RNA delivery vehicle

Abstract

The present disclosure relates to an RNA delivery vehicle comprising lipid nanoparticles comprising the RNA therein, and a RNA-binding protein or peptide coated on the exterior surface of the lipid nanoparticle, and uses thereof.

Description

[0001] RNA DELIVERY VEHICLE RELATED APPLICATION DATA The present application claims priority from US Patent Application No. 63 / 494,274 filed on 5 April 2023 entitled “RNA Delivery Vehicle”. The entire contents of which is hereby incorporated by reference. SEQUENCE LISTING The present application is filed together with a Sequence Listing in electronic form. The entire contents of the Sequence Listing are hereby incorporated by reference. FIELD The present disclosure relates to a RNA delivery vehicle comprising lipid nanoparticles comprising the RNA therein, and a RNA-binding protein or peptide coated on the exterior surface of the lipid nanoparticle, and uses thereof. BACKGROUND Nucleic acid vaccines have recently emerged as a promising approach to the treatment and prevention of various diseases, including against the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) responsible for causing the on-going worldwide pandemic of the severely infectious coronavirus disease 2019 (COVID-19). mRNA vaccines rely on the delivery of the mRNA into the cytoplasm of host cells, where it is transcribed into antigenic proteins to trigger the production of neutralizing antibodies. However, the large size and negative charge of mRNA prevent cellular uptake. Therefore, lipid delivery vehicles, such as liposomes or lipid nanoparticles are used to encapsulate the mRNA, blocking degradation of the RNA in plasma, whilst also promoting cellular uptake for efficient delivery of the mRNA in vivo. However, the lipid nanoparticles may not encapsulate all of the mRNA and some mRNA may remain on the exterior surface of the lipid nanoparticle. Lipid delivery vehicles are commonly formed from cationic lipids and other ionisable lipid components such as neutral lipids, cholesterol and PEGylated lipids. Cationic lipids are amphiphilic molecules having a lipophilic region containing one or more hydrocarbon groups and a hydrophilic region containing at least one positively charged polar head group. Cationic lipids and nucleic acids form a positively charged complex, making it easier for the nucleic acids to pass through the plasma membrane of the cell and enter the cytoplasm. However, several adverse cytotoxic effects of cationic lipids are known including, production of reactive oxygen species and accumulation in plasma due to poor degradation by humans. Thus, much effort has focused on identifying novel lipids or particular lipid compositions that can protect nucleic acids from degradation and elimination, as well as provide effective intracellular delivery and / or expression / translation of mRNA. In addition, these lipid-nucleic acid particles must be well tolerated and provide an appropriate therapeutic index so that treatment with an effective dose of nucleic acid must not be associated with unacceptable toxicity and / or risk to the patient. Therefore, it will be apparent to the skilled person that there is an on-going need for improved lipid nanoparticles for delivery of oligonucleotides, such as RNA. SUMMARY In producing the present invention, the inventors’ identified that a RNA-binding protein or peptide coated on the exterior surface of a lipid nanoparticle may increase stability of the associated RNA and / or facilitate nucleation of the lipid nanoparticle and / or reduce the toxicity and / or adverse side effects of the lipid nanoparticle. The inventors have also identified that the RNA-binding protein or peptide coated on the exterior of the lipid nanoparticle may protect against toll-like receptor (TLR) stimulation / induction. Thus, providing the basis for an RNA delivery vehicle comprising a lipid nanoparticle comprising the RNA therein, and a RNA-binding protein or peptide coated on the exterior surface of the lipid nanoparticle and methods of use of the RNA delivery vehicle as a vaccine or as a therapeutic. The inventors additionally sought to identify a method for determining the quality of an RNA delivery vehicle (e.g., detecting exposed RNA on the RNA delivery vehicle which can destabilise, degrade and / or contribute to reduced efficiency of the RNA). In particular, the inventors recognised that there was a need for methods for discriminating between unencapsulated and / or partially encapsulated RNA on the exterior surface of the lipid nanoparticle and the RNA therein. The inventors found that the combination of an RNA binding protein or peptide and an antibody that binds thereto comprising a detectable label was particularly effective at detecting unencapsulated and / or partially encapsulated RNA on the exterior surface of the lipid nanoparticle. The findings by the inventors provide a RNA delivery vehicle, the delivery vehicle comprising: (i) a lipid nanoparticle comprising the RNA therein; and (ii) a RNA-binding protein or peptide coated on the exterior surface of the lipid nanoparticle. In one example, the RNA-binding protein or peptide coated on the exterior surface of the lipid nanoparticle encapsulates the lipid nanoparticle. For example, the RNA- binding protein or peptide surrounds, completely or partially, the exterior of the lipid nanoparticle. For example, the RNA-binding protein or peptide completely encapsulates the lipid nanoparticle. In another example, the RNA-binding protein or peptide partially encapsulates the lipid nanoparticle. For example, the RNA-binding protein or peptide does not completely encapsulate the lipid nanoparticle. In one example, the RNA-binding protein or peptide binds directly to unencapsulated and / or partially encapsulated RNA on the exterior surface of the lipid nanoparticle. In another example, the RNA-binding protein or peptide binds directly to unencapsulated RNA on the exterior surface of the lipid nanoparticle. In yet another example, the RNA-binding protein or peptide binds directly to the partially encapsulated RNA on the exterior surface of the lipid nanoparticle. In a further example, the RNA- binding protein or peptide binds directly to unencapsulated and partially encapsulated RNA on the exterior surface of the lipid nanoparticle. In one example, the RNA-binding protein or peptide non-covalently binds to unencapsulated and / or partially encapsulated RNA on the exterior surface of the lipid nanoparticle. In another example, the RNA-binding protein or peptide non-covalently binds to unencapsulated RNA on the exterior surface of the lipid nanoparticle. In yet another example, the RNA-binding protein or peptide non-covalently binds to the partially encapsulated RNA on the exterior surface of the lipid nanoparticle. In a further example, the RNA-binding protein or peptide non-covalently binds to unencapsulated and partially encapsulated RNA on the exterior surface of the lipid nanoparticle. In one example, the RNA-binding protein or peptide binds directly to the exterior surface of the lipid nanoparticle. In another example, the RNA-binding protein or peptide binds directly to the lipid nanoparticle. In one example, the RNA-binding protein or peptide non-covalently binds to the exterior surface of the lipid nanoparticle. In another example, the RNA-binding protein or peptide non-covalently binds to the lipid nanoparticle. In one example, the RNA-binding protein or peptide binds directly to unencapsulated and / or partially encapsulated RNA on the exterior surface of the lipid nanoparticle and to the exterior surface of the lipid nanoparticle. In another example, the RNA-binding protein or peptide binds directly to unencapsulated RNA on the exterior surface of the lipid nanoparticle and to the exterior surface of the lipid nanoparticle. In yet another example, the RNA-binding protein or peptide binds directly to the partially encapsulated RNA on the exterior surface of the lipid nanoparticle and to the exterior surface of the lipid nanoparticle. In a further example, the RNA-binding protein or peptide binds directly to unencapsulated and partially encapsulated RNA on the exterior surface of the lipid nanoparticle and to the exterior surface of the lipid nanoparticle. In one example, the RNA-binding protein or peptide non-covalently binds to unencapsulated and / or partially encapsulated RNA on the exterior surface of the lipid nanoparticle and to the exterior surface of the lipid nanoparticle. In another example, the RNA-binding protein or peptide non-covalently binds to unencapsulated RNA on the exterior surface of the lipid nanoparticle and to the exterior surface of the lipid nanoparticle. In yet another example, the RNA-binding protein or peptide non-covalently binds to the partially encapsulated RNA on the exterior surface of the lipid nanoparticle and to the exterior surface of the lipid nanoparticle. In a further example, the RNA- binding protein or peptide non-covalently binds to unencapsulated and partially encapsulated RNA on the exterior surface of the lipid nanoparticle and to the exterior surface of the lipid nanoparticle. In another example, the RNA-binding protein or peptide binds to the RNA within the lipid nanoparticle. In such a situation, the RNA-binding protein or peptide will be present within the lipid nanoparticle and on the exterior surface of the lipid nanoparticle. The RNA-binding protein or peptide within the lipid nanoparticle need not be the same as the RNA-binding protein or peptide coated on the exterior surface of the lipid nanoparticle. In one example, the RNA-binding protein or peptide binds on a nucleophilic side chain, at the N-terminal end and / or at the C-terminal end of the RNA. In one example, the RNA-binding protein or peptide binds on a nucleophilic side chain of the RNA. In one example, the RNA-binding protein or peptide binds on a nucleophilic side chain, at the N-terminal end of the RNA. In one example, the RNA-binding protein or peptide binds on a nucleophilic side chain at the C-terminal end of the RNA. In one example, the RNA-binding protein or peptide binds on a nucleophilic side chain, at the N-terminal end and at the C-terminal end of the RNA. In another example, the RNA-binding protein or peptide binds at the N-terminal end and / or at the C-terminal end of the RNA. For example, at the N-terminal end of the RNA. In another example, at the C-terminal end of the RNA. In another example, at the N-terminal end and at the C-terminal end of the RNA. For example, the RNA-binding protein or peptide does not encapsulate the RNA. In one example, the RNA-binding protein or peptide is a lipidated RNA-binding protein or peptide. In one example, the RNA-binding protein or peptide is lipidated prior to coating the exterior surface of the lipid nanoparticle. In another example, the RNA-binding protein or peptide is lipidated after coating the exterior surface of the lipid nanoparticle. In one example, the RNA-binding protein or peptide is lipidated with a lipid moiety selected from the group consisting of a fatty acid, an isoprenoid and combinations thereof. In one example, the RNA-binding protein or peptide is lipidated with a fatty acid. For example, the fatty acid is a triglyceride, a phospholipid or a cholesteryl ester. In one example, the fatty acid is a triglyceride. In another example, the fatty acid is a phospholipid. In a further example, the fatty acid is a cholesteryl ester. In one example, the RNA-binding protein or peptide is lipidated with an isoprenoid. For example, the isoprenoid is isoprene. In one example, the RNA-binding protein or peptide is lipidated on a nucleophilic side chain, at the N-terminal end and / or at the C-terminal end. In one example, the RNA-binding protein or peptide is lipidated on a nucleophilic side chain. For example, on a cysteine, a serine, a threonine, a tyrosine and / or a lysine amino acid residue. In one example, the nucleophilic side chain is a cysteine residue. In another example, the nucleophilic side chain is a serine residue. In a further example, the nucleophilic side chain is a threonine residue. In one example, the nucleophilic side chain is a tyrosine residue. In another example, the nucleophilic side chain is a lysine residue. In one example, the RNA-binding protein or peptide is lipidated at the N-terminal end of the protein or peptide. It will be apparent to the skilled person that the N-terminal end of the RNA- binding protein or peptide comprises a nuclear localisation signal(s) (or sequence) and / or a nuclear export signal. In one example, the RNA-binding protein or peptide is modified to remove nuclear localisation signal(s) and / or introduce nuclear export signal(s). In one example, RNA-binding protein or peptide is modified to remove the nuclear localisation signal. In another example, the RNA-binding protein or peptide is modified to inactivate or remove nuclear localisation signal(s). For example, the RNA- binding protein or peptide does not comprise a nuclear localisation signal(s) (or sequence). The skilled person will understand that the nuclear localisation signal is one or more sequences of positively charged lysines or arginines exposed on the protein surface that tag a protein for import into the cell nuclear by nuclear transport. Methods of modifying the nuclear localisation signal will be apparent to the skilled person and / or are described herein. For example, the nuclear localisation signal is lipidated or removed or inactivated. In one example, the nuclear localisation signal at the N-terminal end of the RNA-binding protein or peptide is lipidated. In another example, the nuclear localisation signal at the N-terminal end of the RNA-binding protein or peptide is removed. In another example, the nuclear localisation signal at the N-terminal end of the RNA-binding protein or peptide is inactivated. In one example, the RNA-binding protein or peptide is modified to introduce a nuclear export signal. The skilled person will understand that the nuclear export signal is a short leucine-rich motif that targets the protein for export from the cell nuclear to the cytoplasm through the nuclear pore complex. Methods for introducing a nuclear export signal will be apparent to the skilled person and / or are described herein. In one example, the RNA-binding protein or peptide is lipidated at the C-terminal end of the protein or peptide. In one example, the RNA-binding protein or peptide is lipidated by palmitoylation, myristoylation, fatty-acylation, esterification, prenylation or combinations thereof. In one example, the RNA-binding protein or peptide is lipidated by palmitoylation. For example, N-terminal cysteine palmitoylation. In one example, the RNA-binding protein or peptide is lipidated by myristoylation. For example, N-terminal glycine myristoylation. In one example, the RNA-binding protein or peptide is lipidated by fatty- acylation. For example, lysine N-acylation. In another example, serine O-acylation. In one example, the RNA-binding protein or peptide is lipidated by esterification. For example, C-terminal cholesterol esterification. In one example, the RNA-binding protein or peptide is lipidated by prenylation. For example, the prenylation is farnesylation or geranylgeranylation. In one example, the prenylation is cysteine prenylation. In one example, the RNA-binding protein or peptide is lipidated by N-terminal cysteine palmitoylation, N-terminal glycine myristoylation, lysine N-acylation, C- terminal cholesterol esterification, cysteine prenylation, serine O-acylation or combinations thereof. In one example, the lipid moiety is linked to the RNA-binding protein or peptide by a thioether bond, an ester bond, a thioester bond and / or an amide bond. In one example, the lipid moiety is linked to the RNA-binding protein or peptide by a thioether bond. In one example, the lipid moiety is linked to the RNA-binding protein or peptide by an ester bond. In one example, the lipid moiety is linked to the RNA-binding protein or peptide by a thioester bond. In one example, the lipid moiety is linked to the RNA-binding protein or peptide by an amide bond. In one example, the RNA-binding protein or peptide is lipidated using chemical or enzymatic lipidation. For example, the RNA-binding protein or peptide is lipidated using chemical lipidation. In one example, the chemical lipidation is selected from the group consisting of chemical ligation, click chemistry, expressed protein ligation and combinations thereof. In one example, the chemical lipidation is chemical ligation. In one example, the chemical lipidation is click chemistry. In one example, the chemical lipidation is expressed protein ligation. In another example, the RNA-binding protein or peptide is lipidated using enzymatic lipidation. For example, the enzymatic lipidation is selected from the group consisting of Sortase-A mediated lipidation, transglutaminase mediated lipidation and combinations thereof. In one example, the enzymatic lipidation is Sortase-A mediated lipidation. In one example, the enzymatic lipidation is transglutaminase mediated lipidation. In one example, the enzymatic lipidation is performed in vivo or in vitro. For example, the enzymatic lipidation is performed in vivo. In another example, the enzymatic lipidation is performed in vitro. In one example, the RNA-binding protein or peptide: a) reduces toxicity of the lipid nanoparticle, b) stabilizes the RNA, c) protects the RNA from degradation, d) facilitates nucleation of the lipid nanoparticle, and / or e) inhibits induction of signalling by one or more Toll-like receptors. In one example, the RNA-binding protein or peptide reduces toxicity of the lipid nanoparticle. In one example, the RNA-binding protein or peptide stabilizes the RNA. In one example, the RNA-binding protein or peptide stabilizes the unencapsulated and / or partially encapsulated RNA. In another example, the RNA-binding protein or peptide stabilizes the RNA therein. In one example, the RNA-binding protein or peptide protects the RNA from degradation. In one example, the RNA-binding protein or peptide protects the unencapsulated and / or partially encapsulated RNA from degradation. In another example, the RNA-binding protein or peptide protects the RNA therein from degradation. In one example, the RNA-binding protein or peptide facilitates nucleation of the lipid nanoparticle. In one example, the RNA-binding protein or peptide inhibits induction of signalling by one or more Toll-like receptors. In one example, the RNA-binding protein or peptide does not inhibit induction of signalling by one or more Toll-like receptors. The skilled person will understand that there are a set of Toll-like receptors, namely endosomal Toll-like receptors comprising TLR-3, TLR-7, TLR-8 and TLR-9, that recognise and bind nucleic acids, such as RNA. Activation of these receptors leads to production of inflammatory cytokines, as well as type I interferons (interferon type I). In one example, the RNA-binding protein or peptide inhibits induction of signalling by one or more endosomal Toll-like receptors. For example, the RNA-binding protein or peptide inhibits induction of signalling by one or more Toll-like receptors selected from the group consisting of TLR-3, TLR-7, TLR-8 and TLR-9. In one example, the RNA-binding protein or peptide inhibits induction of signalling by TLR-3. In another example, the RNA-binding protein or peptide inhibits induction of signalling by TLR-7. In yet another example, the RNA-binding protein or peptide inhibits induction of signalling by TLR-9. In a further example, the RNA-binding protein or peptide inhibits induction of signalling by TLR-8. In one example, the RNA-binding protein or peptide is two RNA-binding proteins or peptides (i.e., a first and a second RNA-binding protein or peptide) linked by a linker. For example, the first and second RNA-binding proteins or peptides are covalently linked by an amide bond. The present disclosure encompasses other forms of covalent and non- covalent linkages. For example, the RNA-binding proteins or peptides can be linked by a chemical linker. In one example the first and the second RNA-binding proteins or peptides are the same. In another example the first and the second RNA-binding proteins or peptides are different. In one example, the linker is a flexible linker, e.g., a flexible peptide linker. For example, the first RNA-binding protein or peptide is linked to the second RNA-binding protein via a flexible linker. In one example, the linker is a peptide linker. For example, the first RNA-binding protein or peptide is linked to the second RNA-binding protein or peptide via a linker wherein the linker is a peptide linker comprising between 2 and 31 amino acids in length. In one example, the linker comprises the sequence (Gly4Ser)n, wherein n is between 1 and 6. For example, the linker comprises the sequence SGGGGS (GS6) or the sequence SGGGGSGGGGSGGGGSGGGGSGGGGSGGGGS (GS31). In another example, the linker comprises the sequence (Ala)n, wherein n is between 2 and 31. In one example, the linker is a rigid linker. For example, the rigid linker comprises the sequence (EAAAK)n, where n is between 1 and 3. In one example, the rigid linker comprises the (EAAAK)n, where n is between 1 and 10 or between about 1 and 100. For example, n is at least 1, or at least 2, or at least 3, or at least 4, or at least 5, or at least 6, or at least 7, or at least 8, or at least 9, or at least 10. In one example, n is less than 100. For example, n is less than 90, or less than about 80, or less than about 60, or less than about 50, or less than about 40, or less than about 30, or less than about 20, or less than about 10. In one example, the RNA-binding protein or peptide is a viral or non-viral RNA- binding protein or peptide. In one example, the RNA-binding protein or peptide is a viral RNA-binding protein. For example, the viral RNA-binding protein or peptide is from a class III, class IV, class V and / or class VI virus. In one example, the viral RNA-binding protein or peptide is from a class III virus. In another example, the viral RNA-binding protein or peptide is from a class IV virus. In a further example, the viral RNA-binding protein or peptide is from a class V virus. In one example, the RNA-binding protein or peptide is from a class VI virus. In one example, the viral RNA-binding protein or peptide is from a respiratory virus selected from the group consisting of an influenza virus, a respiratory syncytial virus, a parainfluenza virus, a metapneumovirus, a rhinovirus, a coronavirus, an adenovirus and a bocavirus. In one example, the viral RNA-binding protein or peptide is from an influenza virus. For example, the influenza virus is influenza A. In another example, the influenza virus is influenza B. In one example, the viral RNA-binding protein or peptide is from a respiratory syncytial virus. In one example, the viral RNA-binding protein or peptide is from a parainfluenza virus. In one example, the viral RNA-binding protein or peptide is from a metapneumovirus. In one example, the viral RNA-binding protein or peptide is from a rhinovirus. In one example, the viral RNA-binding protein or peptide is from a coronavirus. For example, the coronavirus is severe acute respiratory disease 2 (SARS-CoV 2). In one example, the viral RNA-binding protein or peptide is from an adenovirus. In one example, the viral RNA-binding protein or peptide is from a bocavirus. In one example, the viral RNA-binding protein or peptide is a nucleoprotein, a non-structural protein, a matrix protein and / or a nucleocapsid protein. For example, the viral RNA-binding protein or peptide is a nucleoprotein. In another example, the viral RNA-binding protein or peptide is a matrix protein. In a further example, the viral RNA- binding protein or peptide is a nucleocapsid protein. In another example, the viral RNA- binding protein or peptide is a non-structural protein. In one example, the viral RNA-binding protein or peptide comprises a sequence set forth in any one of SEQ ID NOs 9 to 11. In one example, the viral RNA-binding protein or peptide is a non-structural (NS) protein from an influenza B virus. For example, the viral RNA-binding protein or peptide is an influenza B NS1 RNA binding domain. In one example, the influenza B NS1 RNA binding domain is a full length binding domain. In another example, the influenza B NS1 RNA binding domain is a truncated binding domain. In a further example, the influenza B NS1 RNA binding domain is a modified binding domain. In one example, the influenza B NS1 RNA binding domain is set forth in SEQ ID NO: 9. In another example, the influenza B NS1 RNA binding domain is set forth in SEQ ID NO: 10. In a further example, the influenza B NS1 RNA binding domain is set forth in SEQ ID NO: 11. In one example, the influenza B NS1 RNA binding domain is a modified binding domain comprising a first influenza B NS1 RNA binding domain set forth in SEQ ID NO: 11 and a second influenza B NS1 RNA binding domain set forth in SEQ ID NO: 10, wherein the first and second RNA binding domains are linked by a suitable linker. For example, the 3’ end of the first influenza B NS1 RNA binding domain is linked to the 5’ end of the second influenza B NS1 RNA binding domain. In one example, the viral RNA-binding protein or peptide is a nucleoprotein, wherein the RNA-binding protein or peptide encapsulates the RNA, stabilizes the RNA and inhibits induction of signalling by one or more endosomal Toll-like receptors (e.g., TLR-3, TLR-7, TLR-8 and / or TLR-9). In one example, the viral RNA-binding protein or peptide is a nucleocapsid, wherein the RNA-binding protein or peptide encapsulates the RNA, stabilizes the RNA and inhibits induction of signalling by one or more endosomal Toll-like receptors (e.g., TLR-3, TLR-7, TLR-8 and / or TLR-9). In one example, the viral RNA-binding protein or peptide is a matrix protein, wherein the RNA-binding protein or peptide binds to the RNA, stabilizes the RNA, but does not inhibit induction of signalling by one or more endosomal Toll-like receptors (e.g., TLR-3, TLR-7, TLR-8 and / or TLR-9). In one example, the RNA-binding protein or peptide is a non-viral RNA-binding protein or peptide. For example, the RNA-binding protein or peptide is a non-viral protein or peptide derived from cellular proteins. In one example, the RNA-binding protein or peptide is derived from cellular proteins associated with cell growth, cell signalling and / or anti-viral pathways. In one example, the cellular protein is selected from the group consisting of a TAR RNA binding protein (TRBP), a protein kinase R (PKR) RNA binding protein, a Toll-like Receptor 3 (TLR-3) binding protein, a TLR-7 binding protein and combinations thereof. In one example, the cellular protein comprises a sequence set forth in any one of SEQ ID NOs: 1 to 8. In one example, the cellular protein is a TAR RNA binding protein (TRBP). For example, the cellular protein is TRBP RNA binding domain 2. In one example, the TRBP RNA binding domain 2 is full length. For example, the full length TRBP RNA binding domain 2 is set forth in SEQ ID NO: 1. In another example, the TRBP RNA binding domain 2 is a truncated binding domain. For example, the truncated TRBP RNA binding domain 2 is set forth in SEQ ID NO: 2. In one example, the cellular protein is a protein kinase R (PKR) RNA-binding protein. For example, the cellular protein is PKR RNA-binding motif 2. In one example, the PKR RNA-binding motif 2 is a full length binding motif. For example, the full length PKR RNA-binding motif 2 is set forth in SEQ ID NO: 3. In another example, the PKR RNA-binding motif 2 is a truncated binding motif. For example, the truncated PKR RNA-binding motif 2 is set forth in SEQ ID NO: 4. In another example, the truncated PKR RNA-binding motif 2 is set forth in SEQ ID NO: 5. In one example, the cellular protein is a TLR-3 dsRNA-binding domain 1. For example, the cellular protein is a TLR-3 dsRNA-binding domain 1 (leucine rich repeats 1-3). In another example, the cellular protein is a TLR-3 dsRNA-binding domain 1 (leucine rich repeats 17-18). In one example, the TLR-3 dsRNA-binding domain 1 is set forth in SEQ ID NO: 6. In a further example, the TLR-3 dsRNA-binding domain 1 is set forth in SEQ ID NO: 7. In one example, the cellular protein is a TLR-7 RNA-binding site. For example, the cellular protein is a TLR-7 RNA-binding site (leucine rich repeats 14-15). In one example, the TLR-7 RNA-binding site is set forth in SEQ ID NO: 8. In one example, the lipid nanoparticle additionally comprises a PEG-lipid, a structural lipid and / or a neutral lipid. For example, the lipid nanoparticle additionally comprises a PEG-lipid, a structural lipid and a neutral lipid. In another example, the lipid nanoparticle additionally comprises a PEG-lipid, a structural lipid or a neutral lipid. In one example, the lipid nanoparticle additionally comprises a PEG-lipid. For example, the PEG-lipid is selected from the group consisting of PEG-c-DMG, PEG- DMG, PEG-DLPE, PEG-DMPE, PEG-DPPC, a PEG-DSPE lipid and combinations thereof. In one example, the lipid nanoparticle additionally comprises a structural lipid. For example, the structural lipid is selected from the group consisting of cholesterol, campesterol and combinations thereof. In one example, the lipid nanoparticle additionally comprises a neutral lipid. For example, the neutral lipid is selected from the group consisting of DSPC, DOPE, DLPC, DMPC, DOPC, DPPC and combinations thereof. In one example, the lipid nanoparticle does not comprise a cationic lipid. For example, the cationic lipid is 1,2-Dioleoyl-3-trimethylammonium propane (DOTAP). In one example, the RNA is selected from the group consisting of messenger RNA (mRNA), small-interfering RNA (siRNA), microRNA (miRNA) and antisense RNA. In one example, the RNA is mRNA. For example, the mRNA is self-amplifying mRNA (sa-mRNA) or conventional mRNA (cRNA). In one example, the mRNA is sa- mRNA. In another example, the mRNA is cRNA. In one example, the RNA is siRNA. In one example, the RNA is miRNA. In one example, the RNA is antisense RNA. The present disclosure also provides an immunogenic composition comprising the RNA delivery vehicle of the present disclosure. For example, the composition of the present disclosure, when administered, is capable of inducing an immune response in the subject. For example, administration of the composition induces a humoral and / or a cell- mediated immune response. In one example, the composition induces a humoral immune response in the subject. For example, the humoral immune response is an antibody- mediated immune response. In another example, the composition induces a cell-mediated immune response. For example, the cell-mediated immune response includes activation of antigen-specific cytotoxic T cells. The present disclosure also provides a pharmaceutical composition comprising the RNA delivery vehicle of the present disclosure, the immunogenic composition of the present disclosure and a pharmaceutically acceptable carrier. Pharmaceutically acceptable carriers suitable for use in the present disclosure will be apparent to the skilled person and / or are described herein. The present disclosure also provides the immunogenic composition or the pharmaceutical composition of the disclosure for use in therapy. For example, the immunogenic composition or the pharmaceutical composition of the disclosure is suitable for use as a vaccine. In one example, the immunogenic composition or the pharmaceutical composition of the disclosure is supplied in a vial. In another example, the immunogenic composition or the pharmaceutical composition of the disclosure is supplied in a syringe. The present disclosure also provides a method of detecting unencapsulated and / or partially encapsulated RNA on the exterior surface of a lipid nanoparticle, the method comprising: (i) contacting a sample comprising a lipid nanoparticle to a detection protein comprising an antibody variable region which binds to unencapsulated and / or partially encapsulated RNA on the exterior surface of the lipid nanoparticle to thereby form a complex and wherein the detection protein comprises a detectable label; and (ii) detecting the detectable label, wherein presence of the detectable label is indicative of the presence of the unencapsulated and / or partially encapsulated RNA on the exterior surface of the lipid nanoparticle. The present disclosure further provides a method of detecting unencapsulated and / or partially encapsulated RNA on the exterior surface of a lipid nanoparticle, the method comprising: (i) contacting a sample comprising a lipid nanoparticle to a RNA binding protein or peptide which binds to unencapsulated and / or partially encapsulated RNA on the exterior surface of the lipid nanoparticle to thereby form a complex; (ii) contacting the complex with a detection protein comprising an antibody variable region, wherein the detection protein binds to the RNA binding protein or peptide and wherein the detection protein comprises a detectable label; and (iii) detecting the detectable label, wherein presence of the detectable label is indicative of the presence of unencapsulated and / or partially encapsulated RNA on the exterior surface of the lipid nanoparticle in the sample. In one example, the method further comprises immobilising the RNA binding protein or peptide which binds to unencapsulated and / or partially encapsulated RNA onto a solid surface. In one example, the method further comprises washing the solid surface to remove unbound lipid nanoparticle. For example, after contacting the sample to the RNA binding protein or peptide which binds to unencapsulated and / or partially encapsulated RNA immobilized on the solid surface, the solid surface is washed to remove unbound lipid nanoparticle. In one example, the method further comprises washing the solid surface to remove unbound lipid nanoparticle. For example, after contacting the complex with a detection protein comprising an antibody variable region, the solid surface is washed to remove unbound lipid nanoparticle. In one example, the RNA binding protein or peptide is a nucleoprotein. For example, the nucleoprotein is a recombinant nucleoprotein. In another example, the RNA-binding protein or peptide is a matrix protein. In a further example, the RNA- binding protein or peptide is a nucleocapsid protein. In another example, the RNA- binding protein or peptide is a non-structural protein. In one example, the detection protein is an antibody. For example, the antibody is an anti-RNA binding protein or peptide antibody. In one example, the detection protein is a monoclonal antibody. In another example, the detection protein is a polyclonal antibody. In one example, the detectable label is selected from the group consisting of a magnetic label, a radiolabel, an enzyme, a fluorescent label, a luminescent label, a bioluminescent label, a prosthetic group and a contrast agent. In one example, the detectable label is a magnetic label. For example, the magnetic label is a magnetic bead. In one example, the detectable label is a radiolabel. In one example, the detectable label is an enzyme. In one example, the detectable label is a fluorescent label. In one example, the detectable label is a luminescent label. In one example, the detectable label is a bioluminescent label. In one example, the detectable label is a prosthetic group. In one example, the detectable label is a contrast agent. In one example, the method comprises determining the amount of the anti- unencapsulated and / or partially encapsulated RNA in the sample. For example, the amount of the unencapsulated and / or partially encapsulated RNA is determined directly by determining the amount of bound unencapsulated and / or partially encapsulated RNA in the sample. In another example, the amount of the unencapsulated and / or partially encapsulated RNA is determined indirectly by determining the amount of unbound lipid nanoparticle in the sample. In one example, the method comprises performing an enzyme-linked immunosorbent assay (ELISA). In a further example, the method comprises performing a fluorescence linked immunosorbent assay (FLISA). In another example, the method comprises performing a lateral flow immunoassay. In one example, the method comprises performing chromatography. For example, the chromatography is affinity chromatography. In one example, the disclosure provides a method of determining the amount of encapsulated RNA, the method comprising determining the amount of RNA in a sample, determining the amount of unencapsulated and / or partially encapsulated RNA in the sample using a method described herein and subtracting the amount of unencapsulated and / or partially encapsulated RNA in the sample from the amount of RNA in the sample thereby giving the amount of encapsulated RNA in the sample. KEY TO SEQUENCE LISTING SEQ ID NO: 1 Amino acid sequence of full length TAR RNA-binding protein domain 2 SEQ ID NO: 2 Amino acid sequence of truncated TAR RNA-binding protein domain 2 SEQ ID NO: 3 Amino acid sequence of protein kinase R RNA-binding motif 2 SEQ ID NO: 4 Amino acid sequence of truncated protein kinase R RNA-binding motif 2 (#1) SEQ ID NO: 5 Amino acid sequence of truncated protein kinase R RNA-binding motif 2 (#2) SEQ ID NO: 6 Amino acid sequence of Toll-like receptor 3 dsRNA-binding domain 1 (leucine-rich repeats 1-3) SEQ ID NO: 7 Amino acid sequence of Toll-like receptor 3 dsRNA-binding domain 1 (leucine-rich repeats 17-18) SEQ ID NO: 8 Amino acid sequence of Toll-like receptor 7 RNA-binding site (leucine-rich repeats 14-15) SEQ ID NO: 9 Amino acid sequence of influenza B NS1 RNA-binding domain SEQ ID NO: 10 Amino acid sequence of truncated influenza B NS1 RNA-binding domain SEQ ID NO: 11 Amino acid sequence of modified influenza B NS1 RNA-binding domain BRIEF DESCRIPTON OF THE DRAWINGS Figure 1 is a graphical representation of a rabbit reticulocyte lysate assay showing the amount of RNA as measured by the amount of luciferase produced as assessed by measuring luminescence in relative light units (RLU) in nanoluciferase RNA (nLuc RNA) alone or in combination with influenza virus RNA-free nucleoprotein (NP:nLuc RNA). Figure 2 is a graphical representation of the amount of RNA in (A) NP:nLuc RNA and (B) nLuc RNA alone samples following treatment with or without thermolabile proteinase K (PK) and / or RNase. Figure 3 is a series of graphical representations showing the stability of nLuc RNA in samples of nLuc RNA alone and NP:nLuc RNA at (A) 4oC (B) 24oC and (C) 37oC following incubation for up to 96 hours. Figure 4 is a series of graphical representations showing the level of (A-B) TLR3 and (C-D) TLR8 induction in samples of nLuc RNA alone and NP:nLuc RNA at 2 hours and 4 hours post incubation. Figure 5 is a series of graphical representations showing (A) protection of RNA degradation by SARS-CoV-2 nucleocapsid as measured by the amount of luciferase produced as assessed by measuring luminescence in RLU in nanoluciferase RNA (RNA) alone or in combination with COVID RNA-free nucleocapsid (RNA+NP(SCov2)). (B) Dye exclusion assay of nLuc RNA with and without COVID RNA-free nucleocapsid. Figure 6 is a series of graphical representations showing mRNA immunoprecipitation (A) without recombinant NP and (B) with recombinant NP. Figure 7 is a series of graphical representations showing immunoprecipitation of mRNA on the exterior and interior of LNPs (A) without recombinant NP and (B) with recombinant NP. Legend: (mRNA)-LNP = encapsulated mRNA; mRNA-LNP = surface linked mRNA. Figure 8 is a series of graphical representations showing immunoprecipitation of NP bound mRNA on the exterior and interior of LNPs (A) without recombinant NP and (B) with recombinant NP. Legend: (NP+mRNA)-LNP = encapsulated NP bound mRNA; NP+mRNA-LNP = surface linked NP bound mRNA. Figure 9 is a series of graphical representations showing the effect of decreasing the amount of ionizable lipids on immunoprecipitation (A) without recombinant NP and (B) with recombinant NP. Figure 10 is a series of graphical representations showing the effect of NP bound mRNA on immunoprecipitation (A) without recombinant NP and (B) with recombinant NP. Figure 11 is a series of graphical representations showing LNPs that contain an ionizable lipid do not bind to the magnet used in the immunoprecipitation assay (A) mRNA-LNP and (B) NP+mRNA-LNP. DETAILED DESCRIPTION General Throughout this specification, unless specifically stated otherwise or the context requires otherwise, reference to a single step, composition of matter, group of steps or group of compositions of matter shall be taken to encompass one and a plurality (i.e. one or more) of those steps, compositions of matter, groups of steps or groups of compositions of matter. Those skilled in the art will appreciate that the present disclosure is susceptible to variations and modifications other than those specifically described. It is to be understood that the disclosure includes all such variations and modifications. The disclosure also includes all of the steps, features, compositions and compounds referred to or indicated in this specification, individually or collectively, and any and all combinations or any two or more of said steps or features. The present disclosure is not to be limited in scope by the specific examples described herein, which are intended for the purpose of exemplification only. Functionally-equivalent products, compositions and methods are clearly within the scope of the present disclosure. Any example of the present disclosure herein shall be taken to apply mutatis mutandis to any other example of the disclosure unless specifically stated otherwise. Unless specifically defined otherwise, all technical and scientific terms used herein shall be taken to have the same meaning as commonly understood by one of ordinary skill in the art (for example, in cell culture, molecular genetics, immunology, immunohistochemistry, protein chemistry, and biochemistry). Unless otherwise indicated, the recombinant protein, cell culture, and immunological techniques utilized in the present disclosure are standard procedures, well known to those skilled in the art. Such techniques are described and explained throughout the literature in sources such as, J. Perbal, A Practical Guide to Molecular Cloning, John Wiley and Sons (1984), J. Sambrook et al. Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press (1989), T.A. Brown (editor), Essential Molecular Biology: A Practical Approach, Volumes 1 and 2, IRL Press (1991), D.M. Glover and B.D. Hames (editors), DNA Cloning: A Practical Approach, Volumes 1-4, IRL Press (1995 and 1996), and F.M. Ausubel et al. (editors), Current Protocols in Molecular Biology, Greene Pub. Associates and Wiley-Interscience (1988, including all updates until present), Ed Harlow and David Lane (editors) Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory, (1988), and J.E. Coligan et al. (editors) Current Protocols in Immunology, John Wiley & Sons (including all updates until present). The term “and / or”, e.g., “X and / or Y” shall be understood to mean either “X and Y” or “X or Y” and shall be taken to provide explicit support for both meanings or for either meaning. Throughout this specification the word “comprise”, or variations such as “comprises” or “comprising”, will be understood to imply the inclusion of a stated element, integer or step, or group of elements, integers or steps, but not the exclusion of any other element, integer or step, or group of elements, integers or steps. As used herein the term "derived from" shall be taken to indicate that a specified integer may be obtained from a particular source albeit not necessarily directly from that source. Selected Definitions The term “RNA delivery vehicle” as used herein refers to delivery systems for RNA which allow RNA to be transported into host cells. As used herein, the term “lipid nanoparticle” or “LNP” shall be understood to refer to lipid-based particles having at least one dimension on the order of nanometers (e.g., 1-1,000 nm) and which comprises a compound of any formulae described herein. In some examples, LNPs are formulated in a composition for delivery of an oligonucleotide to a desired target such as a cell, tissue, organ, tumor, and the like. For example, the lipid nanoparticle or LNP may be selected from, but not limited to, liposomes or vesicles, where an aqueous volume is encapsulated by amphipathic lipid bilayers (e.g., single; unilamellar or multiple; multilamellar), micelle-like lipid nanoparticles having a non-aqueous core and solid lipid nanoparticles, wherein solid lipid nanoparticles lack lipid bilayers. The term “exterior surface” as used herein refers to the outer, encapsulating, wall of the LNP. The term “unencapsulated RNA” as used herein refers to RNA that is not encapsulated during the preparation of the lipid nanoparticle and wherein the RNA remains accessible on the exterior surface of the lipid nanoparticle. It will be apparent from the foregoing that the RNA need not be completely unencapsulated, rather it can also be “partially encapsulated” or “incompletely encapsulated”, for example, by at least about 10% or 20% or 30% or 40% or 50% or 60% or 70% or 80% or 90% or 95%. Methods for determining the level of unencapsulated RNA are known in the art and / or are described herein. The term “partially encapsulated RNA” or “incompletely encapsulated” as used herein refers to RNA that is not completely encapsulated within the lipid nanoparticle and wherein at least a portion of the RNA remains accessible or exposed on the exterior surface of the lipid nanoparticle. In some examples, the level of unencapsulated RNA on the exterior surface of the lipid nanoparticle is at least 50%, for example about 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%. In one example, the level of unencapsulated RNA is at least 80%. In one example, the level of unencapsulated RNA is at least 90%. In one example, the level of unencapsulated RNA is at least 95%. For example, at least 95% of the RNA is unencapsulated RNA. In some examples, the level of partially encapsulated RNA on the exterior surface of the lipid nanoparticle may be at least 50%, for example about 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%. In one example, the level of partially encapsulated is at least 80%. In one example, the level of partially encapsulated is at least 90%. In one example, the level of partially encapsulated is at least 95%. For example, at least 95% of the RNA is partially encapsulated. In another example, at least 95% of the RNA is incompletely encapsulated. The term “coating” as used herein refers to the RNA-binding protein or peptide binding to, attaching to the exterior surface of the lipid nanoparticle. The term “lipidated” or “lipidation” as used herein refers to the process of covalently modifying a protein (i.e., a RNA-binding protein or peptide) with one or more lipids. As used herein, the term “RNA-binding protein or peptide” or “RBP’ shall be understood to refer to proteins and peptides that bind to double or single stranded RNA and participate in forming ribonucleoprotein complexes. As used herein, the term “recombinant” shall be understood to mean the product of artificial genetic recombination. As used herein, the term “self-replicating RNA” refers to a construct based on an RNA virus that has been engineered to allow expression of heterologous RNA and proteins. Self-replicating RNA (e.g., in the form of naked RNA) can amplify in host cells leading to expression of the desired gene product in the host cell. As used herein, the term “conventional RNA” or “cRNA” or “non-amplifying RNA” refers to a construct that allows expression of heterologous RNA and proteins but the RNA that cannot amplify in host cells. As used herein, the term “detect” or “detecting” refers to the identification of the presence or existence of unencapsulated and / or partially encapsulated RNA on the exterior surface of a lipid nanoparticle or RNA on the interior of a lipid nanoparticle. As used herein, the term “contact” or “contacting” is used to refer to a direct or indirect interaction or association between RNA and a RNA binding protein or peptide. For example, a RNA binding protein or peptide either directly or indirectly binds to RNA. As used herein, the term “binds” in reference to the interaction of two or more proteins means that the interaction is dependent upon the presence of a particular structure (e.g., an antigenic determinant or epitope) on a protein. For example, a protein (e.g. an RNA binding protein or peptide) recognizes and binds to a specific protein structure rather than to proteins generally. If a protein binds to epitope "A", the presence of a molecule containing epitope “A” (or free, unlabeled “A”), in a reaction containing labeled “A” and the protein, will reduce the amount of labeled “A” bound to the protein. As used herein, the term “specifically binds” or “binds specifically” shall be taken to mean that a protein (e.g. an RNA binding protein or peptide) reacts or associates more frequently, more rapidly, with greater duration and / or with greater affinity with a particular antigen (e.g., unencapsulated and / or partially encapsulated RNA on the exterior surface of a lipid nanoparticle) than it does with alternative antigens. For example, an RNA binding protein or peptide binds to the RNA with materially greater affinity (e.g., 20 fold or 40 fold or 60 fold or 80 fold to 100 fold or 150 fold or 200 fold greater affinity) avidity, more readily, and / or with greater duration than it binds to other antigens. Generally, but not necessarily, reference to binding means specific binding, and each term shall be understood to provide explicit support for the other term. As used herein, the term “subject” shall be taken to mean any animal including humans, for example a mammal. Exemplary subjects include but are not limited to humans and non-human primates. For example, the subject is a human. RNA Delivery Vehicle The present disclosure provides a RNA delivery vehicle comprising: a lipid nanoparticle comprising the RNA therein; and a RNA-binding protein or peptide coated on the exterior surface of the lipid nanoparticle. For example, the RNA delivery vehicle of the present disclosure provides a lipid nanoparticle comprising a RNA-binding protein or peptide as an external layer. The skilled person will understand that in the process of formulating a lipid nanoparticle, not all RNA will be encapsulated in the nanoparticle, and the RNA may remain completely unencapsulated by the lipid nanoparticle or partially encapsulated within the lipid nanoparticle. These unencapsulated and / or partially encapsulated RNAs may destabilise, degrade and / or contribute to reduced efficiency of the RNA delivery vehicle. By coating the lipid nanoparticle with a RNA-binding protein or peptide to protect the unencapsulated and / or partially encapsulated RNA there is provided an improved lipid nanoparticle for delivery of RNA. RNA-binding protein or peptides may non-covalently attach to the exterior surface of the lipid nanoparticle, and further facilitate nucleation of the lipid nanoparticle. RNA-binding proteins or peptides The present disclosure provides a RNA-binding protein or peptide coated on the exterior surface of the lipid nanoparticle. For example, RNA-binding protein or peptide binds to the exterior surface of the lipid nanoparticle. The present disclosure also provides a RNA-binding protein or peptide that binds to the RNA within the lipid nanoparticle. The present disclosure further provides a RNA-binding protein or peptide that binds to the unencapsulated and / or partially encapsulated RNA on the exterior of the lipid nanoparticle. RNA-binding proteins or peptides regulate numerous aspects of co- and post- transcription gene expression including, for example, RNA splicing, RNA editing, polyadenylation, export, mRNA stabilization, mRNA localization and translation. RNA- binding proteins or peptides bind to double or single-stranded RNA and participate in the formation of ribonucleoprotein complexes. The skilled person will understand that RNA-binding proteins or peptides can be viral or non-viral proteins or peptides. Non-viral RNA-binding proteins or peptides In one example, the RNA-binding protein is a non-viral protein or peptide derived from cellular proteins. For example, RNA-binding proteins or peptides are derived from cellular proteins associated with cell growth, cell signalling and / or anti-viral pathways. Non-viral RNA-binding proteins or peptides contain numerous structural motifs or RNA-binding domains that facilitate RNA binding including, for example, a RNA recognition motif (RRM), a K-homology (KH) domain (type I and type II), a RGG (Arg- Gly-Gly) box, a Sm domain; DEAD / DEAH box, a CCCH-type zinc finger (ZnF), a double stranded RNA-binding motif (dsRBD), a cold-shock domain; Pumilio / FBF (PUF or Pum-HD) domain, and a Piwi / Argonaute / Zwille (PAZ) domain. In one example, the RNA-binding protein or peptide comprises a RNA-binding domain selected from the group consisting of a RNA recognition motif, a K-homology domain (type I or type II) and a CCCH-type zinc finger. In one example, the RNA-binding protein or peptide comprises a RNA recognition motif. For example, the RNA-binding protein or peptide comprising a RNA recognition motif is selected from the group consisting of A2BP1, ACF, BOLL, BRUNOL4, BRUNOL5, BRUNOL6, CCBL2, CGI-96, CIRBP, CNOT4, CPEB2, CPEB3, CPEB4, CPSF7, CSTF2, CSTF2T, CUGBP1, CUGBP2, D10S102, DAZ1, DAZ2, DAZ3, DAZ4, DAZAP1, DAZL, DNAJC17, DND1, EIF3S4, EIF3S9, EIF4B, EIF4H, ELAVL1, ELAVL2, ELAVL3, ELAVL4, ENOX1, ENOX2, EWSR1, FUS, FUSIP1, G3BP, G3BP1, G3BP2, GRSF1, HNRNPL, HNRPA0, HNRPA1, HNRPA2B1, HNRPA3, HNRPAB, HNRPC, HNRPCL1, HNRPD, HNRPDL, HNRPF, HNRPH1, HNRPH2, HNRPH3, HNRPL, HNRPLL, HNRPM, HNRPR, HRNBP1, HSU53209, HTATSF1, IGF2BP1, IGF2BP2, IGF2BP3, LARP7, MKI67IP, MSI1, MSI2, MSSP-2, MTHFSD, MYEF2, NCBP2, NCL, NOL8, NONO, P14, PABPC1, PABPC1L, PABPC3, PABPC4, PABPC5, PABPN1, PKR, POLDIP3, PPARGC1, PPARGC1A, PPARGC1B, PPIE, PPIL4, PPRC1, PSPC1, PTBP1, PTBP2, PUF60, RALY, RALYL, RAVER1, RAVER2, RBM10, RBM11, RBM12, RBM12B, RBM14, RBM15, RBM15B, RBM16, RBM17, RBM18, RBM19, RBM22, RBM23, RBM24, RBM25, RBM26, RBM27, RBM28, RBM3, RBM32B, RBM33, RBM34, RBM35A, RBM35B, RBM38, RBM39, RBM4, RBM41, RBM42, RBM44, RBM45, RBM46, RBM47, RBM4B, RBM5, RBM7, RBM8A, RBM9, RBMS1, RBMS2, RBMS3, RBMX, RBMX2, RBMXL2, RBMY1A1, RBMY1B, RBMY1E, RBMY1F, RBMY2FP, RBPMS, RBPMS2, RDBP, RNPC3, RNPC4, RNPS1, ROD1, SAFB, SAFB2, SART3, SERBP1, SETD1A, SF3B14, SF3B4, SFPQ, SFRS1, SFRS10, SFRS11, SFRS12, SFRS15, SFRS2, SFRS2B, SFRS3, SFRS4, SFRS5, SFRS6, SFRS7, SFRS9, SLIRP, SLTM, SNRP70, SNRPA, SNRPB2, SPEN, SR140, SRRP35, SSB, SYNCRIP, TAF15, TRBP, THOC4, TIA1, TIAL1, TNRC4, TNRC6C, TRA2A, TRSPAP1, TUT1, U1SNRNPBP, U2AF1, U2AF2, UHMK1, ZCRB1, ZNF638, ZRSR1 and ZRSR2. In one example, the RNA-binding protein or peptide comprises a K-homology domain. For example, the K-homology domain is a type I domain. In another example, the K-homology domain is a type II domain. In one example, the RNA-binding protein or peptide comprising a K-homology domain is selected from the group consisting of AKAP1, ANKHD1, ANKRD17, ASCC1, BICC1, DDX43, DDX53, DPPA5, FMR1, FUBP1, FUBP3, FXR1, FXR2, GLD1, HDLBP, HNRPK, IGF2BP1, IGF2BP2, IGF2BP3, KHDRBS1, KHDRBS2, KHDRBS3, KHSRP, KRR1, MEX3A, MEX3B, MEX3C, MEX3D, NOVA1, NOVA2, PCBP1, PCBP2, PCBP3, PCBP4, PNO1, PNPT1, QKI, SF1, and TDRKH. In one example, the RNA-binding domain comprises a CCCH-type zinc finger domain. Exemplary non-viral RNA-binding protein or peptide will be apparent to the skilled person and include, for example, TAR RNA-binding protein (TRBP), protein kinase R (PKR), Toll-like receptor 3 (TLR-3) and Toll-like receptor 7 (TLR). Viral RNA-binding proteins In one example, the RNA-binding protein or peptide is a viral RNA-binding protein or peptide. For example, the RNA-binding protein is a nucleoprotein, a matrix protein, a nucleocapsid protein and / or a non-structural from a RNA virus. It will be apparent to the skilled person that viruses are classified according to the Baltimore classification system, as shown in Table 1, which is largely based on the transcription of the viral genome. Table 1: Baltimore classification of viruses In one example, the RNA-binding protein or peptide is from a RNA virus. For example, the RNA-binding protein or peptide is from a class III, a class IV, a class V and / or a class VI virus. In one example, the RNA virus is a class III virus (i.e., a double-stranded RNA virus). Class III viruses include, for example, all viruses of the phylum Duplornaviricota and all viruses of class Duplopiviricetes (of phylum Pisuviricota). Exemplary class III viruses include, but are not limited to, Reoviruses (e.g., Orthoreo virus, a Rotavirus, an Orbivirus, or a Coltivirus). In one example, the RNA virus is a class IV virus (i.e., positive sense single- stranded RNA virus). Class IV viruses include, for example, viruses of the phylum Lenarviricota, Pisuviricota (except of the class Duplopidiviricetes) and Kitrinoviricota. Exemplary class IV viruses include, but are not limited to, Togaviruses (e.g., Rubivirus, an Alphavirus, or an Arterivirus), Flaviviruses (e.g., Tick-borne encephalitis (TBE) virus, Dengue (types 1, 2, 3 or 4) virus, Yellow Fever virus, Japanese encephalitis virus, Kyasanur Forest Virus, West Nile encephalitis virus, St. Louis encephalitis virus, Russian spring-summer encephalitis virus, Powassan encephalitis virus), Picornaviruses (e.g., Enteroviruses, Rhinoviruses, Heparnavirus, Parechovirus, Cardioviruses and Aphthoviruses), Enteroviruseses (e.g., Poliovirus types 1, 2 or 3, Coxsackie A virus types 1 to 22 and 24, Coxsackie B virus types 1 to 6, Echovirus (ECHO) virus types 1 to 9, 11 to 27 and 29 to 34 and Enterovirus 68 to 71), Pestiviruses (e.g., Bovine viral diarrhea (BVDV), Classical swine fever (CSFV) or Border disease (BDV)), Caliciviridae (e.g., Norwalk virus, and Norwalk-like Viruses (e.g., Hawaii Virus and Snow Mountain Virus), Coronaviruses (e.g., severe acute respiratory syndrome (SARS) coronavirus (SARS- CoV), SARS coronavirus 2 (SARS-CoV-2), Middle East respiratory syndrome (MERS) coronavirus (MERS-CoV), Avian infectious bronchitis (IBV), Mouse hepatitis virus (MHV), and Porcine transmissible gastroenteritis virus (TGEV)) and Hepatitis E virus (HEV). In one example, the RNA virus is a class V virus (i.e., negative sense single- stranded RNA virus). Class V viruses include, for example, viruses of the phylum Negarnaviricota. Exemplary class V viruses include, but are not limited to, Orthomyxoviruses (e.g., Influenza A, B and C), Paramyxoviridae viruses (Pneumoviruses (e.g., Respiratory syncytial virus (RSV), Bovine respiratory syncytial virus, Pneumonia virus of mice, and Turkey rhinotracheitis virus), Paramyxovirus types 1-4 (PIV), Mumps, Sendai viruses, Simian virus 5), Nipahvirus, Henipavirus, Newcastle disease virus, Morbilliviruses (e.g., Measles), Bunyaviruses (e.g., California encephalitis virus), Phlebovirus (e.g., Rift Valley Fever virus), Nairovirus (e.g., Crimean-Congo hemorrhagic fever virus), Rhabdoviruses (e.g., Lyssavirus (Rabies virus) and Vesiculovirus (VSV)), Delta hepatitis virus (HDV) and Arenaviruses. In one example, the class V RNA virus is an influenza virus. For example, an influenza A virus. In another example, an influenza B virus. In one example, the RNA virus is a class VI virus (i.e., single-stranded RNA viruses with a DNA intermediate in their life cycle). Class VI viruses include, for example, viruses of the class Revtraviricetes (of phylum Aterviricota, excluding Caulimoviridae). Exemplary class VI viruses include, but are not limited to, Heparnaviruses (e.g., Hepatitis A virus (HAV)), Hepadnaviruses (e.g., Hepatitis B virus, Hepatitis C virus) and Retroviruses (e.g., Oncovirus, a Lentivirus or a Spumavirus). Linkers In one example, the RNA-binding protein or peptide comprises a first RNA- binding protein or peptide and a second RNA-binding protein or peptide linked via a linker. For example, the linker is a linker peptide. In one example, the linker is a flexible linker. A “flexible” linker is an amino acid sequence which does not have a fixed structure (secondary or tertiary structure) in solution. Such a flexible linker is therefore free to adopt a variety of conformations. Flexible linkers suitable for use in the present disclosure are known in the art. An example of a flexible linker for use in the present invention is the linker sequence SGGGGS / GGGGS / GGGGS or (Gly4Ser)3. Another example of a flexible linker is an alanine linker (e.g., Alan). The linker may comprise any amino acid sequence that does not substantially hinder interaction of the RNA-binding protein or peptide with the RNA. Preferred amino acid residues for flexible linker sequences include, but are not limited to, glycine, alanine, serine, threonine proline, lysine, arginine, glutamine and glutamic acid. The linker sequences between the RNA-binding protein or peptide preferably comprise five or more amino acid residues. The flexible linker sequences according to the present disclosure consist of 5 or more residues, preferably, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19 or 20 or more residues. In a highly preferred embodiment of the invention, the flexible linker sequences consist of 5, 7, 10 or 16 residues. In one example, the linker is a rigid linker. A “rigid linker” (including a “semi- rigid linker”) refers to a linker having limited flexibility. For example, the relatively rigid linker comprises the sequence (EAAAK)n, where n is between 1 and 3. The value of n can be between 1 and about 10 or between about 1 and 100. For example, n is at least 1, or at least 2, or at least 3, or at least 4, or at least 5, or at least 6, or at least 7, or at least 8, or at least 9, or at least 10. In one example, n is less than 100. For example, n is less than 90, or less than about 80, or less than about 70, or less than about 60, or less than about 50, or less than about 40, or less than about 30, or less than about 20, or less than about 10. A rigid linker need not completely lack flexibility. Lipidation of the RNA-Binding Protein The present disclosure provides a RNA delivery vehicle comprising a lipid nanoparticle and a RNA-binding protein or peptide coated on the exterior surface of the lipid nanoparticle, wherein the RNA-binding protein or peptide is a lipidated RNA- binding protein or peptide. It will be apparent to the skilled person that protein or peptide lipidation is the covalent attachment of a lipid moiety to the protein or peptide (i.e., RNA-binding protein or peptide). Lipids Lipid moieties suitable for use in the present disclosure will be apparent to the skilled person and include, for example, a fatty acid, an isoprenoid and combinations thereof. In one example, the lipid moiety is selected from the group consisting of an isoprenoid, a triglyceride, a phospholipid, a cholesteryl ester and combinations thereof. Isoprenoids Isoprenoids, also known as terpenoids or prenol lipids, are branched lipids and are a class of organic compounds composed of two or more units of hydrocarbons, with each unit consisting of five carbon atoms arranged in a specific pattern. These five-carbon units are termed isoprene and are synthesized from a common intermediate known as mevalonic acid, which is itself synthesized from acetyl-CoA. Isoprenoids can have one or more functional chemical groups attached to their carbon backbone, such as hydroxyls and carbonyls, which make up the diversity of isoprenoids. Isoprenoids can be classified as monoterpenes (C10H16) sesquiterpenes (C15H24), diterpenes (C20H32), triterpenes (C30H48), tetraterpenes (C40H64) or other polyterpenes (C5H8)n. Isoprenoids suitable for use in the present disclosure will be apparent to the skilled person and / or are described herein. In one example, the isoprenoid is a monoterpene. Exemplary monoterpenes include citronellol, citronellal, citral, geraniol, methol, pseudoionone and beta-ionone. In one example, the isoprenoid is a sesquiterpenes. Exemplary sesquiterpenes include cadalene, eudalene, cadinene and beta-selinene. In one example, the isoprenoid is a diterpene. Exemplary diterpenes include phytol and abietic acid. In one example, the isoprenoid is a triterpene. Exemplary triterpenes include squalene and beta-amyrin. In one example, the isoprenoid is a tetraterpene. Exemplary tetraterpenes include carotenoids (e.g., beta-carotene) and lycopene. Fatty acids Fatty acids are lipids that contain long-chain hydrocarbons terminated with a carboxylic acid functional group. Fatty acids may be saturated or unsaturated. In one example, the fatty acid comprises a carbon chain having from 6 to 22 carbons. Exemplary fatty acids include palmitic acid, myristic acid, oleic acid, alpha-linolenic acid and stearic acid. Fatty acids rarely occur in the free form in nature and commonly exist as three main classes of esters: triglycerides, phospholipids and cholesteryl esters. In one example, the fatty acid is a triglyceride. Triglycerides are tri-esters consisting of a glycerol bound to three fatty acid molecules via an ester bond. The three fatty acids may be the same or different. An exemplary triglyceride is tristearin. In one example, the fatty acid is a phospholipid. Phospholipids are complex lipids that comprise a hydrophilic polar head group comprising one or more phosphate groups, and a hydrophobic tail comprising two fatty acyl chains. The polar head group is joined to the hydrophobic moiety by a phosphodiester linkage via a glycerol (i.e., phosphoglycerides) or sphingosine molecule (i.e., phosphosphingo lipids). Phospholipids may be saturated or unsaturated. Exemplary phosphoglycerides include phosphatidic acid (phosphatidate), phosphatidylethanolamine (cephaline), phosphatidylcholine (lecithin), phosphatidylserine, phosphoinositides (e.g., phosphatidylinositol (PI), phosphatidylinositol phosphate (PIP), phosphatidylinositol bisphosphate (PIP2) and phosphatidylinositol trisphosphate (PIP3)), phosphatidylglycerol and cardiolipin. Exemplay phosphosphingo lipids include ceramide phosphorylcholine (sphingomyelin), ceramide phosphorylethanolamine (sphingomyelin), ceramind phosphoryllipid, galactocerebroside, glucocerebroside and lactosylceramide. In one example, the fatty acid is a cholesteryl ester. Cholesteryl esters are the esterification of cholesterol with long-chain fatty acids. Exemplary cholesteryl esters include cholesteryl oleate, cholesteryl benzoate and cholesteryl linoleate. Lipidation Exemplary lipidation includes, palmitoylation, myristoylation, fatty-acylation, esterification, prenylation, or combinations thereof. Palmitoylation In one example, the lipid moiety is attached to the RNA-binding protein or peptide by palmitoylation. In one example, the palmitoylation is cysteine palmitoylation (also known as S- palmitoylation). The skilled person will understand that cysteine palmitoylation is the addition of a 16-carbon palmitoyl group on protein cysteine residues. In one example, the palmitoyl group is added via a thioester bond. In another example, the palmitoyl group is added via an amide bond. Myristoylation In one example, the lipid moiety is attached to the RNA-binding protein or peptide by myristoylation. In one example, the myristoylation is N-glycine myristoylation. The skilled person will recognise that N-glycine myristoylation refers to the co- or post-translational attachment of a saturated 14-carbon fatty acyl group, myristoyl, to the N-terminal glycine of proteins via an amide bond. In one example, the myristoylation is lysine myristoylation. Fatty-acylation In one example, the lipid moiety is attached to the RNA-binding protein or peptide by fatty-acylation. The skilled person will recognise that fatty-acylation involves the covalent attachment of an acyl group to a protein. In one example, the fatty-acylation is lysine N-acylation. The skilled person will understand that lysine N-acylation refers to the transfer of the acetyl moiety from acetyl- CoA to the epsilon (ε)-amino group of a lysine residue on a protein. Esterification In one example, the lipid moiety is attached to the RNA-binding protein or peptide by esterification. In one example, the esterification is C-terminal sterol esterification, for example C-terminal cholesterol esterification. The skilled person will understand that C-terminal cholesterol esterification is the replacement of at least one hydroxyl (-OH) group with an alkoxy (-O-alkyl) group. Prenylation In one example, the lipid moiety is attached to the RNA-binding protein or peptide by prenylation. In one example, the prenylation is cysteine prenylation. The skilled person will understand that cysteine prenylation is the addition of multiple isoprene units to cysteine residues near the C-terminal end of the protein. In one example, the prenylation is farnesylation (i.e., the addition of three isoprene units), or the prenylation is geranylgeranylation (i.e., the addition of four isoprene units). In one example, the linkage between farnesyl or geranylgeranyl groups and cysteine residues is a thioether bond. In another example, the linkage is an ester bond. In a further example, the linkage is a thioester bond. Methods of lipidation Lipid modifications typically occur on the nucleophilic side chains of proteins or peptide (e.g., cysteine, serine and lysine), at the N-terminal end and / or at the C-terminal end of proteins or peptides. Various methods of lipidation will be apparent to the skilled person and / or are described herein. Suitable methods can include chemical or enzymatic lipidation. Chemical lipidation In one example, the lipid moiety is attached to the RNA-binding protein or peptide using chemical ligation. The lipid moiety can comprise an amine, carboxylic acid, hydrazide, or maleimide group and the lipid moiety may be chemically coupled to the RNA-binding protein or peptide via the primary amine group of a lysine or the thiol group of a cysteine. In one example, the lipid moiety comprises a maleimide group and the lipid moiety is attached to the RNA-binding protein or peptide via the formation of a thioether bond with a sulphydryl group in the RNA binding protein or peptide. In one example, the lipid moiety comprises a carboxylic acid and the carboxylic acid is activated by 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) and N- hydroxysulfosuccinimide (Sulfo-NHS). The activated acyl amino ester or sulfo-NHS ester subsequently reacts with a primary amine of a lysine residue in the RNA binding protein or peptide forming an amide bond. In one example, the lipid moiety comprises a maleimide group. For example, the lipid moiety is a phospholipid capped with a maleimide group. In one example, the lipid moiety is a 1,2-Distearoyl-sn-Glycero-3-Phosphoethanolamine–maleimide (DSPE- maleimide; DSPE-Mal). In one example, the lipid moiety is attached to the RNA-binding protein or peptide using various "click chemistry" strategies such as those disclosed in Kolb et al. (2001), WO 2003 / 101972 and Malkoch et al. (2005). In one example, the lipid moiety is attached to the RNA-binding protein or peptide using expressed protein ligation. Expressed protein ligation comprises chemoselective ligation between a protein or peptide with a C-terminal thioester and a protein or peptide with an N-terminal cysteine in aqueous solution at physiological pH. In one example, the C-terminal thioester is inserted into the RNA binding protein or peptide by genetic manipulation and the lipid moiety is fused to a peptide having an N-terminal cysteine residue. Other methods of chemical lipidation known to the skilled person may be used, such as those disclosed in Takahara & Kamiya (2020). Enzymatic lipidation In one example, the lipid moiety is attached to the RNA-binding protein or peptide using enzymatic lipidation. Enzymatic lipidation may be performed in vivo or in vitro. In some examples, the RNA-binding protein or peptide is genetically manipulated using techniques known to the skilled person to comprise a consensus sequence recognized by the lipidating enzyme. In one example, the lipid moiety is attached to the RNA-binding protein or peptide using Sortase-A mediated lipidation. Sortase A (e.g., SrtA from Staphylococcus aureus) covalently attaches secreted proteins to a bacterial cell wall peptidoglycan in the presenceof Ca2+ via a transpeptidation reaction. In this example, the RNA-binding protein orpeptide is genetically manipulated to comprise an LPXTG motif (e.g., LPETG) at the C- terminus and the lipid moiety comprises a nucleophile and an oligo-glycine motif (e.g., triglycine, tetraglycine or pentaglycine). Upon addition of the sortase, the RNA binding- protein or peptide is covalently linked to the lipid through a peptide bond. In one example, the lipid moiety is attached to the RNA-binding protein or peptide using transglutaminase mediated lipidation. Transglutaminase (e.g., Microbial transglutaminase: MTG) catalyzes a reaction between a glutamine residue and a lysine residue in a peptide or protein in the absence Ca2+forming an irreversible cross-link. In one example, the RNA-binding protein or peptide is genetically manipulated to comprise the MTG lysine recognition sequence (e.g., MRHKGS), for example at the N- or C- terminus, and the lipid moiety comprises the MTG glutamine recognition sequence (e.g., LLQG). In one example, the RNA-binding protein or peptide is genetically manipulated to comprise the MTG glutamine recognition sequence (e.g., LLQG or LQ), for example at the N- or C-terminus, and the lipid moiety comprises MTG lysine recognition sequence (e.g., MRHKGS). Other methods of enzymatic lipidation known to the skilled person may be used, such as those disclosed in Takahara & Kamiya (2020). Additional Lipids In one example, the lipid nanoparticle additionally comprises a PEG-lipid, a sterol structural lipid and / or a neutral lipid. In one example, the lipid nanoparticle does not comprise a cationic lipid. PEG-lipids In one example, the present disclosure provides a lipid nanoparticle comprising a PEGylated lipid. It will be apparent to the skilled person that reference to a PEGylated lipid is a lipid that has been modified with polyethylene glycol. Exemplary PEGylated lipids include, but are not limited to, PEG-modified phosphatidylethanolamines, PEG-modified phosphatidic acids, PEG-modified ceramides, PEG-modified dialkylamines, PEG- modified diacylglycerols, and PEG-modified dialkylglycerols. For example, a PEG lipid includes PEG-c-DMG, PEG-DMG, PEG-DLPE, PEG-DMPE, PEG-DPPC, a PEG- DSPE lipid and combinations thereof. Neutral lipids In one example, the present disclosure provides a lipid nanoparticle comprising a neutral lipid. Suitable neutral or zwitterionic lipids for use in the present disclosure will be apparent to the skilled person and include, for example, 1,2-distearoyl-sn-glycero-3- phosphocholine (DSPC), 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE), 1,2- dilinoleoyl-sn-glycero-3-phosphocholine (DLPC), 1,2-dimyristoyl-sn-glycero- phosphocholine (DMPC), 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), 1,2- dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), 1,2-diundecanoyl-sn-glycero- phosphocholine (DUPC), 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC), 1,2-di-O-octadecenyl-sn-glycero-3-phosphocholine (18:0 Diether PC), 1-oleoyl-2- cholesterylhemisuccinoyl-sn-glycero-3-phosphocholine (OChemsPC), 1-hexadecyl-sn- glycero-3-phosphocholine (C16 Lyso PC), 1,2-dilinolenoyl-sn-glycero-3- phosphocholine, 1,2-diarachidonoyl-sn-glycero-3-phosphocholine, 1,2- didocosahexaenoyl-sn-glycero-3-phosphocholine, 1,2-diphytanoyl-sn-glycero-3- phosphoethanolamine (ME 16.0 PE), 1,2-distearoyl-sn-glycero-3-phosphoethanolamine (DSPE), 1,2-dilinoleoyl-sn-glycero-3-phosphoethanolamine, 1,2-dilinolenoyl-sn- glycero-3-phosphoethanolamine, 1,2-diarachidonoyl-sn-glycero-3- phosphoethanolamine, 1,2-didocosahexaenoyl-sn-glycero-3-phosphoethanolamine, 1,2- dioleoyl-sn-glycero-3-phospho-rac-(1-glycerol) sodium salt (DOPG), and sphingomyelin. The lipids can be saturated or unsaturated. Structural lipids In one example, the present disclosure provides a lipid nanoparticle comprising a structural lipid. Exemplary structural lipids include, but are not limited to, cholesterol fecosterol, sitosterol, campesterol, stigmasterol, brassicasterol, ergosterol, tomatidine, tomatine, ursolic acid and alpha-tocopherol. In one example, the structural lipid is a sterol. For example, the structural lipid is cholesterol. In another example, the structural lipid is campesterol. Pharmaceutically acceptable carrier Suitably, in compositions or methods for administration of the RNA delivery vehicle of the disclosure to a subject, the delivery vehicle is combined with a pharmaceutically acceptable carrier as is understood in the art. Accordingly, one example of the present disclosure provides a composition (e.g., a pharmaceutical composition) comprising the RNA delivery vehicle comprising a lipid nanoparticle coated with a RNA-binding protein or peptide of the disclosure combined with a pharmaceutically acceptable carrier. In general terms, by “carrier” is meant a solid or liquid filler, binder, diluent, encapsulating substance, emulsifier, wetting agent, solvent, suspending agent, coating or lubricant that may be safely administered to any subject, e.g., a human. Depending upon the particular route of administration, a variety of acceptable carriers, known in the art may be used, as for example described in Remington's Pharmaceutical Sciences (Mack Publishing Co. N.J. USA, 1991). A RNA delivery vehicle of the present disclosure is useful for parenteral, topical, oral, or local administration, intramuscular administration, aerosol administration, or transdermal administration, for prophylactic or for therapeutic treatment. In one example, the RNA delivery vehicle is administered parenterally, such as intramuscularly, subcutaneously or intravenously. For example, the RNA delivery vehicle is administered intramuscularly. Formulation of RNA delivery vehicle to be administered will vary according to the route of administration and formulation (e.g., solution, emulsion, capsule) selected. An appropriate pharmaceutical composition comprising a RNA delivery vehicle to be administered can be prepared in a physiologically acceptable carrier. For solutions or emulsions, suitable carriers include, for example, aqueous or alcoholic / aqueous solutions, emulsions or suspensions, including saline and buffered media. Parenteral vehicles can include sodium chloride solution, Ringer's dextrose, dextrose and sodium chloride, lactated Ringer's or fixed oils. A variety of appropriate aqueous carriers are known to the skilled artisan, including water, buffered water, buffered saline, polyols (e.g., glycerol, propylene glycol, liquid polyethylene glycol), dextrose solution and glycine. Intravenous vehicles can include various additives, preservatives, or fluid, nutrient or electrolyte replenishers (see, generally, Remington's Pharmaceutical Science, 16th Edition, Mack, Ed. 1980). The compositions can optionally contain pharmaceutically acceptable auxiliary substances as required to approximate physiological conditions such as pH adjusting and buffering agents and toxicity adjusting agents, for example, sodium acetate, sodium chloride, potassium chloride, calcium chloride and sodium lactate. The RNA delivery vehicle can be stored in the liquid stage or can be lyophilized for storage and reconstituted in a suitable carrier prior to use according to art-known lyophilization and reconstitution techniques. The optimum concentration of the active ingredient(s) (i.e., the RNA) in the chosen medium can be determined empirically, according to procedures known to the skilled artisan, and will depend on the ultimate pharmaceutical formulation desired. Upon formulation, compositions of the present disclosure will be administered in a manner compatible with the dosage formulation and in such amount as is therapeutically / prophylactically effective. The dosage ranges for the administration of the RNA delivery vehicle of the disclosure are those large enough to produce the desired effect. For example, the composition comprises an effective amount of the RNA. In one example, the composition comprises a therapeutically effective amount of the RNA. In another example, the composition comprises a prophylactically effective amount of the RNA. The dosage should not be so large as to cause adverse side effects. Generally, the dosage will vary with the age, condition, sex and extent of the disease in the patient and can be determined by one of skill in the art. The dosage can be adjusted by the individual physician in the event of any complication. RNA The present disclosure provides a RNA delivery vehicle, the delivery vehicle comprising: a lipid nanoparticle comprising the RNA therein; and a RNA-binding protein or peptide coated on the exterior surface of the lipid nanoparticle. For example, the RNA- binding protein or peptide completely or partially encapsulates the lipid nanoparticle. The RNA of the present disclosure may be a naturally or non-naturally occurring RNA, or may include one or more modified nucleobases, nucleosides, or nucleotides. It will be apparent to the skilled person that RNA suitable for use in the present disclosure may also include a 5′ untranslated region (5’-UTR), a 3′ untranslated region (3’UTR), and / or a coding or translating sequence. In addition, the RNA may comprise a 5′ cap structure, a chain terminating nucleotide, a stem loop (e.g., a histone stem loop), a 3’ tailing sequence (e.g., a polyadenylation signal or one or more polyA tails. In one example of the present disclosure, the RNA is a self-replicating mRNA (sa-mRNA). In one example of the present disclosure, the RNA is a conventional mRNA (cRNA). Methods of Preparation Suitable methods for the production of a RNA delivery vehicle of the present disclosure will be apparent to the skilled person and / or described herein. For example, a RNA delivery vehicle of the present disclosure may be made using approaches which are well-known in the art of formulation. For example, suitable LNPs can be formed using mixing processes such as microfluidics, including herringbone micromixing, and T- junction mixing of two fluid streams, one of which contains the messenger RNA, typically in an aqueous solution, and the other of which has the various required lipid components, typically in ethanol. The LNPs may then be prepared by combining a phospholipid (such as DOPE or DSPC, which may be purchased from commercial sources including Avanti Polar Lipids, Alabaster, AL), a PEGylated lipid (such as 1,2-dimyristoyl-sn-glycerol methoxypoly ethylene glycol, also known as PEG-DMG, which may be purchased from commercial sources including Avanti Polar Lipids, Alabaster, AL), and a structural lipid / sterol (such as cholesterol, which may be purchased from commercial sources including Sigma- Aldrich), at concentrations of, for example, about 50 mM in ethanol. Solutions should be refrigerated during storage at, for example, -20° C. The various lipids may be combined to yield the desired molar ratios and diluted with water and ethanol to a final desired lipid concentration of, for example, between about 5.5 mM and about 25 mM. An LNP composition comprising a RNA, including, but not limited to, as a sa- mRNA or cRNA, may prepared by combining the above lipid solution with a solution including the RNA at, for example, a lipid component to RNA wt:wt ratio from about 5:1 to about 50:1. The lipid solution may be rapidly injected using a NanoAssemblr microfluidic system at flow rates between about 3 ml / min and about 18 ml / min into the RNA solution to produce a suspension with a water to ethanol ratio between about 1:1 and about 4:1. For LNP compositions including a sa-mRNA or cRNA, solutions of the RNA at concentrations of 1.0 mg / ml in deionized water may be diluted in 50 mM sodium citrate buffer at a pH between 3 and 6 to form a stock solution. LNP compositions may be further processed, as is known in the art, by 10-fold dilution into 50 mM citrate buffer at pH 6 and subjected to tangential flow filtration (TFF) using a 300k molecular weight cut-off membrane (mPES) until concentrated to the original volume. Subsequently, in one example, the citrate buffer may be replaced with a buffer containing 20 mM Tris buffer at pH 7.5, 80 mM sodium chloride, and 3% sucrose using diafiltration with a 10-fold volume of the new buffer. The LNP solution may be concentrated to a volume of, for example, between 5-10 mL, filtered using a 0.2 micron PES syringe filter, aliquoted into vials, and frozen at 1°C / min using a Corning® CoolCell® LX Cell Freezing Container until the samples reach -80°C. Samples may be stored at -80°C until needed. The method described above induces nano-precipitation and particle formation. Alternative processes including, but not limited to, T-junction and direct injection, may be used to achieve the same nano-precipitation. In some examples, the lipid component of the LNP formulation comprises about 2 mol % to about 25 mol % phospholipid (neutral lipid), about 18.5 mol % to about 60 mol % structural lipid (sterol), and about 0.2 mol % to about 10 mol % of PEGylated lipid, provided that the total mol % does not exceed 100%. In some examples, the lipid component of the LNP formulation comprises about 5 mol % to about 20 mol % phospholipid, about 30 mol % to about 55 mol % structural lipid, and about 1 mol % to about 5 mol % of PEGylated lipid. In a particular example, the lipid component includes about 10 mol % phospholipid, about 48 mol % structural lipid, and about 2.0 mol % of PEG lipid. In some examples, the phospholipid may be DOPE or DSPC. In other examples, the PEG lipid may be PEG-DMG and / or the structural lipid may be cholesterol. In some examples, the PEG lipid may be PEG-DMG and the structural lipid may be cholesterol. In some examples, the PEG lipid may be PEG-DMG. In some examples, the structural lipid may be cholesterol. The RNA delivery vehicle can then be formed by combining the LNP with RNA binding proteins or peptides in a solution, typically in an aqueous solution. The RNA- binding protein or peptide binds to unencapsulated and / or partially encapsulated RNA on the exterior surface of the lipid nanoparticle and / or to the exterior surface of the lipid nanoparticle. In one example, the RNA-binding protein or peptide binds to unencapsulated and partially encapsulated RNA on the exterior surface of the lipid nanoparticle and to the exterior surface of the lipid nanoparticle. In one example, the RNA-binding protein or peptide binds to unencapsulated and partially encapsulated RNA on the exterior surface of the lipid nanoparticle. In one example, the RNA-binding protein or peptide binds to unencapsulated RNA on the exterior surface of the lipid nanoparticle. In one example, the RNA-binding protein or peptide binds to partially encapsulated RNA on the exterior surface of the lipid nanoparticle. In one example, the RNA-binding protein or peptide binds to the exterior surface of the lipid nanoparticle. In some examples, the binding is non-covalent binding. For example, the binding is ionic non-covalent reversible binding. The efficiency of encapsulation of the RNA within the LNPs may be at least 50%, for example about 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%. In some examples, the encapsulation efficiency may be at least 80%. In certain examples, the encapsulation efficiency may be at least 90%. Assaying Lipid Nanoparticles of the Disclosure Lipid nanoparticles of the present disclosure are readily screened for physical and biological activity and / or stability using methods known in the art and / or as described below. Assessing RNA degradation In one example, the level of RNA degradation by RNases is assessed. For example, the RNA, alone or in combination with the RNA-binding protein or peptide, is treated with RNase. In one example, the level of RNA is assessed in RNase treated and untreated samples using real time PCR. In one example, the cycle threshold (CT) value in RNA samples without a RNA-binding protein or peptide are increased compared to RNA samples with a RNA-binding protein or peptide indicating RNA degradation. Assessing RNA translation In one example, RNA translation is assessed using an in vitro translation system. Suitable systems for use in the present disclosure will be apparent to the skilled person, and include for example a rabbit reticulocyte lysate assay. In one example, a rabbit reticulocyte lysate assay is used. In one example, the RNA is assessed in the presence or absence of a RNA-binding protein or peptide. In one example, the RNA is nanoluciferase RNA (nLuc RNA) and the amount of RNA translation is measured by the amount of luciferase produced as assessed by measuring luminescence in relative light units (RLU). In one example, the assay is performed at 4oC, 24oC and / or 37oC. For example, the assay is performed at 4oC. In one example, the assay is performed at 24oC. In one example, the assay is performed at 37oC. In another example, the assay is performed after incubating the samples for 0 hours, 1 hour, 2 hours, 4 hours, 8 hours, 24 hours, 48 hours or 96 hours. Assessing TLR induction In one example, the level of TLR3 and / or TLR8 induction is assessed. For example, the level of TLR3 and / or TLR8 induction by the RNA, alone or in combination with the RNA-binding protein or peptide is assessed. In one example, TLR3 and / or TLR8 induction is assessed using a TLR induction NfKB reporter assay. In this assay, NfKB is operationally linked to a secretary alkaline phosphatase (SEAP). RNA is introduced into either cell type (TLR3 conditionally transduced, or TLR8 conditionally transduced). Binding of the TLR receptor induces NfKB activation and in turn SEAP. In one example, the SEAP level is determined by a chemical reaction and calorific read out. Assessing unencapsulated and / or partially encapsulated RNA The present disclosure provides a method of detecting unencapsulated and / or partially encapsulated RNA on the exterior surface of a lipid nanoparticle. Suitable methods of detecting will be apparent to the skilled person and / or are described herein. Exemplary methods for detecting unencapsulated and / or partially encapsulated RNA on the exterior surface of a lipid nanoparticle include an ELISA, a FLISA, a lateral flow assay or affinity chromatography. Standard ELISA, FLISA, lateral flow or affinity chromatography formats are useful in determining the concentration of unencapsulated and / or partially encapsulated RNA on the exterior surface of a lipid nanoparticle. In one example, the method involves immobilizing a RNA binding protein or peptide which binds to the unencapsulated and / or partially encapsulated RNA onto a solid support. The term “solid support” shall be taken to mean a matrix to which molecules may be attached, directly or indirectly. The solid support may include any substrate material that is capable of providing physical support for the compositions described herein. The materials may be naturally occurring, synthetic, or a modification of a naturally occurring material. Suitable matrix materials may include glass fibers, polyester, cellulose, rayon, silicon, a silicon wafer chip, graphite, mirrored surfaces, laminates, membranes, ceramics, plastics (including polymers such as, e.g., poly(vinyl chloride), cyclo-olefin copolymers, agarose gels or beads, polyacrylamide, polyacrylate, polyethylene, polypropylene, poly(4-methylbutene), polystyrene, polymethacrylate, poly(ethylene terephthalate), polytetrafluoroethylene (PTFE or Teflon®), nylon, poly(vinyl butyrate)), germanium, gallium arsenide, gold, silver, Langmuir Blodgett films, a flow through chip, etc., either used by themselves or in conjunction with other materials. Additional rigid materials may be considered, such as glass, which includes silica and further includes, for example, glass that is available as Bioglass. Other materials that may be employed include porous materials, such as, for example, controlled pore glass beads, crosslinked beaded Sepharose® or agarose resins, or copolymers of crosslinked bis-acrylamide and azalactone. A RNA binding protein or peptide that specifically binds to the unencapsulated and / or partially encapsulated RNA on the exterior surface of a lipid nanoparticle is brought into contact with a sample comprising lipid nanoparticles, and the RNA binding protein or peptide forms a direct bond with any of its target unencapsulated and / or partially encapsulated RNA present in said sample. This RNA binding protein or peptide is contacted with a detection protein comprising an antibody variable region generally labeled with a detectable reporter molecule, such as for example, a magnetic label (e.g. a magnetic bead), a fluorescent label (e.g. FITC or Texas Red) or a fluorescent semiconductor nanocrystal (as described in US 6,306,610) in the case of a FLISA or an enzyme (e.g. horseradish peroxidase (HRP), alkaline phosphatase (AP) or β- galactosidase) in the case of an ELISA, or alternatively a labeled protein or antibody can be used that binds to the RNA binding protein or peptide. Following washing to remove any unbound lipid nanoparticle the label is detected either directly, in the case of a magnetic or fluorescent label, or through the addition of a substrate, such as for example hydrogen peroxide, TMB, or toluidine, or 5-bromo-4-chloro-3-indol-beta-D- galaotopyranoside (x-gal) in the case of an enzymatic label. For example, the magnetic label is detected by a magnetic reader which measures the magnetic field change induced by the label. The signal measured by the magnetic reader is proportional to the bound unencapsulated and / or partially encapsulated RNA within the sample. As used herein, a “detectable label” is a molecular or atomic tag or marker that generates or can be induced to generate an optical or other signal or product that can be detected visually or by using a suitable detector. Detectable labels are well known in the art and include, for example, a magnetic label, a radiolabel, an enzyme, a fluorescent label, a luminescent label, a bioluminescent label, a prosthetic group, a contrast agent and an ultrasound agent. Such methods are particularly suitable for high sensitivity quantification of the amount of unencapsulated and / or partially encapsulated RNA in a sample by calibrating the detection system against known amounts of a standard to which the RNA protein or peptide binds, such as for example, RNA. The skilled person will understand that the method of the present disclosure is suitable for use on a capture enzyme-linked immunosorbent assay (ELISA) or enzyme immunoassay (EIA). As used herein, the term “ELISA” or “sandwich ELISA” or “capture ELISA” or “EIA” refers to immobilizing a RNA binding protein or peptide onto a matrix, such as, for example, a membrane, a polystyrene or polycarbonate microwell, a polystyrene or polycarbonate dipstick or a glass support, followed by addition of an amount of a sample comprising lipid nanoparticles. The unencapsulated and / or partially encapsulated RNA is then “bound” or “captured”. The bound or captured unencapsulated and / or partially encapsulated RNA is detected by the detection protein which can be covalently linked to a magnetic label, or can itself be detected by addition of a secondary protein or antibody which is linked to a magnetic label. Lateral flow assays, also known as “immunochromatographic strip tests” operate on the same principles as ELISA. In essence, these tests run a liquid sample along the surface of a membrane or filter paper with reactive molecules that show a visual positive or negative result depending on the presence of a particular analyte (e.g., unencapsulated and / or partially encapsulated RNA). The skilled person will understand that the method of the present disclosure is also suitable for use on a chromatography column (e.g. affinity chromatography column). Microarrays, BIAcore assays, differential centrifugation, chromatography, electrophoresis, immunoprecipitation, optical biosensors, and other surface plasmon resonance assays can be used as described in WO 2011 / 061351 incorporated herein by reference. Methods of using magnetic labels are described in US 2007 / 0254375 incorporated herein by reference. It will be apparent to the skilled person that the methods described herein are amenable to high throughput methods, such as, for example automation of screening processes or a microarray format as described in Mendoza et al., 1999. Furthermore, variations of the above-described methods will be apparent to those skilled in the art, such as, for example, a competitive ELISA, continuous affinity chromatography. The invention is further disclosed in the following numbered paragraphs: 1. A RNA delivery vehicle, the delivery vehicle comprising: (i) a lipid nanoparticle comprising the RNA therein; and (ii) a RNA-binding protein or peptide coated on the exterior surface of the lipid nanoparticle. 2. The RNA delivery vehicle of paragraph 1, wherein the RNA-binding protein or peptide encapsulates the lipid nanoparticle. 3. The RNA delivery vehicle of paragraph 1 or 2, wherein the RNA-binding protein or peptide binds directly to unencapsulated and / or partially encapsulated RNA on the exterior surface of the lipid nanoparticle. 4. The RNA delivery vehicle of any one of paragraphs 1 to 3, wherein the RNA- binding protein or peptide is a lipidated RNA-binding protein or peptide. 5. The RNA delivery vehicle of any one of paragraphs 1 to 4, wherein the RNA- binding protein or peptide: a) reduces toxicity of the lipid nanoparticle, and / or b) stabilizes the RNA, and / or c) protects the RNA from degradation, and / or d) facilitates nucleation of the lipid nanoparticle, and / or e) inhibits induction of signalling by one or more Toll-like Receptors. 6. The RNA delivery vehicle of any one of paragraphs 1 to 5, wherein the RNA- binding protein or peptide is modified to remove nuclear localisation signal(s) and / or introduce nuclear export signal(s). 7. The RNA delivery vehicle of any one of paragraphs 1 to 6, wherein the RNA- binding protein or peptide is a viral or non-viral RNA-binding protein or peptide. 8. The RNA delivery vehicle of paragraph 7, wherein the viral RNA-binding protein is from a class III, class IV, class V and / or class VI virus. 9. The RNA delivery vehicle of paragraph 8, wherein the viral RNA binding protein or peptide is a respiratory virus selected from the group consisting of an influenza virus, a respiratory syncytial virus, a parainfluenza virus, a metapneumovirus, a rhinovirus, a coronavirus, an adenovirus and a bocavirus. 10. The RNA delivery vehicle of paragraph 9, wherein the viral RNA-binding protein or peptide is a nucleoprotein, a non-structural protein, a matrix protein and / or a nucleocapsid protein. 11. The RNA delivery vehicle of any one of paragraphs 7 to 10, wherein the viral RNA-binding protein or peptide is a non-structural (NS) protein from an influenza B virus. 12. The RNA delivery vehicle of any one of paragraphs 7 to 11, wherein the viral RNA-binding protein or peptide comprises a sequence set forth in any one of SEQ ID NOs: 9 to 11. 13. The RNA delivery vehicle of paragraph 7, wherein the non-viral RNA binding protein or peptide is derived from a cellular protein associated with cell growth, cell signalling and / or anti-viral pathways. 14. The RNA delivery vehicle of paragraph 13, wherein the cellular protein is selected from the group consisting of a TAR RNA-binding protein (TRBP), a protein kinase R (PKR) RNA-binding protein, a Toll-like Receptor 3 (TLR-3) binding protein, a TLR-7 binding protein and combinations thereof. 15. The RNA delivery vehicle of paragraph 13 or 14, wherein the cellular protein comprises a sequence set forth in any one of SEQ ID NOs: 1 to 8. 16. The RNA delivery vehicle of any one of paragraphs 1 to 15, wherein the lipid nanoparticle comprises a PEG-lipid, a structural lipid, a neutral lipid and / or a cationic lipid. 17. The RNA delivery vehicle of any one of paragraphs 1 to 16, wherein the lipid nanoparticle does not comprise a cationic lipid. 18. The RNA delivery vehicle of any one of paragraphs 1 to 17, wherein the RNA is selected from the group consisting of messenger RNA (mRNA), small-interfering RNA (siRNA), microRNA (miRNA) and antisense RNA. 19. The RNA delivery vehicle of paragraph 18, wherein the mRNA is self-replicating mRNA (sa-mRNA) or a conventional RNA (cRNA). 20. An immunogenic composition comprising the RNA delivery vehicle of any one of paragraphs 1 to 19. 21. A pharmaceutical composition comprising the RNA delivery vehicle of any one of paragraphs 1 to 19 or the immunogenic composition of paragraph 20 and a pharmaceutically acceptable carrier. 22. The RNA delivery vehicle of any one of paragraphs 1 to 19, the immunogenic composition of paragraph 20, or the pharmaceutical composition of paragraph 21 for use in therapy. 23. A method of detecting unencapsulated and / or partially encapsulated RNA on the exterior surface of a lipid nanoparticle, the method comprising: (i) contacting a sample comprising a lipid nanoparticle to a RNA binding protein or peptide which binds to unencapsulated and / or partially encapsulated RNA on the exterior surface of the lipid nanoparticle to thereby form a complex; (ii) contacting the complex with a detection protein comprising an antibody variable region, wherein the detection protein binds to the RNA binding protein or peptide and wherein the detection protein comprises a detectable label; and (iii) detecting the detectable label, wherein presence of the detectable label is indicative of the presence of unencapsulated and / or partially encapsulated RNA on the exterior surface of the lipid nanoparticle in the sample. 24. The method of paragraph 23, wherein the detectable label is a magnetic label. 25. The method of paragraph 23 or 24, wherein the sample comprises the RNA delivery vehicle of any one of paragraphs 1 to 19. The present disclosure includes the following non-limiting Examples. EXAMPLES Example 1: Protection of RNA from degradation by RNases An RNA-free monovalent pooled harvest (MPH) was prepared by treating MPH with RNase. MPH (B / Malaysia / 2506 / 2004) was treated twice using RNase A (Promega) for 1 hour at 37°C. RNA was extracted from 140μl treated and untreated MPH (eluted in 60μl), and tested for haemagglutinin (HA) and neuraminidase (NA) RNA using real time PCR. The results showed no increase in CT value for HA RNA and a small increase for NA RNA (Table 2; Exp.1A), indicating minimal degradation of viral RNA. In case the RNase was inactive, the MPH was treated using a different RNase (RNase ONE, Promega M4261), twice, prior to extraction and analysis of RNA. The CT values for both HA and NA RNA increased (Table 2; Exp.1B), indicating a decrease in the amount of viral RNA present (< 83-fold). Further samples of MPH (180 µl) were treated twice using decreasing doses of RNase ONE in the presence of RNase ONE sample buffer. Analysis of treated samples showed dose-dependent decreases in RNA concentration and increases in CT value (Table 2; Exp.1C), indicating low levels of degradation of RNA upon treatment of MPH with RNase ONE (< 35-fold). Overall, the level of degradation of RNA in treated MPH was unexpectedly small. MPH (B / Malaysia / 2506 / 2004) was then treated with RNase ONE in the presence or absence of a disruption buffer. Use of the disruption buffer did not increase degradation of viral RNA in MPH treated with RNase (Table 2; Exp.2). Treatment of MPH with RNase resulted in small reductions in viral RNA only, indicating possible protection of RNA from degradation by RNases. Table 2. Treatment of MPH with RNase. * All RNA treatment was performed twice, each for 1 h at 37°C. NT – not tested. ** Volumes were equalised using PBS. # Baseline level Example 2: Purification of RNA-free nucleoprotein from influenza virus RNA-free nucleoprotein (NP) from influenza virus was isolated by performing dialysis, concentration and detergent treatment followed by a glycerol step gradient centrifugation to isolate the NP:RNA particles. To isolate the RNA-free NP, a further glycerol and caesium chloride gradient centrifugation step was performed. Example 3: RNA-free NP binds RNA To assess whether RNA-free NP protects RNA, NP was combined with nanoluciferase mRNA and samples analysed by MOPS- Agarose Gel electrophoresis following heating to 40oC or incubation at room temperature. On increasing the concentration of NP in the reaction (from 0 to 4000ng), whilst maintaining the concentration of mRNA (250ng), the level of detectable mRNA shifted to a higher molecular weight. At a ratio of 16:1 (4000ng NP; 250ng mRNA), the nanoluciferase mRNA was shifted to be unable to enter the gel. These results indicate that in the presence of increasing NP concentration, increasing amounts of RNA can be complexed to the NP. Using a rabbit reticulocyte lysate as an in vitro translation system, it was shown that at a ratio of 16:1 (4000ng NP; 250ng mRNA), the amount of luciferase produced as assessed by measuring luminescence in relative light units (RLU) was comparable to luciferase RNA alone, whilst 4000ng of NP alone reduced the signal by 2-3 fold (Figure 1). These results indicate that in the presence of increasing NP concentration, RNA is bound by the NP without inhibiting in vitro translation. Example 4: RNA-free NP protects RNA from degradation To assess whether RNA-free NP protects RNA, the NP:RNA and RNA alone were assessed in a RNase assay. Briefly, NP:RNA or RNA was treated with RNase and incubated for 5-10 minutes at 30oC. Samples were further treated with or without 1μl thermolabile proteinase K (PK; NEB P8111S). The reaction was incubated at 37oC for 15-30 minutes, followed by incubation at 60oC for 10-20 minutes to inactivate the PK. 1-2μl RNasine (Promega N2611) was added if required. The level of RNA present was assessed in treated and untreated samples using real time PCR. As shown in Figure 2, there is no increase in CT value in NP:RNA treated with RNase indicating no degradation of viral RNA. In contrast, the CT value of RNA treated with RNase alone significantly increased (p=0.0005), indicating a decrease in the amount of viral RNA present. These results further confirm that in the presence of NP, RNA is protected from degradation by RNase. The addition of PK, which degrades NP, to NP:RNA showed a slight increase in CT value indicating minimal degradation of RNA. The addition of PK in combination with RNase showed a significant increase in CT value (<0.0001) indicating a decrease in the amount of viral RNA present. These results further confirm that in the presence of NP, RNA is protected from degradation by RNase.Example 5: RNA-free NP protects RNA from degradation at 4oC, 24oC and 37oCTo assess whether the ability of NP to protect nanoluciferase RNA (nLuc RNA) was temperature dependent, NP:nLuc RNA and nLuc RNA was incubated at 4oC, 24oC and 37oC for up to 96 hours and the amount of luciferase produced as assessed by measuring luminescence in RLU. As shown in Figure 3, there was no significant difference in RLU between NP:nLuc RNA and nLuc RNA alone at 4oC. At 24oC, there was a notable reduction in RLU at 96 hours post incubation (p=0.0034) in nLuc RNA compared to NP:nLuc RNA indicating protection of the RNA from degradation by the NP. After 8 hours at 37oC, there was a notable reduction in RLU in nLuc RNA compared to NP:nLuc RNA, demonstrating further long term protection of the RNA by the NP. Example 6: RNA-free NP protects TLR induction To assess whether the presence of NP inhibits RNA induction of dsRNA or ss RNA, TLR3 and / or TLR8 induction was assessed using a TLR induction NfKB reporter assay. In this assay, NfKB is operationally linked to a secretary alkaline phosphatase (SEAP). RNA is introduced into either cell type (TLR3 conditionally transduced, or TLR8 conditionally transduced). Binding of the TLR receptor induces NfKB activation and in turn SEAP. The SEAP level can be determined by a chemical reaction and calorific read out. As shown in Figure 4, RNA alone stimulates both TLR3 and TLR8 induction and the presence of NP reduces the induction of TLR3 and TLR8 at both 2 and 4 hours post- incubation. Example 7: RNA-free NP conjugation with maleimide-DSPE lipid NP (0.85mg / ml) was conjugated with maleimide-DSPE (1,2-Distearoyl-sn- glycero-3-phosphorylethanolamine; 8mM) by incubating NP with DSPE in the presence of 10% ethanol. The labelled and unlabelled NP was run on a non-reducing gel to assess molecular weight of the protein and confirm conjugation of the protein with a molecular weight shift of the NP. In addition, DSPE forms a suspension (i.e., liposomes) so the composition was centrifuged and the supernatant assessed. It was subsequently shown that lipidated NP:RNA could be pulled down by centrifugation, whilst RNA alone in the presence of lipid (i.e., not in the presence of NP) could not be. Example 8: COVID nucleocapsid protects RNA RNA-free nucleocapsid from SARS-CoV-2 (NP(SCoV2)) was purified as described above for influenza virus. The ability of NP(SCoV2) to protect nLucRNA from degradation was assessed in an in vitro translation system by measuring the amount of luciferase produced as assessed by measuring luminescence in RLU for up to 168 hours. As shown in Figure 5, there was a reduction in RLU in nLucRNA alone over time indicating degradation of the nLucRNA. Whilst there appeared to be a slight reduction in RLU in NP(SCoV2):nLuc RNA compositions at 16:1 and 8:1 (w / w), suggesting RNA degradation, PCR analysis of the NP(SCoV2):nLucRNA material at each time point confirmed that the RNA is intact and not degraded. In addition, the accessibility of the NP(SCoV2) encapsulated RNA was assessed using a ribogreen dye exclusion assay. As shown in Figure 5B, the presence of the NP(SCoV2) at increasing concentrations interferes with the dye binding to the nLucRNA, however based on the fluorescence signal, the RNA is still accessible to the dye at a 16:1 ratio (4000ng NP; 250ng mRNA). This suggests that whilst the NP(SCoV2) coats and protects the RNA, it does not completely encapsulate the RNA. Example 9: Preparation of RNA-binding peptides Cellular and viral protein sequences were reviewed to identify protein domains and peptide sequences that had the potential to bind RNA. Sequences from cellular proteins correlate to those proteins associated with cell growth, cell signalling and / or antiviral pathways whereas sequences from viral proteins were derived from non- structural and nuclear proteins. Peptides were designed from sequences derived from cellular proteins including TAR RNA binding protein (TRBP), Protein Kinase R (PKR), Toll-like receptor 3 (TLR- 3) and TLR-7 (Table 3). Viral RNA binding proteins included nucleoprotein and non- structural proteins from influenza (Table 4). RNA binding peptide sequences were modified to either exclude known nuclear localisation signals, or include nuclear export signals to facilitate correct localisation of peptide bound RNA when this material is introduced into cells (Table 3). Example 10: Encapsulation assay to detect RNA on the exterior of LNPs To develop an encapsulation assay to detect and discriminate between internal / external mRNA on LNPs, the immunoprecipitation of mRNA was assessed using magnetic beads, an anti-NP monoclonal antibody (mAb), and with and without the presence of a recombinant NP. Immunoprecipitation of mRNA in the absence of recombinant NP PBS washed magnetic beads (Dynabeads) were coated with 10 µg of an anti-NP mAb and incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant containing any unbound anti-NP mAb was removed. The magnetic beads were then washed in PBS to remove any residual unbound anti-NP mAb and the magnetic beads were then coated with different concentrations of luciferase mRNA (500, 100, 50, 10 or 0 ng) and incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant collected (Eluted) and the magnetic beads were resuspended in PBS (Bound). The Eluted and Bound supernatant were then diluted 1:10 in 0.05% Triton-X 100 and incubated at 95°C for 10 minutes. The supernatants were allowed to cool to room temperature and RNA concentration was measured using the Ribogreen RNA assay kit. 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[0002] T 5 6 7 8 T P # 1 23 Immunoprecipitation of mRNA in the presence of recombinant NP PBS washed magnetic beads (Dynabeads) were coated with 10 µg of an anti-NP mAb and incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant containing any unbound anti-NP mAb was removed. The magnetic beads were then washed in PBS to remove any residual unbound anti-NP mAb and the magnetic beads were then coated with 20 ug of NP recombinant protein and incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant containing any unbound recombinant NP was removed. The magnetic beads were washed in PBS to remove any further unbound recombinant NP protein. The magnetic beads were then coated with different concentrations of luciferase mRNA (500, 100, 50, 10 or 0 ng) and incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant collected (Eluted) and the magnetic beads were resuspended in PBS (Bound). The Eluted and Bound supernatant were then diluted 1:10 in 0.05% Triton-X 100 and incubated at 95°C for 10 minutes. The supernatants were allowed to cool to room temperature and RNA concentration was measured using the Ribogreen RNA assay kit. As shown in Figure 6 mRNA was not immunoprecipitated without recombinant NP but it was immunoprecipitated in the presence of a recombinant NP. LNP preparation mRNA found on the exterior (mRNA-LNP) or interior ((mRNA)-LNP) surface of a LNP were prepared with DOTAP, DSPC, Cholesterol and DMG-PEG. Lipids were prepared in ethanol to a standard molarity and lipids were then mixed together. Luciferase mRNA were prepared with or without RNA bound to NP. The ratios of NP to mRNA was 2:1. mRNA was then encapsulated in the lipid mix using a nanoassembler. Immunoprecipitation of mRNA found on the exterior or interior surface of a LNP in the presence of recombinant NP protein PBS washed magnetic beads (Dynabeads) were coated with 10 µg of an anti-NP mAb and incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant containing any unbound anti-NP mAb was removed. The magnetic beads were then washed in PBS to remove any residual unbound anti-NP mAb and the magnetic beads were then coated with 20 µg of NP recombinant protein and incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant containing any unbound recombinant NP was removed. The magnetic beads were washed in PBS to remove any further unbound recombinant NP protein. The magnetic beads were then coated with LNPs containing mRNA on the exterior (mRNA- LNP) or interior ((mRNA)-LNP) surface of a LNP and were incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant collected (Eluted) and the magnetic beads were resuspended in PBS (Bound). The Eluted and Bound supernatant were then diluted 1:10 in 0.05% Triton-X 100 and incubated at 95°C for 10 minutes. The supernatants were allowed to cool to room temperature and RNA concentration was measured using the Ribogreen RNA assay kit. Immunoprecipitation of mRNA found on the exterior or interior surface of a LNP in the absence of recombinant NP protein PBS washed magnetic beads (Dynabeads) were coated with 10 µg of an anti-NP mAb and incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant containing any unbound anti-NP mAb was removed. The magnetic beads were then washed in PBS to remove any residual unbound anti-NP mAb. The magnetic beads were then coated with LNPs containing mRNA on the exterior (mRNA-LNP) or interior ((mRNA)-LNP) surface of a LNP and were incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant collected (Eluted) and the magnetic beads were resuspended in PBS (Bound). The Eluted and Bound supernatant were then diluted 1:10 in 0.05% Triton-X 100 and incubated at 95°C for 10 minutes. The supernatants were allowed to cool to room temperature and RNA concentration was measured using the Ribogreen RNA assay kit. As shown in Figure 7 mRNA on the exterior (mRNA-LNP) or interior ((mRNA)- LNP) surfaces of LNPs was immunoprecipitated in the presence of a recombinant NP and partially immunoprecipitated without the presence of a recombinant NP. Immunoprecipitation of NP bound mRNA found on the exterior or interior surface of a LNP in the presence of recombinant NP protein PBS washed magnetic beads (Dynabeads) were coated with 10 µg of an anti-NP mAb and incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant containing any unbound anti-NP mAb was removed. The magnetic beads were then washed in PBS to remove any residual unbound anti-NP mAb and the magnetic beads were then coated with 20 µg of NP recombinant protein and incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant containing any unbound recombinant NP was removed. The magnetic beads were washed in PBS to remove any further unbound recombinant NP protein. The magnetic beads were then coated with LNPs containing mRNA on the exterior (NP- mRNA-LNP) or interior ((NP-mRNA)-LNP) surface of a LNP and were incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant collected (Eluted) and the magnetic beads were resuspended in PBS (Bound). The Eluted and Bound supernatant were then diluted 1:10 in 0.05% Triton-X 100 and incubated at 95°C for 10 minutes. The supernatants were allowed to cool to room temperature and RNA concentration was measured using the Ribogreen RNA assay kit. Immunoprecipitation of NP bound mRNA found on the exterior or interior surface of a LNP in the absence of recombinant NP protein PBS washed magnetic beads (Dynabeads) were coated with 10 µg of an anti-NP mAb and incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant containing any unbound anti-NP mAb was removed. The magnetic beads were then washed in PBS to remove any residual unbound anti-NP mAb. The magnetic beads were then coated with LNPs containing mRNA on the exterior (NP+mRNA-LNP) or interior ((NP+mRNA)- LNP) surface of a LNP and were incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant collected (Eluted) and the magnetic beads were resuspended in PBS (Bound). The Eluted and Bound supernatant were then diluted 1:10 in 0.05% Triton-X 100 and incubated at 95°C for 10 minutes. The supernatants were allowed to cool to room temperature and RNA concentration was measured using the Ribogreen RNA assay kit. As shown in Figure 8 NP bound mRNA on the exterior (NP+mRNA-LNP) or interior ((NP+mRNA)-LNP) surfaces of LNPs was immunoprecipitated in the presence of a recombinant NP and partially immunoprecipitated without the presence of a recombinant NP. LNP preparation with decreasing amounts of ionisable lipids LNPs were prepared with Dlin-MC3, DSPC, Cholesterol and DMG-PEG. Lipids were prepared in ethanol to a standard molarity and lipids were then mixed at different ratios of ionizable lipid (Dlin-MC3) to DMG-PEG. Luciferase mRNA were prepared with or without RNA bound to NP. The ratios of NP to mRNA was 2:1. mRNA was then encapsulated in the lipid mix using a nanoassemblr. Immunoprecipitation of mRNA encapsulated within LNPs that contain decreasing amounts of ionizable lipid in the presence of recombinant NP protein PBS washed magnetic beads (Dynabeads) were coated with 10 µg of an anti-NP mAb and incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant containing any unbound anti-NP mAb was removed. The magnetic beads were then washed in PBS to remove any residual unbound anti-NP mAb and the magnetic beads were then coated with 20 µg of NP recombinant protein and incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant containing any unbound recombinant NP was removed. The magnetic beads were washed in PBS to further remove any unbound recombinant NP protein. The magnetic beads were then coated mRNA encapsulated within LNPs that contain decreasing amounts of ionizable lipid and were incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant collected (Eluted) and the magnetic beads were resuspended in PBS (Bound). The Eluted and Bound supernatant were then diluted 1:10 in 0.05% Triton-X 100 and incubated at 95°C for 10 minutes. The supernatants were allowed to cool to room temperature and RNA concentration was measured using the Ribogreen RNA assay kit. Immunoprecipitation of mRNA encapsulated within LNPs that contain decreasing amounts of ionizable lipid in the absence of recombinant NP protein PBS washed magnetic beads (Dynabeads) were coated with 10 µg of an anti-NP mAb and incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant containing any unbound anti-NP mAb was removed. The magnetic beads were then washed in PBS to remove any residual unbound anti-NP mAb. The magnetic beads were then coated with mRNA encapsulated within LNPs that contain decreasing amounts of ionizable lipid and were incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant collected (Eluted) and the magnetic beads were resuspended in PBS (Bound). The Eluted and Bound supernatant were then diluted 1:10 in 0.05% Triton-X 100 and incubated at 95°C for 10 minutes. The supernatants were allowed to cool to room temperature and RNA concentration was measured using the Ribogreen RNA assay kit. As shown in Figure 9 decreasing the amount of ionizable lipids leads to increased immunoprecipitation of mRNA with an anti-NP mAb. Immunoprecipitation of NP bound mRNA encapsulated within LNPs that contain decreasing amounts of ionizable lipid in the presence of recombinant NP protein PBS washed magnetic beads (Dynabeads) were coated with 10 µg of an anti-NP mAb and incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant containing any unbound anti-NP mAb was removed. The magnetic beads were then washed in PBS to remove any residual unbound anti-NP mAb and the magnetic beads were then coated with 20 µg of NP recombinant protein and incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant containing any unbound recombinant NP was removed. The magnetic beads were washed in PBS to further remove any unbound recombinant NP protein. The magnetic beads were then coated NP bound mRNA encapsulated within LNPs that contain decreasing amounts of ionizable lipid and were incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant collected (Eluted) and the magnetic beads were resuspended in PBS (Bound). The Eluted and Bound supernatant were then diluted 1:10 in 0.05% Triton-X 100 and incubated at 95°C for 10 minutes. The supernatants were allowed to cool to room temperature and RNA concentration was measured using the Ribogreen RNA assay kit. Immunoprecipitation of NP bound mRNA encapsulated within LNPs that contain decreasing amounts of ionizable lipid in the absence of recombinant NP protein PBS washed magnetic beads (Dynabeads) were coated with 10 µg of an anti-NP mAb and incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant containing any unbound anti-NP mAb was removed. The magnetic beads were then washed in PBS to remove any residual unbound anti-NP mAb. The magnetic beads were then coated with NP bound mRNA encapsulated within LNPs that contain decreasing amounts of ionizable lipid and were incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant collected (Eluted) and the magnetic beads were resuspended in PBS (Bound). The Eluted and Bound supernatant were then diluted 1:10 in 0.05% Triton-X 100 and incubated at 95°C for 10 minutes. The supernatants were allowed to cool to room temperature and RNA concentration was measured using the Ribogreen RNA assay kit. As shown in Figure 10 the use of NP bound mRNA increases the amount of mRNA that can be immunoprecipitated. LNPs containing an ionizable lipid mRNA-LNPs or NP+mRNA-LNPs were added to PBS washed magnetic beads (Dynabeads). The magnetic beads were incubated for 20 minutes at room temperature with shaking rotation. The magnetic beads were then placed on a magnet and the supernatant collected (Eluted) and the magnetic beads were resuspended in PBS (Bound). The Eluted and Bound supernatant were then diluted 1:10 in 0.05% Triton-X 100 and incubated at 95°C for 10 minutes. The supernatants were allowed to cool to room temperature and RNA concentration was measured using the Ribogreen RNA assay kit. As shown in Figure 11 LNPs that contain an ionizable lipid do not bind to the magnet used in the immunoprecipitation assay. Additionally, it was found that the use of NP bound mRNA leads to increased LNP size (Table 5). Table 5: LNP size

Claims

CLAIMS 1. A RNA delivery vehicle, the delivery vehicle comprising: (i) a lipid nanoparticle comprising the RNA therein; and (ii) a RNA-binding protein or peptide coated on the exterior surface of the lipid nanoparticle.

2. The RNA delivery vehicle of claim 1, wherein the RNA-binding protein or peptide encapsulates the lipid nanoparticle.

3. The RNA delivery vehicle of claim 1, wherein the RNA-binding protein or peptide binds directly to unencapsulated and / or partially encapsulated RNA on the exterior surface of the lipid nanoparticle.

4. The RNA delivery vehicle of claim 1, wherein the RNA-binding protein or peptide is a lipidated RNA-binding protein or peptide.

5. The RNA delivery vehicle of claim 1, wherein the RNA-binding protein or peptide: a) reduces toxicity of the lipid nanoparticle, and / or b) stabilizes the RNA, and / or c) protects the RNA from degradation, and / or d) facilitates nucleation of the lipid nanoparticle, and / or e) inhibits induction of signalling by one or more Toll-like Receptors.

6. The RNA delivery vehicle of claim 1, wherein the RNA-binding protein or peptide is modified to remove nuclear localisation signal(s) and / or introduce nuclear export signal(s).

7. The RNA delivery vehicle of claim 1 wherein the RNA-binding protein or peptide is a viral or non-viral RNA-binding protein or peptide.

8. The RNA delivery vehicle of claim 7, wherein the viral RNA-binding protein is from a class III, class IV, class V and / or class VI virus.

9. The RNA delivery vehicle of claim 8, wherein the viral RNA binding protein or peptide is a respiratory virus selected from the group consisting of an influenza virus, arespiratory syncytial virus, a parainfluenza virus, a metapneumovirus, a rhinovirus, a coronavirus, an adenovirus and a bocavirus.

10. The RNA delivery vehicle of claim 9, wherein the viral RNA-binding protein or peptide is a nucleoprotein, a non-structural protein, a matrix protein and / or a nucleocapsid protein.

11. The RNA delivery vehicle of claim 7, wherein the viral RNA-binding protein or peptide is a non-structural (NS) protein from an influenza B virus.

12. The RNA delivery vehicle of claim 7, wherein the viral RNA-binding protein or peptide comprises a sequence set forth in SEQ ID NOs: 9 to 11.

13. The RNA delivery vehicle of claim 7, wherein the non-viral RNA binding protein or peptide is derived from a cellular protein associated with cell growth, cell signalling and / or anti-viral pathways.

14. The RNA delivery vehicle of claim 13, wherein the cellular protein is selected from the group consisting of a TAR RNA-binding protein (TRBP), a protein kinase R (PKR) RNA-binding protein, a Toll-like Receptor 3 (TLR-3) binding protein, a TLR-7 binding protein and combinations thereof.

15. The RNA delivery vehicle of claim 13, wherein the cellular protein comprises a sequence set forth in SEQ ID NOs: 1 to 8.

16. The RNA delivery vehicle of claim 1, wherein the lipid nanoparticle comprises a PEG-lipid, a structural lipid, a neutral lipid and / or a cationic lipid.

17. The RNA delivery vehicle of claim 1, wherein the lipid nanoparticle does not comprise a cationic lipid.

18. The RNA delivery vehicle of claim 1, wherein the RNA is selected from the group consisting of messenger RNA (mRNA), small-interfering RNA (siRNA), microRNA (miRNA) and antisense RNA.

19. The RNA delivery vehicle of claim 18, wherein the mRNA is self-replicating mRNA (sa-mRNA) or a conventional RNA (cRNA).

20. An immunogenic composition comprising the RNA delivery vehicle of claim 1.

21. A pharmaceutical composition comprising the RNA delivery vehicle of claim 1 or the immunogenic composition of claim 20 and a pharmaceutically acceptable carrier.

22. The RNA delivery vehicle of claim 1, the immunogenic composition of claim 20, or the pharmaceutical composition of claim 21 for use in therapy.

23. A method of detecting unencapsulated and / or partially encapsulated RNA on the exterior surface of a lipid nanoparticle, the method comprising: (i) contacting a sample comprising a lipid nanoparticle to a RNA binding protein or peptide which binds to unencapsulated and / or partially encapsulated RNA on the exterior surface of the lipid nanoparticle to thereby form a complex; (ii) contacting the complex with a detection protein comprising an antibody variable region, wherein the detection protein binds to the RNA binding protein or peptide and wherein the detection protein comprises a detectable label; and (iii) detecting the detectable label, wherein presence of the detectable label is indicative of the presence of unencapsulated and / or partially encapsulated RNA on the exterior surface of the lipid nanoparticle in the sample.

24. The method of claim 23, wherein the detectable label is a magnetic label.

25. The method of claim 23, wherein the sample comprises the RNA delivery vehicle of claim 1.

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