalate, alcohol, acetone, castor oil, sodium chloride, benzethonium chloride, formaldehyde, ascorbic acid, hydrolyzed casein, sodium bicarbonate, sodium carbonate, glutaraldehyde, 2-phenoxyethanol, polysorbate 80 (Tween 80), neomycin, polymyxin B sulfate, bovine serum albumin, neomycin sulfate, polymyxin B, yeast protein, streptomycin sulfate, ammonium thiocyanate, rice protein, lactose, formalin, amino acid supplement, phosphate-buffered saline solution, disodium phosphate dihydrate, sodium dihydrogen phosphate dihydrate, yeast DNA, deoxycholate, phosphorothioate linked oligodeoxynucleotide, dibasic dodecahydrate, monobasic dehydrate, L-histidine, sodium borate, sodium taurodeoxycholate, ovalbumin, sorbitan trioleate, sodium citrate dehydrate, citric acid monohydrate, kanamycin, barium, hydrocortisone, egg proteins, cetyltrimethylammonium bromide (CTAB), octoxynol-10 (TRITON X-100), α-tocopheryl hydrogen succinate, gentamicin sulfate, monobasic sodium phosphate, dibasic sodium phosphate, cetyltrimethlyammonium bromide, and β-propiolactone, Thimerosal, α-tocopheryl hydrogen succinate, hydrolyzed porcine gelatin, arginine, dibasic potassium phosphate, monobasic potassium phosphate, protamine sulfate , sodium metabisulphite, Vero cell protein, CRM197 protein, vitamins, bovine calf serum, urea, succinate buffer, isotonic saline solution, phenol, M-199 medium, chicken protein, polygeline, chlortetracycline, dextran, Dulbecco’s Modified Eagle Medium, magnesium sulfate, ferric (III) nitrate, L-cystine, L-tyrosine, sorbitol, xanthan, water, EDTA, dioleoyl phosphatidylcholine (DOPC), 3-O-desacl4’monophosphoryl lipid A (MPL), QS-21, and cholesterol. In one embodiment, the excipients may be arginine, glutamine and trehalose. Suitably the immunogenic composition is formulated as a fluid, suitably as a liquid. Suitably the excipients and additives are selected such that the formulation is a liquid. Suitably an injectable liquid. Immunogenicity The term “Immunogenic" means that a VLP or an immunogenic composition comprising the VLP of the invention is capable of eliciting an immune response in a subject. Suitably a potent and preferably a protective immune response in a subject. Thus, the VLP or an immunogenic composition comprising the VLP of the invention may be capable of generating an antibody response in a subject and/or a non-antibody based immune response in a subject. Suitably this may be referred to as its immunogenic activity. Suitably the immunogenic activity of the VLP or an immunogenic composition comprising the VLP of the invention may be determined by the amount of antibodies present in a subject after administration of the VLP or an immunogenic composition comprising the VLP of the invention i.e. antibody production. Suitably the amount of antibodies which bind to the antigen of the VLP. Suitably the amount of antibodies present in a subject after administration of the VLP or an immunogenic composition comprising the VLP of the invention, i.e. antibody production, is sustained and consistent over a period of time. Suitably the immunogenic activity of the VLP or an immunogenic composition comprising the VLP of the invention may be determined by the amount of antibodies present in a subject after administration of the VLP or an immunogenic composition comprising the VLP of the invention over a given period of time, i.e. antibody production over a given period of time. Suitable periods of time are outlined below. By amount of antibodies it is meant the titre or concentration thereof. Suitably the concentration of antibodies in sera. Suitably a VLP or an immunogenic composition comprising the VLP of the invention may sustain immunogenic activity for at least 5 days, at least 10 days, at least 15 days, at least 20 days, at least 25 days, at least 30 days, at least 35 days, at least 40 days, at least 45 days, at least 50 days, at least 55 days, at least 60 days, at least 65 days, at least 70 days, at least 75 days, at least 80 days, at least 85 days, at least 90 days, at least 95 days, or at least 100 days or more in a subject. Suitably a VLP or an immunogenic composition comprising the VLP of the invention may sustain immunogenic activity for at least 110 days, at least 120 days, at least 130 days, at least 140 days, at least 150 days, at least 160 days, at least 170 days, at least 180 days, at least 190 days, at least 200 days, at least 210 days, at least 220 days, at least 230 days, at least 240 days, at least 250 days, at least 260 days, at least 270 days, at least 280 days, at least 290 days, at least 300 days or more in subject. Suitably a VLP or an immunogenic composition comprising the VLP of the invention may sustain immunogenic activity for at least 1 week, at least 2 weeks, at least 3 weeks, at least 4 weeks, at least 5 weeks, at least 6 weeks, at least 7 weeks, at least 8 weeks, at least 9 weeks, at least 10 weeks, at least 12 weeks, at least 14 weeks, at least 16 weeks, at least 18 weeks, at least 20 weeks days or more in a subject. Suitably a VLP or an immunogenic composition comprising the VLP of the invention may sustain immunogenic activity for at least at least 30 weeks, at least 40 weeks, at least 50 weeks, at least 60 weeks, at least 70 weeks, at least 80 weeks, at least 90 weeks, at least 100 weeks or more in a subject. Suitably a VLP or an immunogenic composition comprising the VLP of the invention may sustain immunogenic activity for at least for at least 1 year, at least 2 years at least 3 years, at least 4 years, at least 5 years, at least 6 years, at least 7 years, at least 8 years, at least 9 years or at least 10 years or more in a subject. Suitably, a VLP or an immunogenic composition comprising the VLP of the invention may sustain immunogenic activity for at least 10 years, for at least 15 years, for at least 20 years, for at least 25 years, for at least 30 years, for at least 35 years, for at least 40 years, for at least 45 years, for at least 50 years or more in a subject.. Suitably wherein immunogenic activity may refer to immunogenic antibody production. Suitably antibody production at a concentration which is immunogenic. Suitably antibody production at a concentration in sera which is immunogenic. Suitably at a concentration of between 1-20 ^g/ml, 1-18 ^g/ml, 1-16 ^g/ml, 1-14 ^g/ml, 1-12 ^g/ml, 2-18 ^g/ml , 2-16 ^g/ml , 2- 14 ^g/ml, 2-12 ^g/ml, or 2 – 10 ^g/ml in sera for example. The skilled reader, on considering the information set out in the Examples, will recognise that the VLPs or the immunogenic compositions of the invention exhibit immunogenic activity that makes them well suited to therapeutic use in the manner described in this specification. Medical Uses The present invention further relates to use of the VLP or the immunogenic composition comprising the VLP for use in therapy, or in the prevention and/or treatment of a disease. In a further aspect, the present invention further provides a method of treating a subject having a disease, comprising administering an effective amount of a VLP according to the first aspect or an immunogenic composition according to the twelfth aspect, to the subject. In further aspect, the present invention further provides a method of manufacturing a medicament for the treatment of a disease, the medicament comprising an effective amount of a VLP according to the first aspect or an immunogenic composition according to the twelfth aspect. Suitably the disease may be selected from: an infectious disease, cancer, an autoimmune disease, a cardiovascular disease, a metabolic disease, an inflammatory disease, a neurological disease, or rheumatological degenerative disease, or an addiction. Suitable infectious diseases include: viral, bacterial, fungal, or protozoan infections. Suitable viral infections include: COVID-19, SARS, MERS, influenza, common cold, respiratory syncytial virus infection, adenovirus infection, parainfluenza virus infection, norovirus infection, rotavirus infection, astrovirus infection, measles, mumps, rubella, chickenpox, shingles, roseola, smallpox, fifth disease, chikungunya virus infection, HPV infection, Hepatitis A, B, C, D or E, warts, herpes, molluscum contagiosum, ebola, lassa fever, dengue fever, yellow fever, Marburg hemorrhagic fever, Crimean-Congo hemorrhagic fever, polio, viral meningitis, viral encephalitis, rabies, zika virus infection, west nile virus infection, HIV/AIDS, Hantavirus infection, HPS. Suitable bacterial infections include: urinary tract infections, cystitis, impetigo, bacterial food poisoning, campylobacteriosis, C.difficile infection, bacterial cellulitis, MRSA, CRPA, VRSA, sepsis, erysipelas, necrotising fasciitis, bacterial folliculitis, gonorrhoea, chlamydia, syphilis, mycoplasma genitalium, bacterila vaginosis, pelvic inflammatory disease, tuberculosis, whooping cough, Haemophilus influenzae disease, pneumonia, bacterial meningitis, lyme disease, cholera, botulism, tetanus, anthrax, Cryptosporidiosis, Diphtheria, E. coli infection, Legionnaires Disease, Leptospirosis, Listeriosis, salmonella infections, Shigellosis gastroenteritis, Staphylococcal infections, Streptococcal infections, TSS, typhoid fever, Yersenia infection. Suitable cancers include: breast cancer, liver cancer, lung cancer, pancreatic cancer, brain cancer, prostate cancer, bowel cancer, rectal cancer, bone cancer, leukemia, bladder cancer, cervical cancer, endometrial cancer, eye cancer, retinoblastoma, ewing sarcoma, gallbladder cancer, head and neck cancer, kaposi’s sarcoma, kidney cancer, laryngeal cancer, mesothelioma, myeloma, lymphoma, ovarian cancer, oesophageal cancer, mouth cancer, nasopharyngeal cancer, nose and sinus cancer, skin cancer, sarcoma, stomach cancer, testicular cancer, thyroid cancer, uterine cancer, vaginal cancer, penile cancer, vulval cancer. Suitable autoimmune diseases include: asthma, psoriasis, MS, rheumatoid arthritis, reactive arthritis, lupus, inflammatory bowel syndrome/disease, type 1 diabetes, Guillain-Barre syndrome, demyelinating polyneuropathy, Graves’ disease, Hashimo’s thyroiditis, Myasthenia gravis, vasculitis, pernicious anemia, ulcerative colitis, antiphospholipid syndrome, Kawasaki disease, alopecia, vitiligo, scleroderma, Sjogren’s syndrome, crohn’s disease, coeliac disease, Addison’s disease, narcolepsy. Suitable cardiovascular diseases include: angina, heart attack, heart failure, coronary heart disease, stroke, transient ischemic attack, peripheral arterial disease, aortic disease, atherosclerosis, hypertension, cerebrovascular disease, renal artery stenosis, aneurysm, cardiomyopathy, pulmonary heart disease, arrythmia, dysrhythmia, endocarditis, cardiomegaly, myocarditis, valvular heart disease, congenital heart disease, rheumatic heart disease. Suitable metabolic diseases include: hypercholesterolemia, hypertriglyceridemia, diabetes, hyperlipidemia, hyperbilirubinemia, hypercalcemia. Suitable inflammatory diseases may include any of the above infections or autoimmune diseases. Suitable inflammatory diseases may include include: arthritis, asthma, tuberculosis, periodontis, chronic ulcers, sinusitis, hepatitis, glomerulonephritis, inflammatory bowel syndrome/disease, preperfusion injury, transplant rejection, sickle cell disease, allergies, cardiovascular disease, psoriasis, cytokine-mediated pruritus, COPD, diabetes, bronchitis, Crohn’s disease, atherosclerosis, dermatitis, arteritis, lupus. Suitable neurological diseases include: Alzheimer’s, ataxia, ALS, Bells palsy, brain tumours, aneurysms, epilepsy, Guillain-Barre syndrome, hydrocephalus, Meningitis, MS, muscular dystrophy, neurocutaneous syndromes, Parkinson’s, migraines, encephalitis, myasthenia gravis, dementia, seizures, spinal muscular atrophy, motor neuron disease, scoliosis, neuropathy, chronic fatigue syndrome, cerebal palsy. Suitable rheumatological degenerative diseases include: rheumatoid arthritis, psoriasis arthritis, spondylarthropathy, osteoarthritis, lupus, systemic sclerosis. Suitable addictions include: alcohol, nicotine, caffeine, amphetamines, opioids, sedatives, hypnotics, anxiolytics, cocaine, cannabinoids, hallucinogenics, phenycylcidine. In one embodiment, the VLP or the immunogenic composition are for use in the prevention or treatment of COVID-19. Suitably in such an embodiment, the functional molecule may be a SARS-CoV-2 antigen, suitably a SARS-CoV-2 spike protein. Alternatively in such an embodiment, the functional molecule may be an inflammatory cytokine, suitably IL-33. In one embodiment, the VLP or the immunogenic composition are for use in the prevention or treatment of psoriasis or arthritis. Suitably in such an embodiment, the functional molecule may be an inflammatory cytokine, suitably IL17. In one embodiment the VLP or the immunogenic composition are for use in the prevention or treatment of asthma or atopic dermatitis. Suitably in such an embodiment, the functional molecule may be an inflammatory cytokine, suitably IL13 or IL33. Suitably, an effective amount for administration to the subject is an effective amount to prevent or treat the disease. Suitable effective amounts can be readily determined by the skilled medical practitioner. Suitably a dose comprises an effective amount. A suitable dose of the VLP may comprise: 10- 100 micrograms, suitably 10-80 micrograms, suitably 20-60 micrograms, suitably 20-40 micrograms. Suitably the VLP or immunogenic composition may be administered by any route. Suitably the VLP or immunogenic composition may be administered enterally or parenterally. Suitably the VLP or immunogenic composition may be administered orally, rectally, vaginally, sublingually, by injection, transdermally, or by inhalation. In one embodiment, the VLP or immunogenic composition may be administered by injection, suitably by subcutaneous injection. In one embodiment, the VLP or immunogenic composition may be administered by inhalation, suitably by nasal inhalation. Subject The present invention relates to the prevention and/or treatment of a disease in a subject by using the VLP or immunogenic composition thereof. Suitably the subject may be human or animal. Suitably therefore the prevention and/or treatment of disease may be in the veterinary field. Suitably the subject may be adult or child. Suitably the subject may be male or female. In one embodiment, the subject is an adult human. Suitably the subject may have been diagnosed with a disease. Alternatively, the subject may be suspected of having a disease. Suitably the subject may display one or more symptoms of a disease. Alternatively, the subject may be at risk of contracting a disease. Suitably the subject may have one or more risk factors associated with a disease. Suitable risk factors may include: weight, smoking, alcohol or substance addiction, age, sex, race, inheritance for example. Suitable risk factors may further include a genetic predisposition to a disease, for example by expression of particular gene, or by the presence of a particular mutation in a gene. In one embodiment, subjects that have been diagnosed with a disease or who have one or more symptoms of a disease are provided with the VLP or immunogenic composition for treatment of the disease. In one embodiment, subjects that are at risk of developing a disease are provided with the VLP or immunogenic composition for prevention of the disease. Other Uses The present invention further relates to use of the VLP in research and in the diagnosis of diseases. Suitably the VLP of the first aspect may be used in research. Suitably the VLP may be used as a detection tool. Suitably the VLP may be used as a label. Suitably in such embodiments, the binding molecule of the VLP is attached to a functional molecule which is a fluorescent molecule. Suitably the binding molecule may be attached to a functional molecule which is an antigen binding molecule such as an antibody. Suitably, the functional molecule may further comprise a fluorescent molecule. Suitably the antigen binding molecule may specifically bind a cell surface receptor. Suitable cell surface receptors are discussed elsewhere herein, however suitably the cell surface receptor is specific to a cell type. Suitably therefore the VLP is capable of binding to, and labelling, specific cell types. Suitably the VLP may be used as a carrier. Suitably in such embodiments, the VLP may comprise a cargo. Suitably the cargo may be contained within the VLP, suitably within the VLP shell. Suitably the cargo may be a therapeutic molecule. Suitably therefore the VLP may not in itself be a therapeutic, but may be a carrier of a therapeutic molecule. Suitable therapeutic molecules may include oligonucleotides, small molecules, peptides, for example. In one embodiment, the therapeutic molecule may comprise an antisense oligonucleotide which may act to repress expression of a particular nucleic acid. In another embodiment, the therapeutic molecule may comprise a cytotoxic chemical which may act to trigger cell death. Suitably, in such embodiments, the VLP is targeted to a particular site, for example to a particular cell or cell type where the therapeutic molecule is required. Suitably this is achieved by the binding molecule of the VLP being attached to a functional molecule which is an antigen binding molecule such as an antibody. Suitably the antigen binding molecule may specifically bind to a cell surface receptor. Suitably to a cell surface receptor specific to the target cell. Suitably binding to the cell surface receptor may stimulate uptake of the VLP into the cell. Suitably therefore, the VLP is capable of binding to specific cell types and delivering cargo thereto. In a further aspect of the invention, there is provided a carrier VLP comprising the features of the first aspect, and in addition a cargo, wherein the cargo is contained within the VLP shell. Suitably the cargo is a therapeutic molecule. Suitably the VLP of the first aspect may also be used in diagnosis. Suitably the binding molecule of the VLP is attached to a functional molecule which is an antigen binding molecule, such as an antibody. Suitably the antibody specifically binds an antigen derived from a disease causing agent as discussed hereinabove. Suitably from an infectious agent such as a virus, bacterium, fungus, protozoan, or archaeon. Suitably, therefore, the VLP is capable of binding to a disease causing agent and allowing detection thereof. Suitably therefore the VLP of the invention may be used in a method of diagnosing a disease in accordance with the sixteenth aspect of the present invention. Suitably there is provided a method of diagnosing a disease in a subject comprising: (a) Providing a virus like particle according to the first aspect of the invention, wherein the binding molecule is attached to a functional molecule and wherein the functional molecule is an antibody directed towards an antigen derived from a disease causing agent; (b) Mixing the virus like particle with a suitable sample from the subject; (c) Detecting whether the virus like particle precipitates; (d) Diagnosing the presence of a disease if the VLP precipitates. Suitably, in an embodiment where the functional molecule is an antigen binding molecule, the VLP further comprises a second binding protein. The second binding protein is described elsewhere herein. Suitably the antigen binding protein is attached to the second binding protein. Suitably the second binding protein binds to the first binding protein which is attached to a monomer of the heterodimeric capsid protein as described hereinabove. Suitably detection is via precipitation of the VLP bound to the disease causing agent. Suitably detecting precipitation may comprise visual confirmation, or testing with a spectrometer. Suitably if no precipitation occurs, the disease is not present. Suitably, the VLP may also comprise a fluorescent molecule. Suitably such a fluorescent molecule may be attached to a chemical modification of the binding molecule. In such embodiments, suitably the detection step may comprise detecting the presence of fluorescence in the sample. Suitably the detection step may comprise detecting the presence of fluorescent precipitation in the sample. Suitably diagnosing the presence of a disease if fluorescent precipitation occurs. Advantageously, the use of fluorescence allows more sensitive detection of the precipitation in a sample. A suitable sample from a subject may be a blood sample, saliva sample, serum sample, sputum sample, sperm sample, mucus sample, CSF sample. Suitably the sample is a fluid sample. Suitably the method of diagnosis may further comprise a step of incubating the sample with the VLP. Suitably for a period of time sufficient to allow the VLP to bind to any antigens in the sample and precipitate. Suitably for at least 1 minute, suitably up to 30 minutes, suitably up to 25 minutes, suitably up to 20 minutes, suitably up to 15minutes. Suitable diseases which may be detected by the method may be any of those listed herein above. Suitably the method of diagnosis may further comprise a step of treatment of the subject if a disease is diagnosed. Suitably treatment of the subject may comprise administering an effective amount of any known treatment for the relevant disease to the subject. Certain embodiments of the invention will now be described with reference to the following examples: Examples Materials and Methods The invention disclosed here enables the production of VLP vaccines in the hepatitis VLP shell where only one protein is presented for each of the VLP-dimers, as shown in Figure 2 (image on the right). This was achieved by introducing specific mutations into the amino acid sequence of the VLP shell protein. Since the monomers shown in Figure 2 are in fact the same protein bound together through self-interaction, this interaction can be weakened if amino acids are introduced which have a positive or negative charge, thereby creating electrostatic repulsion. The inventors have reasoned that this can be exploited to produce heterodimeric viral capsid proteins by introducing the gene for the VLP shell protein into a vector allowing protein synthesis for example in bacteria such as E.coli. This is summarized in Figure 3. Testing of mutational effects: The inventors exploited the recent publication of Alphafold2, more specifically, Alphafold2 Advanced (available at https://colab.research.google.com/github/sokrypton/ColabFold /blob/main/beta/AlphaFold2_a dvanced.ipynb) This algorithm allows the accurate modelling of structures of protein pairs where the quality of predicted folding can be the pTM score rather than the pLDTT score which returns modelled protein structures ranked by the protein-protein interaction. The stoichiometry of interacting subunits is specified as x:y:z where ‘x’ is the predefined number of molecules of protein 1, ‘y’ the number of protein 2 molecules, and so forth. In the case of Hepatitis capsid modelling, the so-called asymmetric unit, which gives rise to the building blocks automatically assembling into the entire capsid, contains two dimers of one single protein, which would be modelled by simply specifying a number of ‘4’ for the capsid protein. This returns a structure of two dimers. Once mutations are introduced, two different proteins are derived from the original wild type capsid protein: one protein which contains a binding protein (such as Im7 or Barstar), and a second protein which does not. When the stoichiometry for these two proteins is defined as “2:2” it means that Alphafold2 is going to return a protein complex which contains 2 molecules of each protein. As expected, Alphafold2 returned two dimers which were in turn positioned exactly as in the published Hepatitis virus asymmetrical unit structure (PDB: 6EDJ). Furthermore, the structures in each case as such were classified as ‘high predictive accuracy’ (Alphafold2 colouring index), with the predicted exception of unfolded domains (glycine serine linkers, and histidine-containing tags). This result confirms the operational accuracy of this modelling approach. Upon introducing a series of mutations, Alphafold2 was then interrogated and returned models consisting of either (i) dimers that were either composed of 2x protein 1 and 2x protein 2 (homodimers only), (ii) dimers that exclusively consisted of protein 1 and protein 2 (heterodimers only), or (iii) a mixture of both. This in silico approach allowed the iterative testing and identification of mutational combinations triggering the exclusive assembly of heterodimer structures, as detailed in the examples below. In each case, both pDLL and pTM scores for the structures were high, confirming a high predictive capacity, as shown below in the Table. Alphafold2 structure prediction of dimer formation generated by the optimized sequences shown in table 2. Model rank Dimer pLDDT score pTM score arrangement wHv – Im7 1 hetero 81.5 0.60 2 hetero 75.8 0.59 3 hetero 78.6 0.52 4 hetero 72.2 0.51 5 hetero 68.4 0.47 wHv Bs 1 hetero 78.7 0.55 2 hetero 81.1 0.51 3 hetero 74.4 0.45 4 hetero 72.1 0.44 5 homo 75.4 0.42 Example 1: Dimerisation of Woodchuck Hepatitis virus capsid proteins In this example, instead of using the VLP shell from Hepatitis B virus (HBc), the groundhog hepatitis (Woodchuck hepatitis virus, (wHv)) was used. Structurally, both virus capsids are extremely similar. However, compared to HBc, wHv has distinct advantages: i) It forms capsids at cold temperatures (> 60% capsid formation occurs at temperatures as low as 4°C, Kukreja2014). This will increase the yield of VLPs in low temperature bacterial fermentation which is preferable for production of complex proteins. (ii) The temperature dependence on capsid formation is much weaker: Since the virus is adapted to groundhogs which hibernate and whose body temperature wildly fluctuates between 6.5°C and 37°C, VLPs from wHv are much more stable during temperature fluctuation. This could be a significant advantage both for manufacture and storage. (iii) Use of wHv abrogates any cross-reactivity to human Hepatitis B. The precludes even the theoretical possibility that having had a past infection with Hepatitis in some way interferes with the response to vaccination with the VLP vaccine. When both the wild type wHv protein and the wHv protein carrying an integrated Im7 protein are produced by bacteria, they can form dimers in two ways: either the two unmodified (called “wild type”) proteins together (called a “homodimer”) or one unmodified and one Im7-carrying protein (called “heterodimer”). The interaction itself is affected by the interaction of electrically charged amino acids within the protein. This is shown in Figure 3B (right). The negatively charged amino acid called E64 from one of the monomers interacts with a positively charged amino acid called K96 from the other monomer. Figure 3 shows the approach to creating a mutant wHv capsid where one dimer displays an integrated Im7 protein (marked as ‘Im7-insert’) toward the VLP surface. A. an expression vector is established which allows simultaneous expression of a wild type wHv protein and a wHv protein carrying the integrated Im7 protein, driven by a single promoter, through an internal ribosome binding site (RBS). This set-up can result in either formation of homodimers or heterodimers. B. The central ‘tip’ of a wHv homodimer, of amino acid making up the protein, as well as a close-up view of electrostatic forces between charged amino acids from both monomers (right). Example 2: modified wHv protein This electrostatic interaction between the monomers can be modified. An example of such a modification is; if a positively charged amino acid, for example K96, is replaced by a negatively charged amino acid, then the protein which is usually forms a dimer with itself (homodimer), experiences electrostatic repulsion (E64 now meets position 96, now mutated from K to E). However, if the K96->E replacement on the protein is accompanied with a complementary replacement of E64->K placed on the corresponding monomer of wHv-Im7, then whenever one wHv monomer and one wHv-Im7 monomer form a dimer (“heterodimer”) this interaction is strengthened by an electrostatic attraction. This is illustrated in Figure 4a. The Alphafold2 software (Jumper, J et al. Nature (2021) and Varadi, M et al. Nucleic Acids Research (2021)) allows accurate prediction of protein structures that will be formed from any given amino acid sequence. When the above mutated protein sequences were entered into Alphafold2, it turned out that- despite the added electrostatic forces, surprisingly the formation of homodimers is still highly favoured, as shown in Figure 4B. Figure 4 shows interaction of wHv capsid protein monomers with exemplary mutations in their amino acid sequences. Panel A shows a schematic of an exemplary expression vector showing that complementary mutations are introduced into the two different monomers: K96E in wHv-Im7 and E64K into wHv, respectively. Panel B shows structural prediction using Alphafold2 database, showing that formation of homodimers composed of wHv/wHv and wHv- Im7/wHv-Im7, respectively, is still favoured despite the mutations introduced (shown is the top-ranked of five models, all of which show homodimer formation). This suggests that the mutations introduced into the amino acid sequences of the monomers to promote formation of heterodimers are not trivial. In order to overcome this problem, the inventors derived and introduced additional mutations as further refinements. These are illustrated below in Figure 5 and Figure 6. In each case, despite the increased electrostatic bias toward formation of wHv- wHv-Im7 heterodimers, still the desired effect could not be achieved. In the example in shown in figure 5, lysine96 in wHv is replaced by aspartate (D96), instead of glutamate (E96) in contrast to model shown in figures 3 and 4. Panel A (of figure 5) shows a schematic of an exemplary expression vector showing that complementary mutations are introduced into the two different monomers: K96D in wHv-Im7 and E64K into wHv, respectively. The mutation of K96 to D96 reduces side-chain bulkiness, shown on the left of panel B. The resulting structural prediction using Alphafold2 database (right) shows a predicted mixture between heterodimer and homodimer formation. In the example shown in Figure 6, further additional intra-chain ionic stabilization was achieved by added mutation of Lysine 67 to glutamate in the wHv149 subunit. Panel A shows a schematic of an exemplary expression vector showing that complementary mutations are introduced into the two different monomers: K96D in wHv-Im7 and E64K into wHv, respectively, in this example, an addition mutation K67E is introduced to the wHv149 subunit. Surprisingly, this set of mutations resulted in increased heterodimer formation, as predicted by Alphafold2 (shown in panel B). Overall, these experiments confirm that exclusive formation of heterodimers is difficult to achieve, cannot be easily predicted based on single electric charge changing mutations, and hence is non-trivial. Example 3: mutations in wHv protein promote heterodimer formation The inventors found that certain combinations of mutations in amino acid sequence of the monomers combined with a specifically required linkers to join the wHv and the binding molecule, in this example Im7, as well as Barstar proteins, achieved the desired result of heterodimeric capsid proteins. This final, optimized, combination of mutations is summarized in Table 2. The analysis using Alphafold2 yielded very high statistical scores, indicating that the structures have a high predictive probability of forming the desired heterodimers, as shown in Table 3. In figure 7, shows the Ribbon diagram of the top rated structures obtained with the optimized engineered combination of mutations summarized in table 2, generated using Alphafold2, for heterodimers consisting of wHv149/wHv-Im7 (top) and wHv149/wHv-Bs (bottom). Despite the mutations, a structural overlay of the unmodified wHv protein with the resulting heterodimer mutant proteins, shows that they are almost completely identical in structure, as shown in Figure 8. This suggests that they will be able to form intact VLPs. In addition, figure 9 shows a space filling model generated using icn3d (NCBI/structure; PDB: 6edj), showing the asymmetric units of wild type wHv capsid (left) and the designed wHv149/wHv-Im7 (centre) and wHv149/wHv-Barstar (right) heterodimers, respectively, from the front (top) and from the surface (bottom) of the capsid. The dashed line indicates the plane of subunit interaction leading to VLP assembly, which remains undisturbed by the integration of Im7 or Barstar. A comparison to the unmodified wHv protein structure suggests that the space occupancy of the mutated structures will not interfere with VLP formation. The examples shown in figure 10 shows a view from the side showing “spike” made from two helices from each monomer protruding to the outside (arrow) and bottom part mediating interaction with other dimers in the capsid ( arrow). Also shown is a top view of the HBc capsid protein: “homodimer” composed of two identical HBc monomer proteins. Figure 11 highlights the a total of four conserved electrostatic interactions in all hepatitis virus (including HBc / wHv) wild type capsid proteins. Protein alignment of capsids from human and woodchuck hepatitis virus showing conservation of E8, R56, E64, K96, mediating conserved electrostatic binding. Interestingly, all four sites become electrostatic repulsed while, when pairing with the complementary mutations inserted into the functionalized monomer, regain electrostatic attraction. For instance, E64 of each monomer interacts with K96 of the other monomer and E8 of each monomer interacts with R56 of the other monomer. Example 4: wHv capsid heterodimer components are soluble and evenly expressed in E.coli. Method: A pET – derived plasmid harbouring DNA encoding the wHv_Im7 and wHv proteins, each under the control of a separate T7-inducible promoter, was transfected into standard BL21/DE3 E.coli. Recombinant proteins were induced by addition of IPTG to 0.3 mM and incubation at 16C for 16h. Subsequently, cells were lyzed by sonication and insoluble proteins and inclusion bodies separated by centrifugation. The resulting cytosolic fractions were subjected to denaturing SDS-PAGE (shown in figure 12). The data shown in the SDS-PAGE gel shows that both wHv_Im7 and wHv proteins, when driven by individual T7 promoters, can be expressed as soluble proteins in E.coli and are synthesized at approximately even stoichiometric ratios (black and grey arrows). Example 5: HBc capsid heterodimer and binding protein form a complex and co-purify on immobilized metal affinity chromatography. Method: A pET – derived plasmid harbouring DNA encoding the HBc_Im7 and HBc_wt proteins, each under the control of a separate T7-inducible promoter, was transfected into standard BL21/DE3 E.coli. Recombinant proteins were induced by addition of IPTG to 0.3 mM and incubation at 16C for 16h. A separate plasmid was transfected harbouring the binding protein ColE7-IL31 under the control of a tetracycline-inducible promoter. Recombinant protein expression was induced by adding 40 ng/ml of anhydrotretracyline at 16C for 16h. Subsequently, cells were lyzed by sonication and insoluble proteins and inclusion bodies separated by centrifugation. The resulting cytosolic fractions of cells expressing HBc_Im7/ HBc_wt and ColE7-IL31 were mixed at room temperature for 30min, followed by purification on Ni-NTA agarose and subsequent SDS-PAGE analysis of the individual fractions (shown in figure 13). The data shown in the SDS-PAGE gel HBc_Im7 and HBc_wt proteins, when driven by individual T7 promoters, can expressed as soluble proteins in E.coli and, furthermore, that they form a complex with the binding protein ColE7-Il31 which co-purifies on Ni- chromatography, confirming formation of stable complexes (white, dark, and light grey arrows, respectively in the eluate lane). Example 6: wHv heterodimeric VLPs can be expressed and autoassemble into large nanoparticles in E.coli, and co-purify on immobilized metal affinity chromatography. Methods: Cloning, expression, density gradient: the epitope protein used was murine Interleukin 31 harbouring a single point mutation to inactivate receptor transactivation (SEQ ID NOs: 35 and 36). The epitope was N-terminally fused to Colicin E7 (SEQ ID NOs: 31 and 32) and connected via a rigid alpha helical linker (SEQ ID NOs: 33 and 34)), these proteins and VLP scaffold proteins were cloned onto plasmid DU75351 (SEQ ID NO:30) into BL21/DE3 E.coli. Transfected cells were inoculated into LB broth overnight at 30 °C, followed by expansion into 200ml medium the next morning at 37°C in shaker flasks. Upon reaching of OD595 of 0.8, temperature was reduced to 16°C. The scaffold protein was under the control of a T7 promoter and induced with 0.3 mM IPTG. The epitope protein was under the control of a tetA/tetR promoter and induced with 40 ng/ml anhydrotetracycline. Induction was maintained for 3h. Biomass was harvested and lysed in 25mM Tris, pH 7.4, 200mM NaCl using a high pressure homogenizer (Emulsiflex). Thereafter, lysates were digested with Benzonase for 1h and Polysorbate 80 was added to 0.005%. Lysates were spun down for 10’ at 25000 rpm and supernatants filtered through 0.45 and 0.22 micron filters, respectively, to yield cytosolic fractions. Cytosols were applied to a discontinuous sucrose gradient in the same buffer and spun for 6h at 255,000G with deactivated deceleration. Individual sucrose fractions were analyzed by SDS PAGE. Immobilized metal affinity chromatography (IMAC): Cytosolic fractions of heterodimeric VLPs decorated with epitope protein were prepared as detailed in the Methods for Figure 1. Cytosols were adjusted to 30mM imidazole, followed by IMAC chromatography on a Sartobind IDA 1ml membrane (Sartorius) charged with Nickel-Sulfate. After adsorption, membrane was washed with the same buffer containing 70mM imidazole. Bound protein was eluted with 250mM imidazole and fractions analyzed by SDS PAGE. Results: The data shown in Figure 14 confirms that heterodimeric VLPs can be expressed and autoassemble into large nanoparticles in E.coli. The data also confirms that these heterodimeric VLPs can be decorated fully with epitope protein on the surface. The data in Figure 15 shows that both the WHcIm7 (grey arrow) and the WHc protein (black arrow) co- purify on IMAC, confirming that the VLP scaffold proteins are indeed both bound to the epitope. The staining density of epitope protein (white arrow) and WHcIm7 moiety (grey arrow) is approximately even, indicating that the VLPs are fully decorated with epitope protein. Example 7: Determination of Size of VLPs. Methods: Dynamic Light Scatter analysis: The eluate fraction shown in Figure 15 was subjected to a Multiangle Dynamic Light Scatter analysis (MADLS) using a Malvern Zetasizer Ultra in a quarz microcuvette with 80 microlitre volume. Transmission electron microscopy (TEM): the samples shown in Figure 15 were adsorbed to glow discharged carbon-formvar-coated copper grids and negatively stained with a 1% aqueous uranyl acetate. The grids were examined at 80 kV. Results: The light scattering profile shown in Figure 16 confirms a uniform size distribution of the VLP particles at the expected size range (approximately 32 nm diameter). The TEM images in Figure 17 confirm the size of VLPs determined by DLS analysis in Figure 16. The thickened rim structure and fuzzy outer rim appearance is consistent with decoration of an epitope localized to the surface.

Table 1. Genetic mutations introduced into wHv subunits failing to achieve tight heterodimer formation. 1 Alphafold2 structure prediction using pTM score ranking and 5 models for each analysis. ‘Hetero’ - the top three ranked models showed heterodimer formation; ‘mixed’ - the top ranked model showed heterodimer. * failure to form tight dimer of dimers.

Table 2 Table 3 Table 3 shows the top-ranked model structures produced with the optimized combination of mutations summarized in Table 2 are shown in Figure 7. The analysis using Alphafold2 yielded very high statistical scores, indicating that the structures have a high predictive probability, as shown in Table 3. These data confirm that achieving heterodimer formation in wHv VLPs is non-trivial, but the inventors have achieved resolution of the modifications which will achieve heterodimer formation reliably during large-scale VLP manufacture. Sequences Complementary mutant pairing exemplified in the woodchuck wHv variant: Sequence Codes: Underlined – mutated compared to wild type Bold font – amino acid negatively charged at physiological pH and forming inter-molecular electrostatic bond Highlighted font – amino acid positively charged at physiological pH and forming inter- molecular electrostatic bond Double underlined – the linker sequence designed to incorporate the functionalizing protein into the wild type HBc/wHv capsid Italic – the functionalized protein sequence SEQ ID NO: 6 – Barstar protein from Bacillus amyloliquefaciens KKAVINGEQIRSISDLHQTLKKELALPEYYGENLDALWDALTGWVEYPLVLEWRQFEQSK Q LTENGAESVLQVFREAKAEGADITIELS SEQ ID NO: 7 – Im7 protein from E.coli ELKNSISDYTEAEFVQLLKEIEKENVAATDDVLDVLLEHFVKITEHPDGTDLIYYPSDNR DDS PEGIVKEIKEWRAANGKPGFKQ SEQ ID NO: 8 – T7 promotor parent sequence from Bacteriophage T7 agcataat SEQ ID NO: 9 – linker sequence (synthetic) GGGGSGGGGS SEQ ID NO: 10 – linker sequence (synthetic) GGGGGSGGGGS SEQ ID NO: 11 – linker sequence (synthetic) SGGGSSGSG SEQ ID NO: 12 – Barnase protein from Bacillus amyloliquefaciens AQVINTFDGVADYLQTYHKLPDNYITKSEAQALGWVASKGNLADVAPGKSIGGDIFSNRE G KLPGKSGRTWRWADINYTSGFRNSDRILYSSDWLIYKTTDHYQTFTKIR SEQ ID NO: 13 – ColE7 protein from E.coli ESKRNKPGKATGKGKPVNNKWLNNAGKDLGSPVPDRIANKLRDKEFKSFDDFRKKFWEEV SKDPELSKQFSRNNNDRMKVGKAPKTRTQDVSGKATSFALHHEKPISQNGGVYDMDNISV VTPKRAIDIHRGKS SEQ ID NO:14 – linker (synthetic) KAAAEKAAAE SEQ ID NO:15 – linker (synthetic) GGKAAAE SEQ ID NO:16: wHv ‘149’ monomer (truncated from wild type woodchuck hepatitis virus capsid protein) MDIDPYKEFGSSYQLLNFLPLDFFPDLNALVDTATALYEEELTGREHCSPHHTAIRQALV CW DELTKLIAWMSSNITSEQVRTIIVNHVNDTWGLKVRQSLWFHLSCLTFGQHTVQEFLVSF GV WIRTPAPYRPPNAPILSTLPEHTVI* SEQ ID NO:17 – Human IL31 functional molecule nucleic acid sequence (optimized for E.coli expression and without the signal peptide): Atgcgtttactacgaccaagtgatgatgtacagaaaatagtcgaggaattacagtccctc tcgaagatgcttttgaaagatgtgga ggaagagaagggcgtgctcgtgtcccagaattacacgctgccgtgtctcagccctgacgc ccagccgccaaacaacatccac agcccagccatccgggcatatctcaagacaatcagacagctagacaacaaatctgttatt gatgagatcatagagcacctcgac aaactcatatttcaagatgcaccagaaacaaacatttctgtgccaacagacacccatgaa tgtaaacgcttcatcctgactatttct caacagttttcagagtgcatggacctcgcactaaaatcattgacctctggagcccaacag gccaccacttaa SEQ ID NO:18 – Human Hepatitis B virus heterodimer monomer with integrated Im7: Atggacattgacccgtataaagaatttggagcttctgtggagttactctcttttttgcct tctgacttctttccttctattcgagatctcctcg acaccgcctcagctctgtatcgggaggccttagagtctccggaacattgttcacctcacc atacagcactcgaccaagctattctgt gttggggtgagttgatgaatttggccacctgggtgggaagtaatttgcaaaaagctgcag cagagaaagctgcagctgaaaata gtattagtgattacacagaggctgagtttgttcaacttcttaaggaaattgaaaaagaga atgttgctgcaactgatgatgtgttagat gtgttactcgaacactttgtaaaaattactgagcatccagatggaacggatctgatttat tatcctagtgataatagagacgatagcc ccgaagggattgtcaaggaaattaaagaatggcgagctgctaacggtaagccaggaggtg gagcatccagggaattagtagt cagctatgttaatgttaatatgggcctagatatcagacaactactgtggtttcacatttc ctgtcttacttttggaagagaaactgttcttg aatatttggtgtcttttggagtgtggattcgcactcctcctgcttacagaccaccaaatg cccctatcttatcaacacttccggaaacta ctgttgtttaa SEQ ID NO:19 – Human Hepatitis B virus heterodimer monomer with integrated Barstar binding protein: atggatattgatccgtataaagaatttggcgcgagcgtggaactgctgagctttctgccg agcgatttttttccgagcattcgcgatct gctggataccgcgagcgcgctgtatcgcgaagcgctggaaagcccggaacattgcagccc gcatcataccgcgctggatcag gcgattctgtgctggggcgaactgatgaacctggcgacctgggtgggcagcaacctgcag aaagcggcggcggaaaaagcg gcggcggaaaaagcggtgattaacggcgaacagattcgcagcattagcgatctgcatcag accctgaaaaaagaactggcg ctgccggaatattatggcgaaaacctggatgcgctgtgggatgcgctgaccggctgggtg gaatatccgctggtgctggaatggc gccagtttgaacagagcaaacagctgaccgaaaacggcgcggaaagcgtgctgcaggtgt ttcgcgaagcgaaagcggaa ggcgcggatattaccattgaactgagcggcggcggcgcgagccgcgaactggtggtgagc tatgtgaacgtgaacatgggcct ggatattcgccagctgctg tggtttcatattagctgcctgacctttggccgcgaaaccgtgctggaatatctggtgagc tttggcgtgtggattcgcaccccgccgg cgtatcgcccgccgaacgcgccgattctgagcaccctgccggaaaccaccgtggtgtaa SEQ ID NO:20 – Complementary Human Hepatitis B virus heterodimer partner monomer without binding protein: Atggacattgacccgtataaaaaatttggagcttctgtggagttactctcttttttgcct tctgacttctttccttctattcgagatctcctcg acaccgcctcagctctgtatcgggaggccttagagtctccggaacattgttcacctcacc atacagcactcaggcaagctattctgt gttggggtaaattgatgaatttggccacctgggtgggaagtaatttggaagacccagcat ccagggaattagtagtcagctatgtt aatgttaatatgggcctaaaaatcagacaactactgtggtttcacatttcctgtcttact tttggaagagaaactgttcttgaatatttggt gtcttttggagtgtggattcgcactcctcctgcttacagaccaccaaatgcccctatctt atcaacacttccggaaactactgttgttta a SEQ ID NO:21 – Woodchuck hepatitis virus heterodimer monomer with integrated Im7 binding protein: ATGGACATCGATCCATATAAGGAGTTTGGCTCCTCATACCAATTACTTAATTTCCTTCCC TTGGACTTTTTCCCCGACCTTAACGCCCTGGTTGACACGGCTACGGCGCTTTACGAAGA GGAATTAACGGGGCGTGAACATTGTTCACCTCATCACACGGCCATTGATCAAGCGTTG GTATGCTGGGATGAACTTACGAAACTGATTGCCGATATGAGTTCAAATATTACGAGCAA AGCAGCAGCCGAGAAGGCAGCAGCCGAAGAACTGAAAAATAGCATTTCAGACTACACC GAAGCAGAATTTGTGCAGTTACTGAAAGAGATCGAGAAGGAGAACGTAGCCGCAACCG ATGACGTGCTTGATGTCCTGCTTGAACATTTAGTAAAGATTACGGAACATCCAGACGGT ACGGATTTAATCTATTATCCTAGTGACAATCGCGACGACAGTCCAGAAGGCATCGTAAA GGAGATTAAAGAATGGCGTGCTGCAAACGGAAAGCCTGGGTTTAAGCAGGGTGGAAAA GCTGCGGCAGAACAGGTGCGTACCATTATCGTAAATCACGTCAATGATACCTGGGGTC TTGATGTTCGTCAGTCCCTGTGGTTTCACCTTTCATGCTTGACGTTTGGTCAGCACACA GTACAGGAGTTCCTTGTTTCTTTCGGGGTATGGATTCGTACACCAGCTCCTTATCGCCC TCCTAACGCACCTATTTTATCCACGTTACCTGAACATACCGTTATTTAG SEQ ID NO:22 – Woodchuck hepatitis virus heterodimer monomer with integrated Barstar binding protein: ATGGACATCGACCCATACAAAGAATTTGGAAGTAGTTACCAGCTTCTGAATTTCTTACCT CTTGACTTCTTTCCAGACTTGAACGCGCTGGTAGACACAGCGACAGCTTTATATGAAGA GGAGCTGACAGGCCGCGAGCACTGCTCACCTCATCATACGGCCATCGATCAAGCACTG GTATGCTGGGATGAGTTGACTAAGTTGATTGCTGACATGTCATCTAACATCACCTCCAA AGCAGCGGCCGAGAAGGCAGCAGCAGAAAAAAAGGCTGTAATTAACGGTGAGCAGAT CCGCAGTATTAGCGACTTACACCAAACATTGAAAAAGGAACTTGCCTTACCCGAGTACT ATGGCGAAAACCTGGATGCTCTGTGGGACGCTTTAACAGGATGGGTCGAGTACCCGTT GGTGTTAGAATGGCGCCAGTTCGAGCAGAGTAAGCAATTGACTGAGAATGGTGCCGAA TCCGTATTACAAGTATTCCGCGAAGCCAAGGCCGAGGGGGCAGATATCACTATTGAAC TGTCTAAAGCCGCGGCCGAACAGGTACGCACTATCATTGTGAACCATGTCAATGACAC CTGGGGGTTAGATGTCCGTCAATCCCTTTGGTTTCATTTATCGTGCTTAACTTTCGGTCA GCACACTGTTCAAGAGTTTCTGGTCTCGTTTGGAGTATGGATTCGCACGCCTGCGCCAT ATCGCCCGCCTAATGCGCCTATTCTGTCTACCTTGCCCGAACATACGGTTATTTAG SEQ ID NO:23 – Complementary Woodchuck Hepatitis virus partner monomer without binding protein: ATGGATATTGATCCGTATAAAAAATTTGGCAGCAGCTATCAGCTGCTGAACTTTCTGCC GCTGGATTTTTTTCCGGATCTGAACGCGCTGGTGGATACCGCGACCGCGCTGTATGAA GAAGAACTGACCGGCCGCGAACATTGCAGCCCGCATCATACCGCGATTCGCCAAGCG CTGGTGTGCTGGGATAAACTGACCGAACTGATTGCGTGGATGAGCAGCAACATTACGA GCAAACAAGTGGATACCATTATTGTGAACAAAGTGAACGATACCTGGGGCCTGAAAGTG CGTCAGAGCCTGTGGTTTCATCTGAGCTGCCTGACCTTTGGTCAGCATACCGTGCAAG AATTTCTGGTGAGCTTTGGCGTGTGGATTCGCACCCCGGCGCCGTATCGCCCGCCGAA CGCGCCGATTCTGAGCACCCTGCCGGAACATACCGTGATTTAA SEQ ID NO:24 – Functional molecule and second binding protein sequence: ColicinE7- fused-to-human-IL31 ATGGAGAGTAAACGGAATAAGCCAGGGAAGGCAACAGGTAAAGGAAAACCTGTCAATA ATAAGTGGTTAAATAATGCAGGTAAAGACTTAGGTTCTCCTGTTCCAGATCGTATAGCTA ATAAACTACGTGATAAGGAGTTTAAAAGTTTCGATGATTTTCGTAAGAAATTCTGGGAAG AAGTGTCAAAAGATCCTGAGTTAAGTAAACAATTTAGTCGAAACAATAATGATCGAATGA AGGTTGGAAAAGCGCCCAAGACTAGAACCCAGGATGTTTCAGGGAAGGCAACTTCATT CGCACTTCATCATGAGAAGCCGATCAGCCAAAATGGTGGTGTCTATGATATGGATAACA TCAGCGTGGTAACACCTAAACGTGCTATTGATATTCACCGAGGTAAAAGCGGAGGTGG CTCATCAGGATCtGGTGAAAACCTGTATTTTCAGGGatccGGAGGTGGCTCAggacgttt actac gaccaagtgatgatgtacagaaaatagtcgaggaattacagtccctctcgaagatgcttt tgaaagatgtggaggaagagaag ggcgtgctcgtgtcccagaattacacgctgccgtgtctcagccctgacgcccagccgcca aacaacatccacagcccagccat ccgggcatatctcaagacaatcagacagctagacaacaaatctgttattgatgagatcat agagcacctcgacaaactcatattt caagatgcaccagaaacaaacatttctgtgccaacagacacccatgaatgtaaacgcttc atcctgactatttctcaacagttttca gagtgcatggacctcgcactaaaatcattgacctctggagcccaacaggccaccacttaa SEQ ID NO:25 – Functional molecule and second binding protein sequence: Barnase-fused- to-murine-IL31 ATGgcacaggttatcaacacgtttgacggggttgcggattatcttcagacatatcataag ctacctgataattacattacaaaatc agaagcacaagccctcggctgggtggcatcaaaagggaaccttgcagacgtcgctccggg gaaaagcatcggcggagaca tcttctcaaacagggaaggcaaactcccgggcaaaagcggacgaacatggcgtTGGgcgg atattaactatacatcaggctt cagaaattcagaccggattctttactcaagcgactggctgatttacaaaacaacggacca ttatcagacctttacaaaaatcaga GGAGGTTTAGCTGAGGCAGCTGCTAAGGAAGCTGCCGCAAAGGCTGCAAAAGAAGATC TGCGCACCACCATTGATCTGCTGAAACAGGAAAGCCAGGATCTGTATAACAACTATAGC ATTAAACAGGCGAGCGGCATGAGCGCGGATGAAAGCATTCAGCTGCCGTGCTTTAGCC TGGATCGCGAAGCGCTGACCAACATTAGCGTGATTATTGCGCATCTGGAAAAAGTGAAA GTGCTGAGCGAAAACACCGTGGATACCAGCTGGGTGATTCGCTGGCTGACCAACATTA GCTGCTTTAACCCGCTGAACCTGAACATTAGCGTGCCGGGCAACACCGATGAAAGCTA TGATTGCGCGGTGTTTGTGCTGACCGTGCTGAAACAGTTTAGCAACTGCATGGCGGAA CTGCAGGCGAAGGACCACGACCACGACCACGACCACGACCACGAGtaataa SEQ ID NO:26 – Nucleic acid sequence for vector that expresses both human Hepatitis B virus heterodimer monomer units (internal number DU73928; derived from pET-duet vector) GGGGAATTGTGAGCGGATAACAATTCCCCTCTAGAAATAATTTTGTTTAACTTTAAGAAG GAGATATACCAtggacattgacccgtataaagaatttggagcttctgtggagttactctc ttttttgccttctgacttctttccttcta ttcgagatctcctcgacaccgcctcagctctgtatcgggaggccttagagtctccggaac attgttcacctcaccatacagcactcg accaagctattctgtgttggggtgagttgatgaatttggccacctgggtgggaagtaatt tgcaaaaagctgcagcagagaaagct gcagctgaaaatagtattagtgattacacagaggctgagtttgttcaacttcttaaggaa attgaaaaagagaatgttgctgcaact gatgatgtgttagatgtgttactcgaacactttgtaaaaattactgagcatccagatgga acggatctgatttattatcctagtgataat agagacgatagccccgaagggattgtcaaggaaattaaagaatggcgagctgctaacggt aagccaggaggtggagcatcc agggaattagtagtcagctatgttaatgttaatatgggcctagatatcagacaactactg tggtttcacatttcctgtcttacttttggaa gagaaactgttcttgaatatttggtgtcttttggagtgtggattcgcactcctcctgctt acagaccaccaaatgcccctatcttatcaac acttccggaaactactgttgtttaaTGAGCGGCCGCTTAACCTAGGCTGCTGCCACCGCT GAGCAAT AACTAGCATAACCCCTTGGGGCCTCTAAACGGGTCTTGAGGGGTTTTTTGTTGTACACG GCCGCATAATAATACGACTCACTATAGGGGAATTGTGAGCGGATAACAATTCCCCTCTA GAAATAATTTTGTTTAACTTTAAGAAGGAGATATACCatggacattgacccgtataaaaa atttggagctt ctgtggagttactctcttttttgccttctgacttctttccttctattcgagatctcctcg acaccgcctcagctctgtatcgggaggccttaga gtctccggaacattgttcacctcaccatacagcactcaggcaagctattctgtgttgggg taaattgatgaatttggccacctgggtg ggaagtaatttggaagacccagcatccagggaattagtagtcagctatgttaatgttaat atgggcctaaaaatcagacaactact gtggtttcacatttcctgtcttacttttggaagagaaactgttcttgaatatttggtgtc ttttggagtgtggattcgcactcctcctgcttaca gaccaccaaatgcccctatcttatcaacacttccggaaactactgttgtttaataaTAAG CGGCCGCTTAACCTAGG CTGCTGCCACCGCTGAGCAATAACTAGCATAACCCCTTGGGGCCTCTAAACGGGTCTT GAGGGGTTTTTTGCTAGCATAACCCCTTGGGGCCTCTAAACGGGTCTTGAGGGGTTTTT TGTTGTACACGGCCGCATAATCGgttgacactctatcattgatagagttattttaccact ccctatcagtgatagaga aAagtgaaatgaatagttcgacaaaaatctagataacgagggcaaCATaaGGTACCgTCG AGTCTGGTAAAG AAACCGCTGCTGCGAAATTTGAACGCCAGCACATGGACTCGTCTACTAGCGCAGCTTA ATTAACCTAGGCTGCTGCCACCGCTGAGCAATAACTAGCATAACCCCTTGGGGCCTCTA AACGGGTCTTGAGGGGTTTTTTGCTGAAAGGAGGAACTATATCCGGATTGGCGAATGG GACGCGCCCTGTAGCGGCGCATTAAGCGCGGCGGGTGTGGTGGTTACGCGCAGCGT GACCGCTACACTTGCCAGCGCCCTAGCGCCCGCTCCTTTCGCTTTCTTCCCTTCCTTTC TCGCCACGTTCGCCGGCTTTCCCCGTCAAGCTCTAAATCGGGGGCTCCCTTTAGGGTT CCGATTTAGTGCTTTACGGCACCTCGACCCCAAAAAACTTGATTAGGGTGATGGTTCAC GTAGTGGGCCATCGCCCTGATAGACGGTTTTTCGCCCTTTGACGTTGGAGTCCACGTT CTTTAATAGTGGACTCTTGTTCCAAACTGGAACAACACTCAACCCTATCTCGGTCTATTC TTTTGATTTATAAGGGATTTTGCCGATTTCGGCCTATTGGTTAAAAAATGAGCTGATTTA ACAAAAATTTAACGCGAATTTTAACAAAATATTAACGTTTACAATTTCTGGCGGCACGAT GGCATGAGATTATCAAAAAGGATCTTCACCTAGATCCTTTTAAATTAAAAATGAAGTTTT A AATCAATCTAAAGTATATATGAGTAAACTTGGTCTTtaGGACCCACTTTCACATTTAAGT T GTTTTTCTAATCCGCAgATGATCAATTCAAGGCCGAATAAGAAGGCTGGCTCTGCACCT TGGTGATCAAATAATTCGATAGCTTGTCGTAATAATGGCGGCATACTATCAGTAGTAGG TGTTTCCCTTTCTTCTTTAGCGACTTGATGCTCTTGATCTTCCAATACGCAACCTAAAGT AAAATGCCCCACAGCGCTGAGTGCATATAATGCATTCTCTAGTGAAAAACCTTGTTGGC ATAAAAAGGCTAATTGATTTTCGAGAGTTTCATACTGTTTTTCTGTAGGCCGTGTACCTA AATGTACTTTTGCTCCATCGCGATGACTTAGTAAAGCACATCTAAAACTTTTAGCGTTAT TACGTAAAAAATCTTGCCAGCTTTCCCCTTCTAAAGGGCAAAAGTGAGTATGGTGCCTA TCTAACATCTCAATGGCTAAGGCGTCGAGCAAAGCCCGCTTATTTTTTACATGCCAATA CAATGTAGGCTGCTCTACACCTAGCTTCTGGGCGAGTTTACGGGTTGTTAAACCTTCGA TTCCGACCTCATTAAGCAGCTCTAATGCGCTGTTAATCACTTTACTTTTATCTAATCTAG A CATcattaattccTACCAATGCTTAATCAGTGAGGCACCTATCTCAGCGATCTGTCTATT TCG TTCATCCATAGTTGCCTGACTCCCCGTCGTGTAGATAACTACGATACGGGAGGGCTTAC CATCTGGCCCCAGTGCTGCAATGATACCGCGAGACCCACGCTCACCGGCTCCAGATTT ATCAGCAATAAACCAGCCAGCCGGAAGGGCCGAGCGCAGAAGTGGTCCTGCAACTTTA TCCGCCTCCATCCAGTCTATTAATTGTTGCCGGGAAGCTAGAGTAAGTAGTTCGCCAGT TAATAGTTTGCGCAACGTTGTTGCCATTGCTACAGGCATCGTGGTGTCACGCTCGTCGT TTGGTATGGCTTCATTCAGCTCCGGTTCCCAACGATCAAGGCGAGTTACATGATCCCCC ATGTTGTGCAAAAAAGCGGTTAGCTCCTTCGGTCCTCCGATCGTTGTCAGAAGTAAGTT GGCCGCAGTGTTATCACTCATGGTTATGGCAGCACTGCATAATTCTCTTACTGTCATGC CATCCGTAAGATGCTTTTCTGTGACTGGTGAGTACTCAACCAAGTCATTCTGAGAATAG TGTATGCGGCGACCGAGTTGCTCTTGCCCGGCGTCAATACGGGATAATACCGCGCCAC ATAGCAGAACTTTAAAAGTGCTCATCATTGGAAAACGTTCTTCGGGGCGAAAACTCTCA AGGATCTTACCGCTGTTGAGATCCAGTTCGATGTAACCCACTCGTGCACCCAACTGATC TTCAGCATCTTTTACTTTCACCAGCGTTTCTGGGTGAGCAAAAACAGGAAGGCAAAATG CCGCAAAAAAGGGAATAAGGGCGACACGGAAATGTTGAATACTCATACTCTTCCTTTTT CAATCATGATTGAAGCATTTATCAGGGTTATTGTCTCATGAGCGGATACATATTTGAATG TATTTAGAAAAATAAACAAATAGGTCATGACCAAAATCCCTTAACGTGAGTTTTCGTTCC ACTGAGCGTCAGACCCCGTAGAAAAGATCAAAGGATCTTCTTGAGATCCTTTTTTTCTG CGCGTAATCTGCTGCTTGCAAACAAAAAAACCACCGCTACCAGCGGTGGTTTGTTTGCC GGATCAAGAGCTACCAACTCTTTTTCCGAAGGTAACTGGCTTCAGCAGAGCGCAGATAC CAAATACTGTCCTTCTAGTGTAGCCGTAGTTAGGCCACCACTTCAAGAACTCTGTAGCA CCGCCTACATACCTCGCTCTGCTAATCCTGTTACCAGTGGCTGCTGCCAGTGGCGATA AGTCGTGTCTTACCGGGTTGGACTCAAGACGATAGTTACCGGATAAGGCGCAGCGGTC GGGCTGAACGGGGGGTTCGTGCACACAGCCCAGCTTGGAGCGAACGACCTACACCGA ACTGAGATACCTACAGCGTGAGCTATGAGAAAGCGCCACGCTTCCCGAAGGGAGAAAG GCGGACAGGTATCCGGTAAGCGGCAGGGTCGGAACAGGAGAGCGCACGAGGGAGCT TCCAGGGGGAAACGCCTGGTATCTTTATAGTCCTGTCGGGTTTCGCCACCTCTGACTTG AGCGTCGATTTTTGTGATGCTCGTCAGGGGGGCGGAGCCTATGGAAAAACGCCAGCAA CGCGGCCTTTTTACGGTTCCTGGCCTTTTGCTGGCCTTTTGCTCACATGTTCTTTCCTG CGTTATCCCCTGATTCTGTGGATAACCGTATTACCGCCTTTGAGTGAGCTGATACCGCT CGCCGCAGCCGAACGACCGAGCGCAGCGAGTCAGTGAGCGAGGAAGCGGAAGAGCG CCTGATGCGGTATTTTCTCCTTACGCATCTGTGCGGTATTTCACACCGCATATATGGTG CACTCTCAGTACAATCTGCTCTGATGCCGCATAGTTAAGCCAGTATACACTCCGCTATC GCTACGTGACTGGGTCATGGCTGCGCCCCGACACCCGCCAACACCCGCTGACGCGCC CTGACGGGCTTGTCTGCTCCCGGCATCCGCTTACAGACAAGCTGTGACCGTCTCCGGG AGCTGCATGTGTCAGAGGTTTTCACCGTCATCACCGAAACGCGCGAGGCAGCTGCGGT AAAGCTCATCAGCGTGGTCGTGAAGCGATTCACAGATGTCTGCCTGTTCATCCGCGTC CAGCTCGTTGAGTTTCTCCAGAAGCGTTAATGTCTGGCTTCTGATAAAGCGGGCCATGT TAAGGGCGGTTTTTTCCTGTTTGGTCACTGATGCCTCCGTGTAAGGGGGATTTCTGTTC ATGGGGGTAATGATACCGATGAAACGAGAGAGGATGCTCACGATACGGGTTACTGATG ATGAACATGCCCGGTTACTGGAACGTTGTGAGGGTAAACAACTGGCGGTATGGATGCG GCGGGACCAGAGAAAAATCACTCAGGGTCAATGCCAGCGCTTCGTTAATACAGATGTA GGTGTTCCACAGGGTAGCCAGCAGCATCCTGCGATGCAGATCCGGAACATAATGGTGC AGGGCGCTGACTTCCGCGTTTCCAGACTTTACGAAACACGGAAACCGAAGACCATTCA TGTTGTTGCTCAGGTCGCAGACGTTTTGCAGCAGCAGTCGCTTCACGTTCGCTCGCGT ATCGGTGATTCATTCTGCTAACCAGTAAGGCAACCCCGCCAGCCTAGCCGGGTCCTCA ACGACAGGAGCACGATCATGCTAGTCATGCCCCGCGCCCACCGGAAGGAGCTGACTG GGTTGAAGGCTCTCAAGGGCATCGGTCGAGATCCCGGTGCCTAATGAGTGAGCTAACT TACATTAATTGCGTTGCGCTCACTGCCCGCTTTCCAGTCGGGAAACCTGTCGTGCCAG CTGCATTAATGAATCGGCCAACGCGCGGGGAGAGGCGGTTTGCGTATTGGGCGCCAG GGTGGTTTTTCTTTTCACCAGTGAGACGGGCAACAGCTGATTGCCCTTCACCGCCTGG CCCTGAGAGAGTTGCAGCAAGCGGTCCACGCTGGTTTGCCCCAGCAGGCGAAAATCCT GTTTGATGGTGGTTAACGGCGGGATATAACATGAGCTGTCTTCGGTATCGTCGTATCCC ACTACCGAGATGTCCGCACCAACGCGCAGCCCGGACTCGGTAATGGCGCGCATTGCG CCCAGCGCCATCTGATCGTTGGCAACCAGCATCGCAGTGGGAACGATGCCCTCATTCA GCATTTGCATGGTTTGTTGAAAACCGGACATGGCACTCCAGTCGCCTTCCCGTTCCGCT ATCGGCTGAATTTGATTGCGAGTGAGATATTTATGCCAGCCAGCCAGACGCAGACGCG CCGAGACAGAACTTAATGGGCCCGCTAACAGCGCGATTTGCTGGTGACCCAATGCGAC CAGATGCTCCACGCCCAGTCGCGTACCGTCTTCATGGGAGAAAATAATACTGTTGATG GGTGTCTGGTCAGAGACATCAAGAAATAACGCCGGAACATTAGTGCAGGCAGCTTCCA CAGCAATGGCATCCTGGTCATCCAGCGGATAGTTAATGATCAGCCCACTGACGCGTTG CGCGAGAAGATTGTGCACCGCCGCTTTACAGGCTTCGACGCCGCTTCGTTCTACCATC GACACCACCACGCTGGCACCCAGTTGATCGGCGCGAGATTTAATCGCCGCGACAATTT GCGACGGCGCGTGCAGGGCCAGACTGGAGGTGGCAACGCCAATCAGCAACGACTGTT TGCCCGCCAGTTGTTGTGCCACGCGGTTGGGAATGTAATTCAGCTCCGCCATCGCCGC TTCCACTTTTTCCCGCGTTTTCGCAGAAACGTGGCTGGCCTGGTTCACCACGCGGGAA ACGGTCTGATAAGAGACACCGGCATACTCTGCGACATCGTATAACGTTACTGGTTTCAC ATTCACCACCCTGAATTGACTCTCTTCCGGGCGCTATCATGCCATACCGCGAAAGGTTT TGCGCCATTCGATGGTGTCCGGGATCTCGACGCTCTCCCTTATGCGACTCCTGCATTA GGAAGCAGCCCAGTAGTAGGTTGAGGCCGTTGAGCACCGCCGCCGCAAGGAATGGTG CATGCAAGGAGATGGCGCCCAACAGTCCCCCGGCCACGGGGCCTGCCACCATACCCA CGCCGAAACAAGCGCTCATGAGCCCGAAGTGGCGAGCCCGATCTTCCCCATCGGTGA TGTCGGCGATATAGGCGCCAGCAACCGCACCTGTGGCGCCGGTGATGCCGGCCACGA TGCGTCCGGCGTAGAGGATCGAGATCGATCTCGATCCCGCGAAATTAATACGACTCAC TATA SEQ ID NO:27 – Sequence of vector that expresses both woodchuck hepatitis virus heterodimer monomer subunits (as well as second binding protein-functional molecule Barnase-IL31, derived from pET duet plasmid) GGGGAATTGTGAGCGGATAACAATTCCCCTCTAGAAATAATTTTGTTTAACTTTAAGAAG GAGATATACCATGGACATCGACCCATACAAAGAATTTGGAAGTAGTTACCAGCTTCTGA ATTTCTTACCTCTTGACTTCTTTCCAGACTTGAACGCGCTGGTAGACACAGCGACAGCT TTATATGAAGAGGAGCTGACAGGCCGCGAGCACTGCTCACCTCATCATACGGCCATCG ATCAAGCACTGGTATGCTGGGATGAGTTGACTAAGTTGATTGCTGACATGTCATCTAAC ATCACCTCCAAAGCAGCGGCCGAGAAGGCAGCAGCAGAAAAAAAGGCTGTAATTAACG GTGAGCAGATCCGCAGTATTAGCGACTTACACCAAACATTGAAAAAGGAACTTGCCTTA CCCGAGTACTATGGCGAAAACCTGGATGCTCTGTGGGACGCTTTAACAGGATGGGTCG AGTACCCGTTGGTGTTAGAATGGCGCCAGTTCGAGCAGAGTAAGCAATTGACTGAGAA TGGTGCCGAATCCGTATTACAAGTATTCCGCGAAGCCAAGGCCGAGGGGGCAGATATC ACTATTGAACTGTCTAAAGCCGCGGCCGAACAGGTACGCACTATCATTGTGAACCATGT CAATGACACCTGGGGGTTAGATGTCCGTCAATCCCTTTGGTTTCATTTATCGTGCTTAA CTTTCGGTCAGCACACTGTTCAAGAGTTTCTGGTCTCGTTTGGAGTATGGATTCGCACG CCTGCGCCATATCGCCCGCCTAATGCGCCTATTCTGTCTACCTTGCCCGAACATACGGT TATTTAGTGAGCGGCCGCTTAACCTAGGCTGCTGCCACCGCTGAGCAATAACTAGCATA ACCCCTTGGGGCCTCTAAACGGGTCTTGAGGGGTTTTTTGTTGTACACGGCCGCATAAT AATACGACTCACTATAGGGGAATTGTGAGCGGATAACAATTCCCCTCTAGAAATAATTTT GTTTAACTTTAAGAAGGAGATATACCATGGATATTGATCCGTATAAAAAATTTGGCAGCA GCTATCAGCTGCTGAACTTTCTGCCGCTGGATTTTTTTCCGGATCTGAACGCGCTGGTG GATACCGCGACCGCGCTGTATGAAGAAGAACTGACCGGCCGCGAACATTGCAGCCCG CATCATACCGCGATTCGCCAAGCGCTGGTGTGCTGGGATAAACTGACCGAACTGATTG CGTGGATGAGCAGCAACATTACGAGCAAACAAGTGGATACCATTATTGTGAACAAAGTG AACGATACCTGGGGCCTGAAAGTGCGTCAGAGCCTGTGGTTTCATCTGAGCTGCCTGA CCTTTGGTCAGCATACCGTGCAAGAATTTCTGGTGAGCTTTGGCGTGTGGATTCGCACC CCGGCGCCGTATCGCCCGCCGAACGCGCCGATTCTGAGCACCCTGCCGGAACATACC GTGATTTAATAAGCGGCCGCTTAACCTAGGCTGCTGCCACCGCTGAGCAATAACTAGC ATAACCCCTTGGGGCCTCTAAACGGGTCTTGAGGGGTTTTTTGTTGTACACGGCCGCAT AATCGgttgacactctatcattgatagagttattttaccactccctatcagtgatagaga aAagtgaaatgaatagttcgacaaa aatctagataacgagggcaaCATATGgcacaggttatcaacacgtttgacggggttgcgg attatcttcagacatatcataag ctacctgataattacattacaaaatcagaagcacaagccctcggctgggtggcatcaaaa gggaaccttgcagacgtcgctccg gggaaaagcatcggcggagacatcttctcaaacagggaaggcaaactcccgggcaaaagc ggacgaacatggcgtTGG gcggatattaactatacatcaggcttcagaaattcagaccggattctttactcaagcgac tggctgatttacaaaacaacggacca ttatcagacctttacaaaaatcagaGGAGGTTTAGCTGAGGCAGCTGCTAAGGAAGCTGC CGCAAA GGCTGCAAAAGAAGATCTGCGCACCACCATTGATCTGCTGAAACAGGAAAGCCAGGAT CTGTATAACAACTATAGCATTAAACAGGCGAGCGGCATGAGCGCGGATGAAAGCATTC AGCTGCCGTGCTTTAGCCTGGATCGCGAAGCGCTGACCAACATTAGCGTGATTATTGC GCATCTGGAAAAAGTGAAAGTGCTGAGCGAAAACACCGTGGATACCAGCTGGGTGATT CGCTGGCTGACCAACATTAGCTGCTTTAACCCGCTGAACCTGAACATTAGCGTGCCGG GCAACACCGATGAAAGCTATGATTGCGCGGTGTTTGTGCTGACCGTGCTGAAACAGTTT AGCAACTGCATGGCGGAACTGCAGGCGAAGGACCACGACCACGACCACGACCACGAC CACGAGtaataaGGTACCCTCGAGTCTGGTAAAGAAACCGCTGCTGCGAAATTTGAACGC CAGCACATGGACTCGTCTACTAGCGCAGCTTAATTAACCTAGGCTGCTGCCACCGCTG AGCAATAACTAGCATAACCCCTTGGGGCCTCTAAACGGGTCTTGAGGGGTTTTTTGCTG AAAGGAGGAACTATATCCGGATTGGCGAATGGGACGCGCCCTGTAGCGGCGCATTAAG CGCGGCGGGTGTGGTGGTTACGCGCAGCGTGACCGCTACACTTGCCAGCGCCCTAGC GCCCGCTCCTTTCGCTTTCTTCCCTTCCTTTCTCGCCACGTTCGCCGGCTTTCCCCGTC AAGCTCTAAATCGGGGGCTCCCTTTAGGGTTCCGATTTAGTGCTTTACGGCACCTCGAC CCCAAAAAACTTGATTAGGGTGATGGTTCACGTAGTGGGCCATCGCCCTGATAGACGG TTTTTCGCCCTTTGACGTTGGAGTCCACGTTCTTTAATAGTGGACTCTTGTTCCAAACTG GAACAACACTCAACCCTATCTCGGTCTATTCTTTTGATTTATAAGGGATTTTGCCGATTT CGGCCTATTGGTTAAAAAATGAGCTGATTTAACAAAAATTTAACGCGAATTTTAACAAAA TATTAACGTTTACAATTTCTGGCGGCACGATGGCATGAGATTATCAAAAAGGATCTTCAC CTAGATCCTTTTAAATTAAAAATGAAGTTTTAAATCAATCTAAAGTATATATGAGTAAAC T TGGTCTTtaGGACCCACTTTCACATTTAAGTTGTTTTTCTAATCCGCAgATGATCAATTC A AGGCCGAATAAGAAGGCTGGCTCTGCACCTTGGTGATCAAATAATTCGATAGCTTGTCG TAATAATGGCGGCATACTATCAGTAGTAGGTGTTTCCCTTTCTTCTTTAGCGACTTGATG CTCTTGATCTTCCAATACGCAACCTAAAGTAAAATGCCCCACAGCGCTGAGTGCATATA ATGCATTCTCTAGTGAAAAACCTTGTTGGCATAAAAAGGCTAATTGATTTTCGAGAGTTT CATACTGTTTTTCTGTAGGCCGTGTACCTAAATGTACTTTTGCTCCATCGCGATGACTTA GTAAAGCACATCTAAAACTTTTAGCGTTATTACGTAAAAAATCTTGCCAGCTTTCCCCTT CTAAAGGGCAAAAGTGAGTATGGTGCCTATCTAACATCTCAATGGCTAAGGCGTCGAG CAAAGCCCGCTTATTTTTTACATGCCAATACAATGTAGGCTGCTCTACACCTAGCTTCTG GGCGAGTTTACGGGTTGTTAAACCTTCGATTCCGACCTCATTAAGCAGCTCTAATGCGC TGTTAATCACTTTACTTTTATCTAATCTAGACATcattaattccTACCAATGCTTAATCA GTGAG GCACCTATCTCAGCGATCTGTCTATTTCGTTCATCCATAGTTGCCTGACTCCCCGTCGT GTAGATAACTACGATACGGGAGGGCTTACCATCTGGCCCCAGTGCTGCAATGATACCG CGAGACCCACGCTCACCGGCTCCAGATTTATCAGCAATAAACCAGCCAGCCGGAAGGG CCGAGCGCAGAAGTGGTCCTGCAACTTTATCCGCCTCCATCCAGTCTATTAATTGTTGC CGGGAAGCTAGAGTAAGTAGTTCGCCAGTTAATAGTTTGCGCAACGTTGTTGCCATTGC TACAGGCATCGTGGTGTCACGCTCGTCGTTTGGTATGGCTTCATTCAGCTCCGGTTCCC AACGATCAAGGCGAGTTACATGATCCCCCATGTTGTGCAAAAAAGCGGTTAGCTCCTTC GGTCCTCCGATCGTTGTCAGAAGTAAGTTGGCCGCAGTGTTATCACTCATGGTTATGGC AGCACTGCATAATTCTCTTACTGTCATGCCATCCGTAAGATGCTTTTCTGTGACTGGTGA GTACTCAACCAAGTCATTCTGAGAATAGTGTATGCGGCGACCGAGTTGCTCTTGCCCG GCGTCAATACGGGATAATACCGCGCCACATAGCAGAACTTTAAAAGTGCTCATCATTGG AAAACGTTCTTCGGGGCGAAAACTCTCAAGGATCTTACCGCTGTTGAGATCCAGTTCGA TGTAACCCACTCGTGCACCCAACTGATCTTCAGCATCTTTTACTTTCACCAGCGTTTCTG GGTGAGCAAAAACAGGAAGGCAAAATGCCGCAAAAAAGGGAATAAGGGCGACACGGA AATGTTGAATACTCATACTCTTCCTTTTTCAATCATGATTGAAGCATTTATCAGGGTTAT T GTCTCATGAGCGGATACATATTTGAATGTATTTAGAAAAATAAACAAATAGGTCATGACC AAAATCCCTTAACGTGAGTTTTCGTTCCACTGAGCGTCAGACCCCGTAGAAAAGATCAA AGGATCTTCTTGAGATCCTTTTTTTCTGCGCGTAATCTGCTGCTTGCAAACAAAAAAACC ACCGCTACCAGCGGTGGTTTGTTTGCCGGATCAAGAGCTACCAACTCTTTTTCCGAAGG TAACTGGCTTCAGCAGAGCGCAGATACCAAATACTGTCCTTCTAGTGTAGCCGTAGTTA GGCCACCACTTCAAGAACTCTGTAGCACCGCCTACATACCTCGCTCTGCTAATCCTGTT ACCAGTGGCTGCTGCCAGTGGCGATAAGTCGTGTCTTACCGGGTTGGACTCAAGACGA TAGTTACCGGATAAGGCGCAGCGGTCGGGCTGAACGGGGGGTTCGTGCACACAGCCC AGCTTGGAGCGAACGACCTACACCGAACTGAGATACCTACAGCGTGAGCTATGAGAAA GCGCCACGCTTCCCGAAGGGAGAAAGGCGGACAGGTATCCGGTAAGCGGCAGGGTC GGAACAGGAGAGCGCACGAGGGAGCTTCCAGGGGGAAACGCCTGGTATCTTTATAGT CCTGTCGGGTTTCGCCACCTCTGACTTGAGCGTCGATTTTTGTGATGCTCGTCAGGGG GGCGGAGCCTATGGAAAAACGCCAGCAACGCGGCCTTTTTACGGTTCCTGGCCTTTTG CTGGCCTTTTGCTCACATGTTCTTTCCTGCGTTATCCCCTGATTCTGTGGATAACCGTAT TACCGCCTTTGAGTGAGCTGATACCGCTCGCCGCAGCCGAACGACCGAGCGCAGCGA GTCAGTGAGCGAGGAAGCGGAAGAGCGCCTGATGCGGTATTTTCTCCTTACGCATCTG TGCGGTATTTCACACCGCATATATGGTGCACTCTCAGTACAATCTGCTCTGATGCCGCA TAGTTAAGCCAGTATACACTCCGCTATCGCTACGTGACTGGGTCATGGCTGCGCCCCG ACACCCGCCAACACCCGCTGACGCGCCCTGACGGGCTTGTCTGCTCCCGGCATCCGC TTACAGACAAGCTGTGACCGTCTCCGGGAGCTGCATGTGTCAGAGGTTTTCACCGTCA TCACCGAAACGCGCGAGGCAGCTGCGGTAAAGCTCATCAGCGTGGTCGTGAAGCGAT TCACAGATGTCTGCCTGTTCATCCGCGTCCAGCTCGTTGAGTTTCTCCAGAAGCGTTAA TGTCTGGCTTCTGATAAAGCGGGCCATGTTAAGGGCGGTTTTTTCCTGTTTGGTCACTG ATGCCTCCGTGTAAGGGGGATTTCTGTTCATGGGGGTAATGATACCGATGAAACGAGA GAGGATGCTCACGATACGGGTTACTGATGATGAACATGCCCGGTTACTGGAACGTTGT GAGGGTAAACAACTGGCGGTATGGATGCGGCGGGACCAGAGAAAAATCACTCAGGGT CAATGCCAGCGCTTCGTTAATACAGATGTAGGTGTTCCACAGGGTAGCCAGCAGCATC CTGCGATGCAGATCCGGAACATAATGGTGCAGGGCGCTGACTTCCGCGTTTCCAGACT TTACGAAACACGGAAACCGAAGACCATTCATGTTGTTGCTCAGGTCGCAGACGTTTTGC AGCAGCAGTCGCTTCACGTTCGCTCGCGTATCGGTGATTCATTCTGCTAACCAGTAAGG CAACCCCGCCAGCCTAGCCGGGTCCTCAACGACAGGAGCACGATCATGCTAGTCATGC CCCGCGCCCACCGGAAGGAGCTGACTGGGTTGAAGGCTCTCAAGGGCATCGGTCGAG ATCCCGGTGCCTAATGAGTGAGCTAACTTACATTAATTGCGTTGCGCTCACTGCCCGCT TTCCAGTCGGGAAACCTGTCGTGCCAGCTGCATTAATGAATCGGCCAACGCGCGGGGA GAGGCGGTTTGCGTATTGGGCGCCAGGGTGGTTTTTCTTTTCACCAGTGAGACGGGCA ACAGCTGATTGCCCTTCACCGCCTGGCCCTGAGAGAGTTGCAGCAAGCGGTCCACGCT GGTTTGCCCCAGCAGGCGAAAATCCTGTTTGATGGTGGTTAACGGCGGGATATAACAT GAGCTGTCTTCGGTATCGTCGTATCCCACTACCGAGATGTCCGCACCAACGCGCAGCC CGGACTCGGTAATGGCGCGCATTGCGCCCAGCGCCATCTGATCGTTGGCAACCAGCAT CGCAGTGGGAACGATGCCCTCATTCAGCATTTGCATGGTTTGTTGAAAACCGGACATG GCACTCCAGTCGCCTTCCCGTTCCGCTATCGGCTGAATTTGATTGCGAGTGAGATATTT ATGCCAGCCAGCCAGACGCAGACGCGCCGAGACAGAACTTAATGGGCCCGCTAACAG CGCGATTTGCTGGTGACCCAATGCGACCAGATGCTCCACGCCCAGTCGCGTACCGTCT TCATGGGAGAAAATAATACTGTTGATGGGTGTCTGGTCAGAGACATCAAGAAATAACGC CGGAACATTAGTGCAGGCAGCTTCCACAGCAATGGCATCCTGGTCATCCAGCGGATAG TTAATGATCAGCCCACTGACGCGTTGCGCGAGAAGATTGTGCACCGCCGCTTTACAGG CTTCGACGCCGCTTCGTTCTACCATCGACACCACCACGCTGGCACCCAGTTGATCGGC GCGAGATTTAATCGCCGCGACAATTTGCGACGGCGCGTGCAGGGCCAGACTGGAGGT GGCAACGCCAATCAGCAACGACTGTTTGCCCGCCAGTTGTTGTGCCACGCGGTTGGGA ATGTAATTCAGCTCCGCCATCGCCGCTTCCACTTTTTCCCGCGTTTTCGCAGAAACGTG GCTGGCCTGGTTCACCACGCGGGAAACGGTCTGATAAGAGACACCGGCATACTCTGC GACATCGTATAACGTTACTGGTTTCACATTCACCACCCTGAATTGACTCTCTTCCGGGC GCTATCATGCCATACCGCGAAAGGTTTTGCGCCATTCGATGGTGTCCGGGATCTCGAC GCTCTCCCTTATGCGACTCCTGCATTAGGAAGCAGCCCAGTAGTAGGTTGAGGCCGTT GAGCACCGCCGCCGCAAGGAATGGTGCATGCAAGGAGATGGCGCCCAACAGTCCCCC GGCCACGGGGCCTGCCACCATACCCACGCCGAAACAAGCGCTCATGAGCCCGAAGTG GCGAGCCCGATCTTCCCCATCGGTGATGTCGGCGATATAGGCGCCAGCAACCGCACC TGTGGCGCCGGTGATGCCGGCCACGATGCGTCCGGCGTAGAGGATCGAGATCGATCT CGATCCCGCGAAATTAATACGACTCACTATA SEQ ID NO:28 – Sequence of vector that expresses one woodchuck hepatitis virus monomer subunit (containing Barstar binding protein) GGGGAATTGTGAGCGGATAACAATTCCCCTCTAGAAATAATTTTGTTTAACTTTAAGAAG GAGATATACCATGGACATCGACCCATACAAAGAATTTGGAAGTAGTTACCAGCTTCTGA ATTTCTTACCTCTTGACTTCTTTCCAGACTTGAACGCGCTGGTAGACACAGCGACAGCT TTATATGAAGAGGAGCTGACAGGCCGCGAGCACTGCTCACCTCATCATACGGCCATCG ATCAAGCACTGGTATGCTGGGATGAGTTGACTAAGTTGATTGCTGACATGTCATCTAAC ATCACCTCCAAAGCAGCGGCCGAGAAGGCAGCAGCAGAAAAAAAGGCTGTAATTAACG GTGAGCAGATCCGCAGTATTAGCGACTTACACCAAACATTGAAAAAGGAACTTGCCTTA CCCGAGTACTATGGCGAAAACCTGGATGCTCTGTGGGACGCTTTAACAGGATGGGTCG AGTACCCGTTGGTGTTAGAATGGCGCCAGTTCGAGCAGAGTAAGCAATTGACTGAGAA TGGTGCCGAATCCGTATTACAAGTATTCCGCGAAGCCAAGGCCGAGGGGGCAGATATC ACTATTGAACTGTCTAAAGCCGCGGCCGAACAGGTACGCACTATCATTGTGAACCATGT CAATGACACCTGGGGGTTAGATGTCCGTCAATCCCTTTGGTTTCATTTATCGTGCTTAA CTTTCGGTCAGCACACTGTTCAAGAGTTTCTGGTCTCGTTTGGAGTATGGATTCGCACG CCTGCGCCATATCGCCCGCCTAATGCGCCTATTCTGTCTACCTTGCCCGAACATACGGT TATTTAGTGAGCGGCCGCTTAACCTAGGCTGCTGCCACCGCTGAGCAATAACTAGCATA ACCCCTTGGGGCCTCTAAACGGGTCTTGAGGGGTTTTTTGTTGTACACGGCCGCATAAT AATACGACTCACTATAGGGGAATTGTGAGCGGATAACAATTCCCCTCTAGAAATAATTTT GTTTAACTTTAAGAAGGAGATATACCATGGATATTGATCCGTATAAAAAATTTGGCAGCA GCTATCAGCTGCTGAACTTTCTGCCGCTGGATTTTTTTCCGGATCTGAACGCGCTGGTG GATACCGCGACCGCGCTGTATGAAGAAGAACTGACCGGCCGCGAACATTGCAGCCCG CATCATACCGCGATTCGCCAAGCGCTGGTGTGCTGGGATAAACTGACCGAACTGATTG CGTGGATGAGCAGCAACATTACGAGCAAACAAGTGGATACCATTATTGTGAACAAAGTG AACGATACCTGGGGCCTGAAAGTGCGTCAGAGCCTGTGGTTTCATCTGAGCTGCCTGA CCTTTGGTCAGCATACCGTGCAAGAATTTCTGGTGAGCTTTGGCGTGTGGATTCGCACC CCGGCGCCGTATCGCCCGCCGAACGCGCCGATTCTGAGCACCCTGCCGGAACATACC GTGATTTAAGGTACCCTCGAGTCTGGTAAAGAAACCGCTGCTGCGAAATTTGAACGCCA GCACATGGACTCGTCTACTAGCGCAGCTTAATTAACCTAGGCTGCTGCCACCGCTGAG CAATAACTAGCATAACCCCTTGGGGCCTCTAAACGGGTCTTGAGGGGTTTTTTGCTGAA AGGAGGAACTATATCCGGATTGGCGAATGGGACGCGCCCTGTAGCGGCGCATTAAGC GCGGCGGGTGTGGTGGTTACGCGCAGCGTGACCGCTACACTTGCCAGCGCCCTAGCG CCCGCTCCTTTCGCTTTCTTCCCTTCCTTTCTCGCCACGTTCGCCGGCTTTCCCCGTCA AGCTCTAAATCGGGGGCTCCCTTTAGGGTTCCGATTTAGTGCTTTACGGCACCTCGACC CCAAAAAACTTGATTAGGGTGATGGTTCACGTAGTGGGCCATCGCCCTGATAGACGGT TTTTCGCCCTTTGACGTTGGAGTCCACGTTCTTTAATAGTGGACTCTTGTTCCAAACTGG AACAACACTCAACCCTATCTCGGTCTATTCTTTTGATTTATAAGGGATTTTGCCGATTTC GGCCTATTGGTTAAAAAATGAGCTGATTTAACAAAAATTTAACGCGAATTTTAACAAAAT ATTAACGTTTACAATTTCTGGCGGCACGATGGCATGAGATTATCAAAAAGGATCTTCAC CTAGATCCTTTTAAATTAAAAATGAAGTTTTAAATCAATCTAAAGTATATATGAGTAAAC T TGGTCTTtaGGACCCACTTTCACATTTAAGTTGTTTTTCTAATCCGCAgATGATCAATTC A AGGCCGAATAAGAAGGCTGGCTCTGCACCTTGGTGATCAAATAATTCGATAGCTTGTCG TAATAATGGCGGCATACTATCAGTAGTAGGTGTTTCCCTTTCTTCTTTAGCGACTTGATG CTCTTGATCTTCCAATACGCAACCTAAAGTAAAATGCCCCACAGCGCTGAGTGCATATA ATGCATTCTCTAGTGAAAAACCTTGTTGGCATAAAAAGGCTAATTGATTTTCGAGAGTTT CATACTGTTTTTCTGTAGGCCGTGTACCTAAATGTACTTTTGCTCCATCGCGATGACTTA GTAAAGCACATCTAAAACTTTTAGCGTTATTACGTAAAAAATCTTGCCAGCTTTCCCCTT CTAAAGGGCAAAAGTGAGTATGGTGCCTATCTAACATCTCAATGGCTAAGGCGTCGAG CAAAGCCCGCTTATTTTTTACATGCCAATACAATGTAGGCTGCTCTACACCTAGCTTCTG GGCGAGTTTACGGGTTGTTAAACCTTCGATTCCGACCTCATTAAGCAGCTCTAATGCGC TGTTAATCACTTTACTTTTATCTAATCTAGACATcattaattccTACCAATGCTTAATCA GTGAG GCACCTATCTCAGCGATCTGTCTATTTCGTTCATCCATAGTTGCCTGACTCCCCGTCGT GTAGATAACTACGATACGGGAGGGCTTACCATCTGGCCCCAGTGCTGCAATGATACCG CGAGACCCACGCTCACCGGCTCCAGATTTATCAGCAATAAACCAGCCAGCCGGAAGGG CCGAGCGCAGAAGTGGTCCTGCAACTTTATCCGCCTCCATCCAGTCTATTAATTGTTGC CGGGAAGCTAGAGTAAGTAGTTCGCCAGTTAATAGTTTGCGCAACGTTGTTGCCATTGC TACAGGCATCGTGGTGTCACGCTCGTCGTTTGGTATGGCTTCATTCAGCTCCGGTTCCC AACGATCAAGGCGAGTTACATGATCCCCCATGTTGTGCAAAAAAGCGGTTAGCTCCTTC GGTCCTCCGATCGTTGTCAGAAGTAAGTTGGCCGCAGTGTTATCACTCATGGTTATGGC AGCACTGCATAATTCTCTTACTGTCATGCCATCCGTAAGATGCTTTTCTGTGACTGGTGA GTACTCAACCAAGTCATTCTGAGAATAGTGTATGCGGCGACCGAGTTGCTCTTGCCCG GCGTCAATACGGGATAATACCGCGCCACATAGCAGAACTTTAAAAGTGCTCATCATTGG AAAACGTTCTTCGGGGCGAAAACTCTCAAGGATCTTACCGCTGTTGAGATCCAGTTCGA TGTAACCCACTCGTGCACCCAACTGATCTTCAGCATCTTTTACTTTCACCAGCGTTTCTG GGTGAGCAAAAACAGGAAGGCAAAATGCCGCAAAAAAGGGAATAAGGGCGACACGGA AATGTTGAATACTCATACTCTTCCTTTTTCAATCATGATTGAAGCATTTATCAGGGTTAT T GTCTCATGAGCGGATACATATTTGAATGTATTTAGAAAAATAAACAAATAGGTCATGACC AAAATCCCTTAACGTGAGTTTTCGTTCCACTGAGCGTCAGACCCCGTAGAAAAGATCAA AGGATCTTCTTGAGATCCTTTTTTTCTGCGCGTAATCTGCTGCTTGCAAACAAAAAAACC ACCGCTACCAGCGGTGGTTTGTTTGCCGGATCAAGAGCTACCAACTCTTTTTCCGAAGG TAACTGGCTTCAGCAGAGCGCAGATACCAAATACTGTCCTTCTAGTGTAGCCGTAGTTA GGCCACCACTTCAAGAACTCTGTAGCACCGCCTACATACCTCGCTCTGCTAATCCTGTT ACCAGTGGCTGCTGCCAGTGGCGATAAGTCGTGTCTTACCGGGTTGGACTCAAGACGA TAGTTACCGGATAAGGCGCAGCGGTCGGGCTGAACGGGGGGTTCGTGCACACAGCCC AGCTTGGAGCGAACGACCTACACCGAACTGAGATACCTACAGCGTGAGCTATGAGAAA GCGCCACGCTTCCCGAAGGGAGAAAGGCGGACAGGTATCCGGTAAGCGGCAGGGTC GGAACAGGAGAGCGCACGAGGGAGCTTCCAGGGGGAAACGCCTGGTATCTTTATAGT CCTGTCGGGTTTCGCCACCTCTGACTTGAGCGTCGATTTTTGTGATGCTCGTCAGGGG GGCGGAGCCTATGGAAAAACGCCAGCAACGCGGCCTTTTTACGGTTCCTGGCCTTTTG CTGGCCTTTTGCTCACATGTTCTTTCCTGCGTTATCCCCTGATTCTGTGGATAACCGTAT TACCGCCTTTGAGTGAGCTGATACCGCTCGCCGCAGCCGAACGACCGAGCGCAGCGA GTCAGTGAGCGAGGAAGCGGAAGAGCGCCTGATGCGGTATTTTCTCCTTACGCATCTG TGCGGTATTTCACACCGCATATATGGTGCACTCTCAGTACAATCTGCTCTGATGCCGCA TAGTTAAGCCAGTATACACTCCGCTATCGCTACGTGACTGGGTCATGGCTGCGCCCCG ACACCCGCCAACACCCGCTGACGCGCCCTGACGGGCTTGTCTGCTCCCGGCATCCGC TTACAGACAAGCTGTGACCGTCTCCGGGAGCTGCATGTGTCAGAGGTTTTCACCGTCA TCACCGAAACGCGCGAGGCAGCTGCGGTAAAGCTCATCAGCGTGGTCGTGAAGCGAT TCACAGATGTCTGCCTGTTCATCCGCGTCCAGCTCGTTGAGTTTCTCCAGAAGCGTTAA TGTCTGGCTTCTGATAAAGCGGGCCATGTTAAGGGCGGTTTTTTCCTGTTTGGTCACTG ATGCCTCCGTGTAAGGGGGATTTCTGTTCATGGGGGTAATGATACCGATGAAACGAGA GAGGATGCTCACGATACGGGTTACTGATGATGAACATGCCCGGTTACTGGAACGTTGT GAGGGTAAACAACTGGCGGTATGGATGCGGCGGGACCAGAGAAAAATCACTCAGGGT CAATGCCAGCGCTTCGTTAATACAGATGTAGGTGTTCCACAGGGTAGCCAGCAGCATC CTGCGATGCAGATCCGGAACATAATGGTGCAGGGCGCTGACTTCCGCGTTTCCAGACT TTACGAAACACGGAAACCGAAGACCATTCATGTTGTTGCTCAGGTCGCAGACGTTTTGC AGCAGCAGTCGCTTCACGTTCGCTCGCGTATCGGTGATTCATTCTGCTAACCAGTAAGG CAACCCCGCCAGCCTAGCCGGGTCCTCAACGACAGGAGCACGATCATGCTAGTCATGC CCCGCGCCCACCGGAAGGAGCTGACTGGGTTGAAGGCTCTCAAGGGCATCGGTCGAG ATCCCGGTGCCTAATGAGTGAGCTAACTTACATTAATTGCGTTGCGCTCACTGCCCGCT TTCCAGTCGGGAAACCTGTCGTGCCAGCTGCATTAATGAATCGGCCAACGCGCGGGGA GAGGCGGTTTGCGTATTGGGCGCCAGGGTGGTTTTTCTTTTCACCAGTGAGACGGGCA ACAGCTGATTGCCCTTCACCGCCTGGCCCTGAGAGAGTTGCAGCAAGCGGTCCACGCT GGTTTGCCCCAGCAGGCGAAAATCCTGTTTGATGGTGGTTAACGGCGGGATATAACAT GAGCTGTCTTCGGTATCGTCGTATCCCACTACCGAGATGTCCGCACCAACGCGCAGCC CGGACTCGGTAATGGCGCGCATTGCGCCCAGCGCCATCTGATCGTTGGCAACCAGCAT CGCAGTGGGAACGATGCCCTCATTCAGCATTTGCATGGTTTGTTGAAAACCGGACATG GCACTCCAGTCGCCTTCCCGTTCCGCTATCGGCTGAATTTGATTGCGAGTGAGATATTT ATGCCAGCCAGCCAGACGCAGACGCGCCGAGACAGAACTTAATGGGCCCGCTAACAG CGCGATTTGCTGGTGACCCAATGCGACCAGATGCTCCACGCCCAGTCGCGTACCGTCT TCATGGGAGAAAATAATACTGTTGATGGGTGTCTGGTCAGAGACATCAAGAAATAACGC CGGAACATTAGTGCAGGCAGCTTCCACAGCAATGGCATCCTGGTCATCCAGCGGATAG TTAATGATCAGCCCACTGACGCGTTGCGCGAGAAGATTGTGCACCGCCGCTTTACAGG CTTCGACGCCGCTTCGTTCTACCATCGACACCACCACGCTGGCACCCAGTTGATCGGC GCGAGATTTAATCGCCGCGACAATTTGCGACGGCGCGTGCAGGGCCAGACTGGAGGT GGCAACGCCAATCAGCAACGACTGTTTGCCCGCCAGTTGTTGTGCCACGCGGTTGGGA ATGTAATTCAGCTCCGCCATCGCCGCTTCCACTTTTTCCCGCGTTTTCGCAGAAACGTG GCTGGCCTGGTTCACCACGCGGGAAACGGTCTGATAAGAGACACCGGCATACTCTGC GACATCGTATAACGTTACTGGTTTCACATTCACCACCCTGAATTGACTCTCTTCCGGGC GCTATCATGCCATACCGCGAAAGGTTTTGCGCCATTCGATGGTGTCCGGGATCTCGAC GCTCTCCCTTATGCGACTCCTGCATTAGGAAGCAGCCCAGTAGTAGGTTGAGGCCGTT GAGCACCGCCGCCGCAAGGAATGGTGCATGCAAGGAGATGGCGCCCAACAGTCCCCC GGCCACGGGGCCTGCCACCATACCCACGCCGAAACAAGCGCTCATGAGCCCGAAGTG GCGAGCCCGATCTTCCCCATCGGTGATGTCGGCGATATAGGCGCCAGCAACCGCACC TGTGGCGCCGGTGATGCCGGCCACGATGCGTCCGGCGTAGAGGATCGAGATCGATCT CGATCCCGCGAAATTAATACGACTCACTATA SEQ ID NO:29 – Sequence of vector that expresses one woodchuck hepatitis virus monomer subunit (without a binding protein) GGGGAATTGTGAGCGGATAACAATTCCCCTCTAGAAATAATTTTGTTTAACTTTAAGAAG GAGATATACCATGgcacaggttatcaacacgtttgacggggttgcggattatcttcagac atatcataagctacctgataat tacattacaaaatcagaagcacaagccctcggctgggtggcatcaaaagggaaccttgca gacgtcgctccggggaaaagc atcggcggagacatcttctcaaacagggaaggcaaactcccgggcaaaagcggacgaaca tggcgtTGGgcggatattaa ctatacatcaggcttcagaaattcagaccggattctttactcaagcgactggctgattta caaaacaacggaccattatcagaccttt acaaaaatcagaGGAGGTTTAGCTGAGGCAGCTGCTAAGGAAGCTGCCGCAAAGGCTGCA AAAGAAGATCTGCGCACCACCATTGATCTGCTGAAACAGGAAAGCCAGGATCTGTATAA CAACTATAGCATTAAACAGGCGAGCGGCATGAGCGCGGATGAAAGCATTCAGCTGCCG TGCTTTAGCCTGGATCGCGAAGCGCTGACCAACATTAGCGTGATTATTGCGCATCTGGA AAAAGTGAAAGTGCTGAGCGAAAACACCGTGGATACCAGCTGGGTGATTCGCTGGCTG ACCAACATTAGCTGCTTTAACCCGCTGAACCTGAACATTAGCGTGCCGGGCAACACCG ATGAAAGCTATGATTGCGCGGTGTTTGTGCTGACCGTGCTGAAACAGTTTAGCAACTGC ATGGCGGAACTGCAGGCGAAGGACCACGACCACGACCACGACCACGACCACGAGtaata aGGTACCCTCGAGTCTGGTAAAGAAACCGCTGCTGCGAAATTTGAACGCCAGCACATG GACTCGTCTACTAGCGCAGCTTAATTAACCTAGGCTGCTGCCACCGCTGAGCAATAACT AGCATAACCCCTTGGGGCCTCTAAACGGGTCTTGAGGGGTTTTTTGCTGAAAGGAGGA ACTATATCCGGATTGGCGAATGGGACGCGCCCTGTAGCGGCGCATTAAGCGCGGCGG GTGTGGTGGTTACGCGCAGCGTGACCGCTACACTTGCCAGCGCCCTAGCGCCCGCTC CTTTCGCTTTCTTCCCTTCCTTTCTCGCCACGTTCGCCGGCTTTCCCCGTCAAGCTCTA AATCGGGGGCTCCCTTTAGGGTTCCGATTTAGTGCTTTACGGCACCTCGACCCCAAAAA ACTTGATTAGGGTGATGGTTCACGTAGTGGGCCATCGCCCTGATAGACGGTTTTTCGC CCTTTGACGTTGGAGTCCACGTTCTTTAATAGTGGACTCTTGTTCCAAACTGGAACAAC ACTCAACCCTATCTCGGTCTATTCTTTTGATTTATAAGGGATTTTGCCGATTTCGGCCTA TTGGTTAAAAAATGAGCTGATTTAACAAAAATTTAACGCGAATTTTAACAAAATATTAAC G TTTACAATTTCTGGCGGCACGATGGCATGAGATTATCAAAAAGGATCTTCACCTAGATC CTTTTAAATTAAAAATGAAGTTTTAAATCAATCTAAAGTATATATGAGTAAACTTGGTCT Tt aGGACCCACTTTCACATTTAAGTTGTTTTTCTAATCCGCAgATGATCAATTCAAGGCCGA ATAAGAAGGCTGGCTCTGCACCTTGGTGATCAAATAATTCGATAGCTTGTCGTAATAAT GGCGGCATACTATCAGTAGTAGGTGTTTCCCTTTCTTCTTTAGCGACTTGATGCTCTTGA TCTTCCAATACGCAACCTAAAGTAAAATGCCCCACAGCGCTGAGTGCATATAATGCATT CTCTAGTGAAAAACCTTGTTGGCATAAAAAGGCTAATTGATTTTCGAGAGTTTCATACTG TTTTTCTGTAGGCCGTGTACCTAAATGTACTTTTGCTCCATCGCGATGACTTAGTAAAGC ACATCTAAAACTTTTAGCGTTATTACGTAAAAAATCTTGCCAGCTTTCCCCTTCTAAAGG GCAAAAGTGAGTATGGTGCCTATCTAACATCTCAATGGCTAAGGCGTCGAGCAAAGCC CGCTTATTTTTTACATGCCAATACAATGTAGGCTGCTCTACACCTAGCTTCTGGGCGAG TTTACGGGTTGTTAAACCTTCGATTCCGACCTCATTAAGCAGCTCTAATGCGCTGTTAAT CACTTTACTTTTATCTAATCTAGACATcattaattccTACCAATGCTTAATCAGTGAGGC ACCT ATCTCAGCGATCTGTCTATTTCGTTCATCCATAGTTGCCTGACTCCCCGTCGTGTAGATA ACTACGATACGGGAGGGCTTACCATCTGGCCCCAGTGCTGCAATGATACCGCGAGACC CACGCTCACCGGCTCCAGATTTATCAGCAATAAACCAGCCAGCCGGAAGGGCCGAGC GCAGAAGTGGTCCTGCAACTTTATCCGCCTCCATCCAGTCTATTAATTGTTGCCGGGAA GCTAGAGTAAGTAGTTCGCCAGTTAATAGTTTGCGCAACGTTGTTGCCATTGCTACAGG CATCGTGGTGTCACGCTCGTCGTTTGGTATGGCTTCATTCAGCTCCGGTTCCCAACGAT CAAGGCGAGTTACATGATCCCCCATGTTGTGCAAAAAAGCGGTTAGCTCCTTCGGTCCT CCGATCGTTGTCAGAAGTAAGTTGGCCGCAGTGTTATCACTCATGGTTATGGCAGCACT GCATAATTCTCTTACTGTCATGCCATCCGTAAGATGCTTTTCTGTGACTGGTGAGTACTC AACCAAGTCATTCTGAGAATAGTGTATGCGGCGACCGAGTTGCTCTTGCCCGGCGTCA ATACGGGATAATACCGCGCCACATAGCAGAACTTTAAAAGTGCTCATCATTGGAAAACG TTCTTCGGGGCGAAAACTCTCAAGGATCTTACCGCTGTTGAGATCCAGTTCGATGTAAC CCACTCGTGCACCCAACTGATCTTCAGCATCTTTTACTTTCACCAGCGTTTCTGGGTGA GCAAAAACAGGAAGGCAAAATGCCGCAAAAAAGGGAATAAGGGCGACACGGAAATGTT GAATACTCATACTCTTCCTTTTTCAATCATGATTGAAGCATTTATCAGGGTTATTGTCTC A TGAGCGGATACATATTTGAATGTATTTAGAAAAATAAACAAATAGGTCATGACCAAAATC CCTTAACGTGAGTTTTCGTTCCACTGAGCGTCAGACCCCGTAGAAAAGATCAAAGGATC TTCTTGAGATCCTTTTTTTCTGCGCGTAATCTGCTGCTTGCAAACAAAAAAACCACCGCT ACCAGCGGTGGTTTGTTTGCCGGATCAAGAGCTACCAACTCTTTTTCCGAAGGTAACTG GCTTCAGCAGAGCGCAGATACCAAATACTGTCCTTCTAGTGTAGCCGTAGTTAGGCCAC CACTTCAAGAACTCTGTAGCACCGCCTACATACCTCGCTCTGCTAATCCTGTTACCAGT GGCTGCTGCCAGTGGCGATAAGTCGTGTCTTACCGGGTTGGACTCAAGACGATAGTTA CCGGATAAGGCGCAGCGGTCGGGCTGAACGGGGGGTTCGTGCACACAGCCCAGCTTG GAGCGAACGACCTACACCGAACTGAGATACCTACAGCGTGAGCTATGAGAAAGCGCCA CGCTTCCCGAAGGGAGAAAGGCGGACAGGTATCCGGTAAGCGGCAGGGTCGGAACAG GAGAGCGCACGAGGGAGCTTCCAGGGGGAAACGCCTGGTATCTTTATAGTCCTGTCG GGTTTCGCCACCTCTGACTTGAGCGTCGATTTTTGTGATGCTCGTCAGGGGGGCGGAG CCTATGGAAAAACGCCAGCAACGCGGCCTTTTTACGGTTCCTGGCCTTTTGCTGGCCTT TTGCTCACATGTTCTTTCCTGCGTTATCCCCTGATTCTGTGGATAACCGTATTACCGCCT TTGAGTGAGCTGATACCGCTCGCCGCAGCCGAACGACCGAGCGCAGCGAGTCAGTGA GCGAGGAAGCGGAAGAGCGCCTGATGCGGTATTTTCTCCTTACGCATCTGTGCGGTAT TTCACACCGCATATATGGTGCACTCTCAGTACAATCTGCTCTGATGCCGCATAGTTAAG CCAGTATACACTCCGCTATCGCTACGTGACTGGGTCATGGCTGCGCCCCGACACCCGC CAACACCCGCTGACGCGCCCTGACGGGCTTGTCTGCTCCCGGCATCCGCTTACAGACA AGCTGTGACCGTCTCCGGGAGCTGCATGTGTCAGAGGTTTTCACCGTCATCACCGAAA CGCGCGAGGCAGCTGCGGTAAAGCTCATCAGCGTGGTCGTGAAGCGATTCACAGATG TCTGCCTGTTCATCCGCGTCCAGCTCGTTGAGTTTCTCCAGAAGCGTTAATGTCTGGCT TCTGATAAAGCGGGCCATGTTAAGGGCGGTTTTTTCCTGTTTGGTCACTGATGCCTCCG TGTAAGGGGGATTTCTGTTCATGGGGGTAATGATACCGATGAAACGAGAGAGGATGCT CACGATACGGGTTACTGATGATGAACATGCCCGGTTACTGGAACGTTGTGAGGGTAAA CAACTGGCGGTATGGATGCGGCGGGACCAGAGAAAAATCACTCAGGGTCAATGCCAG CGCTTCGTTAATACAGATGTAGGTGTTCCACAGGGTAGCCAGCAGCATCCTGCGATGC AGATCCGGAACATAATGGTGCAGGGCGCTGACTTCCGCGTTTCCAGACTTTACGAAAC ACGGAAACCGAAGACCATTCATGTTGTTGCTCAGGTCGCAGACGTTTTGCAGCAGCAG TCGCTTCACGTTCGCTCGCGTATCGGTGATTCATTCTGCTAACCAGTAAGGCAACCCCG CCAGCCTAGCCGGGTCCTCAACGACAGGAGCACGATCATGCTAGTCATGCCCCGCGC CCACCGGAAGGAGCTGACTGGGTTGAAGGCTCTCAAGGGCATCGGTCGAGATCCCGG TGCCTAATGAGTGAGCTAACTTACATTAATTGCGTTGCGCTCACTGCCCGCTTTCCAGT CGGGAAACCTGTCGTGCCAGCTGCATTAATGAATCGGCCAACGCGCGGGGAGAGGCG GTTTGCGTATTGGGCGCCAGGGTGGTTTTTCTTTTCACCAGTGAGACGGGCAACAGCT GATTGCCCTTCACCGCCTGGCCCTGAGAGAGTTGCAGCAAGCGGTCCACGCTGGTTTG CCCCAGCAGGCGAAAATCCTGTTTGATGGTGGTTAACGGCGGGATATAACATGAGCTG TCTTCGGTATCGTCGTATCCCACTACCGAGATGTCCGCACCAACGCGCAGCCCGGACT CGGTAATGGCGCGCATTGCGCCCAGCGCCATCTGATCGTTGGCAACCAGCATCGCAGT GGGAACGATGCCCTCATTCAGCATTTGCATGGTTTGTTGAAAACCGGACATGGCACTCC AGTCGCCTTCCCGTTCCGCTATCGGCTGAATTTGATTGCGAGTGAGATATTTATGCCAG CCAGCCAGACGCAGACGCGCCGAGACAGAACTTAATGGGCCCGCTAACAGCGCGATT TGCTGGTGACCCAATGCGACCAGATGCTCCACGCCCAGTCGCGTACCGTCTTCATGGG AGAAAATAATACTGTTGATGGGTGTCTGGTCAGAGACATCAAGAAATAACGCCGGAACA TTAGTGCAGGCAGCTTCCACAGCAATGGCATCCTGGTCATCCAGCGGATAGTTAATGAT CAGCCCACTGACGCGTTGCGCGAGAAGATTGTGCACCGCCGCTTTACAGGCTTCGACG CCGCTTCGTTCTACCATCGACACCACCACGCTGGCACCCAGTTGATCGGCGCGAGATT TAATCGCCGCGACAATTTGCGACGGCGCGTGCAGGGCCAGACTGGAGGTGGCAACGC CAATCAGCAACGACTGTTTGCCCGCCAGTTGTTGTGCCACGCGGTTGGGAATGTAATT CAGCTCCGCCATCGCCGCTTCCACTTTTTCCCGCGTTTTCGCAGAAACGTGGCTGGCC TGGTTCACCACGCGGGAAACGGTCTGATAAGAGACACCGGCATACTCTGCGACATCGT ATAACGTTACTGGTTTCACATTCACCACCCTGAATTGACTCTCTTCCGGGCGCTATCAT GCCATACCGCGAAAGGTTTTGCGCCATTCGATGGTGTCCGGGATCTCGACGCTCTCCC TTATGCGACTCCTGCATTAGGAAGCAGCCCAGTAGTAGGTTGAGGCCGTTGAGCACCG CCGCCGCAAGGAATGGTGCATGCAAGGAGATGGCGCCCAACAGTCCCCCGGCCACGG GGCCTGCCACCATACCCACGCCGAAACAAGCGCTCATGAGCCCGAAGTGGCGAGCCC GATCTTCCCCATCGGTGATGTCGGCGATATAGGCGCCAGCAACCGCACCTGTGGCGC CGGTGATGCCGGCCACGATGCGTCCGGCGTAGAGGATCGAGATCGATCTCGATCCCG CGAAATTAATACGACTCACTATA SEQ ID NO:30 – Sequence of vector that expresses one woodchuck hepatitis virus capsid monomer subunit (without a binding protein), one woodchuck hepatitis virus capsid monomer subunit including a binding protein (lm7), and an epitope protein ( modified murine IL31) fused to both Colicin E7 (via an alpha helical linker) and an affinity ligand (internal ID DU73351).GGGGAATTGTGAGCGGATAACAATTCCCCTCTAGAAATAATTTTGTTTAAC TT TAAGAAGGAGATATACCATGGACATCGATCCATATAAGGAGTTTGGCTCCTCATACCAA TTACTTAATTTCCTTCCCTTGGACTTTTTCCCCGACCTTAACGCCCTGGTTGACACGGCT ACGGCGCTTTACGAAGAGGAATTAACGGGGCGTGAACATTGTTCACCTCATCACACGG CCATTGATCAAGCGTTGGTATGCTGGGATGAACTTACGAAACTGATTGCCGATATGAGT TCAAATATTACGAGCAAAGCAGCAGCCGAGAAGGCAGCAGCCGAAGAACTGAAAAATA GCATTTCAGACTACACCGAAGCAGAATTTGTGCAGTTACTGAAAGAGATCGAGAAGGAG AACGTAGCCGCAACCGATGACGTGCTTGATGTCCTGCTTGAACATTTAGTAAAGATTAC GGAACATCCAGACGGTACGGATTTAATCTATTATCCTAGTGACAATCGCGACGACAGTC CAGAAGGCATCGTAAAGGAGATTAAAGAATGGCGTGCTGCAAACGGAAAGCCTGGGTT TAAGCAGGGTGGAAAAGCTGCGGCAGAACAGGTGCGTACCATTATCGTAAATCACGTC AATGATACCTGGGGTCTTGATGTTCGTCAGTCCCTGTGGTTTCACCTTTCATGCTTGAC GTTTGGTCAGCACACAGTACAGGAGTTCCTTGTTTCTTTCGGGGTATGGATTCGTACAC CAGCTCCTTATCGCCCTCCTAACGCACCTATTTTATCCACGTTACCTGAACATACCGTTA TTTAGTGAGCGGCCGCTTAACCTAGGCTGCTGCCACCGCTGAGCAATAACTAGCATAA CCCCTTGGGGCCTCTAAACGGGTCTTGAGGGGTTTTTTGTTGTACACGGCCGCATAATA ATACGACTCACTATAGGGGAATTGTGAGCGGATAACAATTCCCCTCTAGAAATAATTTTG TTTAACTTTAAGAAGGAGATATACCATGGATATTGATCCGTATAAAAAATTTGGCAGCAG CTATCAGCTGCTGAACTTTCTGCCGCTGGATTTTTTTCCGGATCTGAACGCGCTGGTGG ATACCGCGACCGCGCTGTATGAAGAAGAACTGACCGGCCGCGAACATTGCAGCCCGC ATCATACCGCGATTCGCCAAGCGCTGGTGTGCTGGGATAAACTGACCGAACTGATTGC GTGGATGAGCAGCAACATTACGAGCAAACAAGTGGATACCATTATTGTGAACAAAGTGA ACGATACCTGGGGCCTGAAAGTGCGTCAGAGCCTGTGGTTTCATCTGAGCTGCCTGAC CTTTGGTCAGCATACCGTGCAAGAATTTCTGGTGAGCTTTGGCGTGTGGATTCGCACCC CGGCGCCGTATCGCCCGCCGAACGCGCCGATTCTGAGCACCCTGCCGGAACATACCG TGATTTAATAAGCGGCCGCTTAACCTAGGCTGCTGCCACCGCTGAGCAATAACTAGCAT AACCCCTTGGGGCCTCTAAACGGGTCTTGAGGGGTTTTTTGTTGTACACGGCCGCATA ATCGgttgacactctatcattgatagagttattttaccactccctatcagtgatagagaa Aagtgaaatgaatagttcgacaaaa atctagataacgagggcaaCATATGGAGAGTAAACGGAATAAGCCAGGGAAGGCAACAGG TAA AGGAAAACCTGTCAATAATAAGTGGTTAAATAATGCAGGTAAAGACTTAGGTTCTCCTGT TCCAGATCGTATAGCTAATAAACTACGTGATAAGGAGTTTAAAAGTTTCGATGATTTTCG TAAGAAATTCTGGGAAGAAGTGTCAAAAGATCCTGAGTTAAGTAAACAATTTAGTCGAAA CAATAATGATCGAATGAAGGTTGGAAAAGCGCCCAAGACTAGAACCCAGGATGTTTCAG GGAAGGCAACTTCATTCGCACTTCATCATGAGAAGCCGATCAGCCAAAATGGTGGTGT CTATGATATGGATAACATCAGCGTGGTAACACCTAAACGTGCTATTGATATTCACCGACT GGCGGAAGCGGCGGCGAAAGAAGCGGCGGCGAAAGAAGCGGCGAAAGCGGCGAAAG AAGATCTGCGCACCACCATTGATCTGCTGAAACAGGAAAGCCAGGATCTGTATAACAAC TATAGCATTAAACAGGCGAGCGGCATGAGCGCGGATGAAAGCATTCAGCTGCCGTGCT TTAGCCTGGATCGCGAAGCGCTGACCAACATTAGCGTGATTATTGCGCATCTGGAAAAA GTGAAAGTGCTGAGCGAAAACACCGTGGATACCAGCTGGGTGATTCGCTGGCTGACCA ACATTAGCTGCTTTAACCCGCTGAACCTGAACATTAGCGTGCCGGGCAACACCGATGA AAGCTATGATTGCGCGGTGTTTGTGCTGACCGTGCTGAAACAGTTTAGCAACTGCATGG CGGAACTGCAGGCGGGCAGCGGCGGCAGCCATGATCATGATCATGATCATGATCATGA AtaataaGGTACCgTCGAGTCTGGTAAAGAAACCGCTGCTGCGAAATTTGAACGCCAGCA CATGGACTCGTCTACTAGCGCAGCTTAATTAACCTAGGCTGCTGCCACCGCTGAGCAAT AACTAGCATAACCCCTTGGGGCCTCTAAACGGGTCTTGAGGGGTTTTTTGCTGAAAGGA GGAACTATATCCGGATTGGCGAATGGGACGCGCCCTGTAGCGGCGCATTAAGCGCGG CGGGTGTGGTGGTTACGCGCAGCGTGACCGCTACACTTGCCAGCGCCCTAGCGCCCG CTCCTTTCGCTTTCTTCCCTTCCTTTCTCGCCACGTTCGCCGGCTTTCCCCGTCAAGCT CTAAATCGGGGGCTCCCTTTAGGGTTCCGATTTAGTGCTTTACGGCACCTCGACCCCAA AAAACTTGATTAGGGTGATGGTTCACGTAGTGGGCCATCGCCCTGATAGACGGTTTTTC GCCCTTTGACGTTGGAGTCCACGTTCTTTAATAGTGGACTCTTGTTCCAAACTGGAACA ACACTCAACCCTATCTCGGTCTATTCTTTTGATTTATAAGGGATTTTGCCGATTTCGGCC TATTGGTTAAAAAATGAGCTGATTTAACAAAAATTTAACGCGAATTTTAACAAAATATTA A CGTTTACAATTTCTGGCGGCACGATGGCATGAGATTATCAAAAAGGATCTTCACCTAGA TCCTTTTAAATTAAAAATGAAGTTTTAAATCAATCTAAAGTATATATGAGTAAACTTGGT C TTtaGGACCCACTTTCACATTTAAGTTGTTTTTCTAATCCGCAgATGATCAATTCAAGGC C GAATAAGAAGGCTGGCTCTGCACCTTGGTGATCAAATAATTCGATAGCTTGTCGTAATA ATGGCGGCATACTATCAGTAGTAGGTGTTTCCCTTTCTTCTTTAGCGACTTGATGCTCTT GATCTTCCAATACGCAACCTAAAGTAAAATGCCCCACAGCGCTGAGTGCATATAATGCA TTCTCTAGTGAAAAACCTTGTTGGCATAAAAAGGCTAATTGATTTTCGAGAGTTTCATAC TGTTTTTCTGTAGGCCGTGTACCTAAATGTACTTTTGCTCCATCGCGATGACTTAGTAAA GCACATCTAAAACTTTTAGCGTTATTACGTAAAAAATCTTGCCAGCTTTCCCCTTCTAAA GGGCAAAAGTGAGTATGGTGCCTATCTAACATCTCAATGGCTAAGGCGTCGAGCAAAG CCCGCTTATTTTTTACATGCCAATACAATGTAGGCTGCTCTACACCTAGCTTCTGGGCG AGTTTACGGGTTGTTAAACCTTCGATTCCGACCTCATTAAGCAGCTCTAATGCGCTGTTA ATCACTTTACTTTTATCTAATCTAGACATcattaattccTACCAATGCTTAATCAGTGAG GCAC CTATCTCAGCGATCTGTCTATTTCGTTCATCCATAGTTGCCTGACTCCCCGTCGTGTAG ATAACTACGATACGGGAGGGCTTACCATCTGGCCCCAGTGCTGCAATGATACCGCGAG ACCCACGCTCACCGGCTCCAGATTTATCAGCAATAAACCAGCCAGCCGGAAGGGCCGA GCGCAGAAGTGGTCCTGCAACTTTATCCGCCTCCATCCAGTCTATTAATTGTTGCCGGG AAGCTAGAGTAAGTAGTTCGCCAGTTAATAGTTTGCGCAACGTTGTTGCCATTGCTACA GGCATCGTGGTGTCACGCTCGTCGTTTGGTATGGCTTCATTCAGCTCCGGTTCCCAAC GATCAAGGCGAGTTACATGATCCCCCATGTTGTGCAAAAAAGCGGTTAGCTCCTTCGGT CCTCCGATCGTTGTCAGAAGTAAGTTGGCCGCAGTGTTATCACTCATGGTTATGGCAGC ACTGCATAATTCTCTTACTGTCATGCCATCCGTAAGATGCTTTTCTGTGACTGGTGAGTA CTCAACCAAGTCATTCTGAGAATAGTGTATGCGGCGACCGAGTTGCTCTTGCCCGGCG TCAATACGGGATAATACCGCGCCACATAGCAGAACTTTAAAAGTGCTCATCATTGGAAA ACGTTCTTCGGGGCGAAAACTCTCAAGGATCTTACCGCTGTTGAGATCCAGTTCGATGT AACCCACTCGTGCACCCAACTGATCTTCAGCATCTTTTACTTTCACCAGCGTTTCTGGG TGAGCAAAAACAGGAAGGCAAAATGCCGCAAAAAAGGGAATAAGGGCGACACGGAAAT GTTGAATACTCATACTCTTCCTTTTTCAATCATGATTGAAGCATTTATCAGGGTTATTGT C TCATGAGCGGATACATATTTGAATGTATTTAGAAAAATAAACAAATAGGTCATGACCAAA ATCCCTTAACGTGAGTTTTCGTTCCACTGAGCGTCAGACCCCGTAGAAAAGATCAAAGG ATCTTCTTGAGATCCTTTTTTTCTGCGCGTAATCTGCTGCTTGCAAACAAAAAAACCACC GCTACCAGCGGTGGTTTGTTTGCCGGATCAAGAGCTACCAACTCTTTTTCCGAAGGTAA CTGGCTTCAGCAGAGCGCAGATACCAAATACTGTCCTTCTAGTGTAGCCGTAGTTAGGC CACCACTTCAAGAACTCTGTAGCACCGCCTACATACCTCGCTCTGCTAATCCTGTTACC AGTGGCTGCTGCCAGTGGCGATAAGTCGTGTCTTACCGGGTTGGACTCAAGACGATAG TTACCGGATAAGGCGCAGCGGTCGGGCTGAACGGGGGGTTCGTGCACACAGCCCAGC TTGGAGCGAACGACCTACACCGAACTGAGATACCTACAGCGTGAGCTATGAGAAAGCG CCACGCTTCCCGAAGGGAGAAAGGCGGACAGGTATCCGGTAAGCGGCAGGGTCGGAA CAGGAGAGCGCACGAGGGAGCTTCCAGGGGGAAACGCCTGGTATCTTTATAGTCCTGT CGGGTTTCGCCACCTCTGACTTGAGCGTCGATTTTTGTGATGCTCGTCAGGGGGGCGG AGCCTATGGAAAAACGCCAGCAACGCGGCCTTTTTACGGTTCCTGGCCTTTTGCTGGC CTTTTGCTCACATGTTCTTTCCTGCGTTATCCCCTGATTCTGTGGATAACCGTATTACCG CCTTTGAGTGAGCTGATACCGCTCGCCGCAGCCGAACGACCGAGCGCAGCGAGTCAG TGAGCGAGGAAGCGGAAGAGCGCCTGATGCGGTATTTTCTCCTTACGCATCTGTGCGG TATTTCACACCGCATATATGGTGCACTCTCAGTACAATCTGCTCTGATGCCGCATAGTTA AGCCAGTATACACTCCGCTATCGCTACGTGACTGGGTCATGGCTGCGCCCCGACACCC GCCAACACCCGCTGACGCGCCCTGACGGGCTTGTCTGCTCCCGGCATCCGCTTACAG ACAAGCTGTGACCGTCTCCGGGAGCTGCATGTGTCAGAGGTTTTCACCGTCATCACCG AAACGCGCGAGGCAGCTGCGGTAAAGCTCATCAGCGTGGTCGTGAAGCGATTCACAG ATGTCTGCCTGTTCATCCGCGTCCAGCTCGTTGAGTTTCTCCAGAAGCGTTAATGTCTG GCTTCTGATAAAGCGGGCCATGTTAAGGGCGGTTTTTTCCTGTTTGGTCACTGATGCCT CCGTGTAAGGGGGATTTCTGTTCATGGGGGTAATGATACCGATGAAACGAGAGAGGAT GCTCACGATACGGGTTACTGATGATGAACATGCCCGGTTACTGGAACGTTGTGAGGGT AAACAACTGGCGGTATGGATGCGGCGGGACCAGAGAAAAATCACTCAGGGTCAATGCC AGCGCTTCGTTAATACAGATGTAGGTGTTCCACAGGGTAGCCAGCAGCATCCTGCGAT GCAGATCCGGAACATAATGGTGCAGGGCGCTGACTTCCGCGTTTCCAGACTTTACGAA ACACGGAAACCGAAGACCATTCATGTTGTTGCTCAGGTCGCAGACGTTTTGCAGCAGC AGTCGCTTCACGTTCGCTCGCGTATCGGTGATTCATTCTGCTAACCAGTAAGGCAACCC CGCCAGCCTAGCCGGGTCCTCAACGACAGGAGCACGATCATGCTAGTCATGCCCCGC GCCCACCGGAAGGAGCTGACTGGGTTGAAGGCTCTCAAGGGCATCGGTCGAGATCCC GGTGCCTAATGAGTGAGCTAACTTACATTAATTGCGTTGCGCTCACTGCCCGCTTTCCA GTCGGGAAACCTGTCGTGCCAGCTGCATTAATGAATCGGCCAACGCGCGGGGAGAGG CGGTTTGCGTATTGGGCGCCAGGGTGGTTTTTCTTTTCACCAGTGAGACGGGCAACAG CTGATTGCCCTTCACCGCCTGGCCCTGAGAGAGTTGCAGCAAGCGGTCCACGCTGGTT TGCCCCAGCAGGCGAAAATCCTGTTTGATGGTGGTTAACGGCGGGATATAACATGAGC TGTCTTCGGTATCGTCGTATCCCACTACCGAGATGTCCGCACCAACGCGCAGCCCGGA CTCGGTAATGGCGCGCATTGCGCCCAGCGCCATCTGATCGTTGGCAACCAGCATCGCA GTGGGAACGATGCCCTCATTCAGCATTTGCATGGTTTGTTGAAAACCGGACATGGCACT CCAGTCGCCTTCCCGTTCCGCTATCGGCTGAATTTGATTGCGAGTGAGATATTTATGCC AGCCAGCCAGACGCAGACGCGCCGAGACAGAACTTAATGGGCCCGCTAACAGCGCGA TTTGCTGGTGACCCAATGCGACCAGATGCTCCACGCCCAGTCGCGTACCGTCTTCATG GGAGAAAATAATACTGTTGATGGGTGTCTGGTCAGAGACATCAAGAAATAACGCCGGAA CATTAGTGCAGGCAGCTTCCACAGCAATGGCATCCTGGTCATCCAGCGGATAGTTAAT GATCAGCCCACTGACGCGTTGCGCGAGAAGATTGTGCACCGCCGCTTTACAGGCTTCG ACGCCGCTTCGTTCTACCATCGACACCACCACGCTGGCACCCAGTTGATCGGCGCGAG ATTTAATCGCCGCGACAATTTGCGACGGCGCGTGCAGGGCCAGACTGGAGGTGGCAA CGCCAATCAGCAACGACTGTTTGCCCGCCAGTTGTTGTGCCACGCGGTTGGGAATGTA ATTCAGCTCCGCCATCGCCGCTTCCACTTTTTCCCGCGTTTTCGCAGAAACGTGGCTGG CCTGGTTCACCACGCGGGAAACGGTCTGATAAGAGACACCGGCATACTCTGCGACATC GTATAACGTTACTGGTTTCACATTCACCACCCTGAATTGACTCTCTTCCGGGCGCTATC ATGCCATACCGCGAAAGGTTTTGCGCCATTCGATGGTGTCCGGGATCTCGACGCTCTC CCTTATGCGACTCCTGCATTAGGAAGCAGCCCAGTAGTAGGTTGAGGCCGTTGAGCAC CGCCGCCGCAAGGAATGGTGCATGCAAGGAGATGGCGCCCAACAGTCCCCCGGCCAC GGGGCCTGCCACCATACCCACGCCGAAACAAGCGCTCATGAGCCCGAAGTGGCGAGC CCGATCTTCCCCATCGGTGATGTCGGCGATATAGGCGCCAGCAACCGCACCTGTGGC GCCGGTGATGCCGGCCACGATGCGTCCGGCGTAGAGGATCGAGATCGATCTCGATCC CGCGAAATTAATACGACTCACTATA SEQ ID NO:31 – Colicin E7 protein encoded by SEQ ID NO: 30 nts 1687-2082: ESKRNKPGKATGKGKPVNNKWLNNAGKDLGSPVPDRIANKLRDKEFKSFDDFRKKFWEEV SKDPELSKQFSRNNNDRMKVGKAPKTRTQDVSGKATSFALHHEKPISQNGGVYDMDNISV VTPKRAIDIHR SEQ ID NO:32 – Colicin E7 nucleic acid sequence used in SEQ ID NO: 30 nts 1687-2082 - DNA ATGGAGAGTAAACGGAATAAGCCAGGGAAGGCAACAGGTAAAGGAAAACCTGTCAATA ATAAGTGGTTAAATAATGCAGGTAAAGACTTAGGTTCTCCTGTTCCAGATCGTATAGCTA ATAAACTACGTGATAAGGAGTTTAAAAGTTTCGATGATTTTCGTAAGAAATTCTGGGAAG AAGTGTCAAAAGATCCTGAGTTAAGTAAACAATTTAGTCGAAACAATAATGATCGAATGA AGGTTGGAAAAGCGCCCAAGACTAGAACCCAGGATGTTTCAGGGAAGGCAACTTCATT CGCACTTCATCATGAGAAGCCGATCAGCCAAAATGGTGGTGTCTATGATATGGATAACA TCAGCGTGGTAACACCTAAACGTGCTATTGATATTCACCGA SEQ ID NO: 33 - Helix-Linker protein used in SEQ ID NO: 30 nts 2083-2136 between Colicin E7 and murine IL31 LAEAAAKEAAAKEAAKAA SEQ ID NO: 34 - nucleic acid sequence of Helix-Linker used in SEQ ID NO: 30 nts 2083-2136 between Colicin E7 and murine IL31 - DNA CTGGCGGAAGCGGCGGCGAAAGAAGCGGCGGCGAAAGAAGCGGCGAAAGCGGCG SEQ ID NO: 35 ––modified murine IL31 protein epitope - mIL31K/A (with specified receptor inactivating mutation K116->A) – encoded in SEQ ID NO: 30 by nt 2137-2505 KEDLRTTIDLLKQESQDLYNNYSIKQASGMSADESIQLPCFSLDREALTNISVIIAHLEK VKVL SENTVDTSWVIRWLTNISCFNPLNLNISVPGNTDESYDCAVFVLTVLKQFSNCMAELQA SEQ ID NO: 36 –nucleic acid sequence of modified murine IL31 epitope - mIL31K/A (with specified receptor inactivating mutation K116->A) –used in SEQ ID NO: 30 nts 2137-2505 – DNA AAAGAAGATCTGCGCACCACCATTGATCTGCTGAAACAGGAAAGCCAGGATCTGTATAA CAACTATAGCATTAAACAGGCGAGCGGCATGAGCGCGGATGAAAGCATTCAGCTGCCG TGCTTTAGCCTGGATCGCGAAGCGCTGACCAACATTAGCGTGATTATTGCGCATCTGGA AAAAGTGAAAGTGCTGAGCGAAAACACCGTGGATACCAGCTGGGTGATTCGCTGGCTG ACCAACATTAGCTGCTTTAACCCGCTGAACCTGAACATTAGCGTGCCGGGCAACACCG ATGAAAGCTATGATTGCGCGGTGTTTGTGCTGACCGTGCTGAAACAGTTTAGCAACTGC ATGGCGGAACTGCAGGCG SEQ ID NO: 37 - affinity tag protein used for purification – encoded in SEQ ID NO: 30 by nt 2506-2550 GSGGSHDHDHDHDHE SEQ ID NO: 38 – nucleic acid sequence of affinity tag used for purification – encoded in SEQ ID NO: 30 by nt 2506-2550 – DNA GGCAGCGGCGGCAGCCATGATCATGATCATGATCATGATCATGAA References: Jumper, J et al. Highly accurate protein structure prediction with AlphaFold. Nature (2021). Varadi, M et al. AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models. Nucleic Acids Research (2021). Kukreja et al. J Virol.2014 Dec;88(24):14105-15. doi: 10.1128/JVI.01840-14. Structurally similar woodchuck and human hepadnavirus core proteins have distinctly different temperature dependences of assembly Konczal et al, PLoS One 2019 14(4): e0215892, https://doi.org/10.1371/journal.pone.0215892 Re-introducing non-optimal synonymous codons into codon-optimized constructs enhances soluble recovery of recombinant proteins from Escherichia coli.