SARS-cov-2 vaccines and therapeutics

Abstract

The present disclosure relates generally to receptor binding domain of SARS-CoV- 2 and nucleic acids encoding the receptor binding domain, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. Such a receptor binding domain can be included as one of the components or constituents of polypeptide or multisubunit peptide disclosed herein, including the nucleic acids encoding them.

Description

[0001]SARS-CoV-2 Vaccines and Therapeutics RELATED APPLICATIONS This application claims the benefit of priority to Indian Provisional Patent Application number IN202421064707, filed on August 27, 2024, the entire contents of which are hereby incorporated herein by reference in its entirety. REFERENCE TO A SEQUENCE LISTING XML This application contains a Sequence Listing which has been submitted electronically in XML format. The Sequence Listing XML is incorporated herein by reference. Said XML file, created on August 21, 2025, is named PVX-PAT-2421.xml and is 99,786 bytes in size. FIELD OF THE DISCLOSURE The present disclosure relates to nucleic acid sequences, receptor binding domain, polypeptides, multisubunit peptides, and polypeptide nanoparticle and their compositions for vaccine and therapeutic purpose against SARS-CoV-2. BACKGROUND COVID-19 is a viral infection caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2). Since its initial outbreak in 2019, SARS-CoV-2 has spread globally, resulting in several waves of infections, and causing significant health, economic, and social burden on most nations. The virus has shown remarkable capacity to evolve leading to emergence of variants with increased infectivity, including the ones with the ability to escape the currently available vaccines. SARS-CoV-2 continues to be one of the major threats that has potential to cause future pandemics or local community outbreaks that can cripple the healthcare system. Therefore, there is a need to develop vaccines that can offer protection against current as well as emerging variants of SARS-CoV-2. SUMMARY Accordingly, the present disclosure relates to a receptor binding domain comprising one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In another aspect, provided herein is a polypeptide comprising a receptor binding domain, a self-assembling peptide, and a linker peptide connecting the receptor binding domain and the self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In another aspect, provided herein is a nucleic acid encoding a receptor binding domain comprising one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In another aspect, provided herein is a nucleic acid encoding a polypeptide comprising a receptor binding domain, a self-assembling peptide, and a linker peptide connecting the receptor binding domain and the self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In another aspect, provided herein is a vaccine comprising a receptor binding domain, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In another aspect, provided herein is a vaccine comprising a polypeptide, wherein the polypeptide comprises a receptor binding domain, a self-assembling peptide, and a linker peptide connecting the receptor binding domain and the self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In another aspect, provided herein is a vaccine comprising a nucleic acid encoding a receptor binding domain, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In another aspect, provided herein is a vaccine comprising a nucleic acid encoding a polypeptide, wherein the polypeptide comprises a receptor binding domain, a self- assembling peptide, and a linker peptide connecting the receptor binding domain and the self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments the nucleic acid encodes a signal peptide on the amino- terminus of the receptor binding domain or the polypeptide. In some embodiments, the receptor binding domain, the linker peptide, and the self- assembling peptide are in N-terminus to C-terminus order. In another aspect, provided herein is a nucleic acid comprising a plurality of polynucleotide sequences, wherein some or all polynucleotide sequences of the plurality comprises either a receptor binding domain sequence, a linker sequence, and a self- assembling sequence or a linker sequence, a receptor binding domain sequence, a linker sequence and a self-assembling sequence or a combination thereof, wherein the receptor binding domain sequence comprises a mutation at: (a) a codon encoding an amino acid R at the position corresponding to the position 28 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid R with an amino acid T, (b) a codon encoding an amino acid K at the position corresponding to the position 38 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid V or T, (c) a codon encoding an amino acid K at the position corresponding to the position 126 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid T, (d) a codon encoding an amino acid F at the position corresponding to the position 138 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid F with an amino acid L, (e) a codon encoding an amino acid A at the position corresponding to the position 157 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid V, (f) a codon encoding an amino acid V at the position corresponding to the position 165 of the SEQ ID NO: 1, wherein the mutation is a deletion, (g) a codon encoding an amino acid E at the position corresponding to the position 166 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid E with an amino acid A, or K, or P, (h) a codon encoding an amino acid Q at the position corresponding to the position 175 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid Q with an amino acid E, (i) a codon encoding an amino acid S at the position corresponding to the position 176 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid S with an amino acid P, (j) a codon encoding an amino acid A at the position corresponding to the position 202 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid G, or a combination thereof. In another aspect, provided herein is a vaccine comprising a nucleic acid, wherein the nucleic acid comprises a plurality of polynucleotide sequences, wherein some or all polynucleotide sequences of the plurality comprises either a receptor binding domain sequence, a linker sequence, and a self-assembling sequence or a linker sequence, a receptor binding domain sequence, a linker sequence and a self-assembling sequence or a combination thereof, wherein the receptor binding domain sequence comprises a mutation at: (a) a codon encoding an amino acid R at the position corresponding to the position 28 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid R with an amino acid T, (b) a codon encoding an amino acid K at the position corresponding to the position 38 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid V or T, (c) a codon encoding an amino acid K at the position corresponding to the position 126 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid T, (d) a codon encoding an amino acid F at the position corresponding to the position 138 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid F with an amino acid L, (e) a codon encoding an amino acid A at the position corresponding to the position 157 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid V, (f) a codon encoding an amino acid V at the position corresponding to the position 165 of the SEQ ID NO: 1, wherein the mutation is a deletion, (g) a codon encoding an amino acid E at the position corresponding to the position 166 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid E with an amino acid A, or K, or P, (h) a codon encoding an amino acid Q at the position corresponding to the position 175 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid Q with an amino acid E, (i) a codon encoding an amino acid S at the position corresponding to the position 176 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid S with an amino acid P, (j) a codon encoding an amino acid A at the position corresponding to the position 202 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid G, or a combination thereof. In some embodiments, each polynucleotide sequence of the plurality is connected to an adjacent polynucleotide sequence of the plurality by a cleavage sequence. In some embodiments, the nucleic acid further comprises a signal sequence upstream of one or more of the polynucleotide sequences of the plurality. In some embodiments, the receptor binding domain sequence, the linker sequence, and the self-assembling sequence or the linker sequence, the receptor binding domain sequence, the linker sequence, and the self- assembling sequence are in 5′ to 3′ order. In another aspect, provided herein is a nucleic acid comprising a plurality of polynucleotide sequences, wherein each polynucleotide sequence of the plurality comprises a receptor binding domain sequence, a linker sequence, and a self-assembling sequence, wherein the receptor binding domain sequence comprises a mutation at: (a) a codon encoding an amino acid R at the position corresponding to the position 28 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid R with an amino acid T, (b) a codon encoding an amino acid K at the position corresponding to the position 38 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid V or T, (c) a codon encoding an amino acid K at the position corresponding to the position 126 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid T, (d) a codon encoding an amino acid F at the position corresponding to the position 138 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid F with an amino acid L, (e) a codon encoding an amino acid A at the position corresponding to the position 157 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid V, (f) a codon encoding an amino acid V at the position corresponding to the position 165 of the SEQ ID NO: 1, wherein the mutation is a deletion, (g) a codon encoding an amino acid E at the position corresponding to the position 166 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid E with an amino acid A, or K, or P, (h) a codon encoding an amino acid Q at the position corresponding to the position 175 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid Q with an amino acid E, (i) a codon encoding an amino acid S at the position corresponding to the position 176 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid S with an amino acid P, (j) a codon encoding an amino acid A at the position corresponding to the position 202 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid G, or a combination thereof. In another aspect, provided herein is a vaccine comprising a nucleic acid, wherein the nucleic acid comprises a plurality of polynucleotide sequences, wherein each polynucleotide sequence of the plurality comprises a receptor binding domain sequence, a linker sequence, and a self-assembling sequence, wherein the receptor binding domain sequence comprises a mutation at: (a) a codon encoding an amino acid R at the position corresponding to the position 28 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid R with an amino acid T, (b) a codon encoding an amino acid K at the position corresponding to the position 38 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid V or T, (c) a codon encoding an amino acid K at the position corresponding to the position 126 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid T, (d) a codon encoding an amino acid F at the position corresponding to the position 138 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid F with an amino acid L, (e) a codon encoding an amino acid A at the position corresponding to the position 157 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid V, (f) a codon encoding an amino acid V at the position corresponding to the position 165 of the SEQ ID NO: 1, wherein the mutation is a deletion, (g) a codon encoding an amino acid E at the position corresponding to the position 166 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid E with an amino acid A, or K, or P, (h) a codon encoding an amino acid Q at the position corresponding to the position 175 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid Q with an amino acid E, (i) a codon encoding an amino acid S at the position corresponding to the position 176 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid S with an amino acid P, (j) a codon encoding an amino acid A at the position corresponding to the position 202 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid G, or a combination thereof. In some embodiments, each polynucleotide sequence of the plurality is connected to an adjacent polynucleotide sequence of the plurality by a cleavage sequence. In some embodiments, the nucleic acid further comprises a signal sequence upstream of one or more of the polynucleotide sequences of the plurality. In some embodiments, the receptor binding domain sequence, the linker sequence, and the self-assembling sequence are in 5′ to 3′ order. In another aspect, provided herein is a nucleic acid comprising a plurality of polynucleotide sequences, wherein each polynucleotide sequence of the plurality comprises a linker sequence, a receptor binding domain sequence, a linker sequence, and a self- assembling sequence, wherein the receptor binding domain sequence comprises a mutation at: (a) a codon encoding an amino acid R at the position corresponding to the position 28 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid R with an amino acid T, (b) a codon encoding an amino acid K at the position corresponding to the position 38 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid V or T, (c) a codon encoding an amino acid K at the position corresponding to the position 126 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid T, (d) a codon encoding an amino acid F at the position corresponding to the position 138 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid F with an amino acid L, (e) a codon encoding an amino acid A at the position corresponding to the position 157 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid V, (f) a codon encoding an amino acid V at the position corresponding to the position 165 of the SEQ ID NO: 1, wherein the mutation is a deletion, (g) a codon encoding an amino acid E at the position corresponding to the position 166 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid E with an amino acid A, or K, or P, (h) a codon encoding an amino acid Q at the position corresponding to the position 175 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid Q with an amino acid E, (i) a codon encoding an amino acid S at the position corresponding to the position 176 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid S with an amino acid P, (j) a codon encoding an amino acid A at the position corresponding to the position 202 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid G, or a combination thereof. In another aspect, provided herein is a vaccine comprising a nucleic acid, wherein the nucleic acid comprises a plurality of polynucleotide sequences, wherein each polynucleotide sequence of the plurality comprises a linker sequence, a receptor binding domain sequence, a linker sequence, and a self-assembling sequence, wherein the receptor binding domain sequence comprises a mutation at: (a) a codon encoding an amino acid R at the position corresponding to the position 28 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid R with an amino acid T, (b) a codon encoding an amino acid K at the position corresponding to the position 38 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid V or T, (c) a codon encoding an amino acid K at the position corresponding to the position 126 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid T, (d) a codon encoding an amino acid F at the position corresponding to the position 138 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid F with an amino acid L, (e) a codon encoding an amino acid A at the position corresponding to the position 157 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid V, (f) a codon encoding an amino acid V at the position corresponding to the position 165 of the SEQ ID NO: 1, wherein the mutation is a deletion, (g) a codon encoding an amino acid E at the position corresponding to the position 166 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid E with an amino acid A, or K, or P, (h) a codon encoding an amino acid Q at the position corresponding to the position 175 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid Q with an amino acid E, (i) a codon encoding an amino acid S at the position corresponding to the position 176 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid S with an amino acid P, (j) a codon encoding an amino acid A at the position corresponding to the position 202 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid G, or a combination thereof. In some embodiments, each polynucleotide sequence of the plurality is connected to an adjacent polynucleotide sequence of the plurality by a cleavage sequence. In some embodiments, the nucleic acid further comprises a signal sequence upstream of one or more of the polynucleotide sequences of the plurality. In some embodiments, the linker sequence, the receptor binding domain sequence, the linker sequence, and the self-assembling sequence are in 5′ to 3′ order. In another aspect, provided herein is a nucleic acid encoding a multisubunit peptide comprising a plurality of polypeptides, wherein some or all polypeptides of the plurality comprises either a receptor binding domain, a linker peptide, and a self-assembling peptide or a linker peptide, a receptor binding domain, a linker peptide and a self-assembling peptide or a combination thereof, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In another aspect, provided herein is a vaccine comprising a nucleic acid encoding a multisubunit peptide, wherein the multisubunit peptide comprises a plurality of polypeptides, wherein some or all polypeptides of the plurality comprises either a receptor binding domain, a linker peptide, and a self-assembling peptide or a linker peptide, a receptor binding domain, a linker peptide and a self-assembling peptide or a combination thereof, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, each polypeptide of the plurality is connected to an adjacent polypeptide of the plurality by a cleavage peptide in a multisubunit peptide. In some embodiments, the nucleic acid further encodes a signal peptide on the amino-terminus of one or more of the polypeptides of the plurality in a multisubunit peptide. In some embodiments, the receptor binding domain, the linker peptide, and the self-assembling peptide or the linker peptide, the receptor binding domain, the linker peptide, and the self-assembling peptide are in N-terminus to C-terminus order. In another aspect, provided herein is a nucleic acid encoding a multisubunit peptide comprising a plurality of polypeptides, wherein each polypeptide of the plurality comprises a receptor binding domain, a linker peptide, and a self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In another aspect, provided herein is a vaccine comprising a nucleic acid encoding a multisubunit peptide, wherein the multisubunit peptide comprises a plurality of polypeptides, wherein each polypeptide of the plurality comprises a receptor binding domain, a linker peptide, and a self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, each polypeptide of the plurality is connected to an adjacent polypeptide of the plurality by a cleavage peptide in a multisubunit peptide. In some embodiments, the nucleic acid further encodes a signal peptide on the amino-terminus of one or more of the polypeptides of the plurality in a multisubunit peptide. In some embodiments, the receptor binding domain, the linker peptide, and the self-assembling peptide are in N- terminus to C-terminus order. In another aspect, provided herein is a nucleic acid encoding a multisubunit peptide comprising a plurality of polypeptides, wherein each polypeptide of the plurality comprises a linker peptide, a receptor binding domain, a linker peptide, and a self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In another aspect, provided herein is a vaccine comprising a nucleic acid encoding a multisubunit peptide, wherein the multisubunit peptide comprises a plurality of polypeptides, wherein each polypeptide of the plurality comprises a linker peptide, a receptor binding domain, a linker peptide, and a self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, each polypeptide of the plurality is connected to an adjacent polypeptide of the plurality by a cleavage peptide in a multisubunit peptide. In some embodiments, the nucleic acid further encodes a signal peptide on the amino-terminus of one or more of the polypeptides of the plurality in a multisubunit peptide. In some embodiments, the linker peptide, the receptor binding domain, the linker peptide, and the self-assembling peptide are in N-terminus to C-terminus order. In some embodiments, total number of the polynucleotide sequences are not more than 100. In some embodiments, total number of the polynucleotide sequences are between 2-5, 2-10, 10-20, 20-30, 30-40, 40-50, 50-60, 60-70, 70-80, 80-90, or 90-99. In some embodiments, the nucleic acid is a DNA or an RNA. In some embodiments, the RNA is an mRNA. In some embodiments, the mRNA is obtained or synthesized through a single IVT process or step. In some embodiments, the nucleic acid encodes a linker peptide, in addition to other peptides. In some embodiments, the linker sequence encodes a linker peptide. In some embodiments, the linker peptide is an amino acid linker, a foldon, a scaffold, or a combination thereof. In some embodiments, the linker peptide is an amino acid linker. In some embodiments, the linker peptide is a foldon. In some embodiments, the linker peptide is a scaffold. In some embodiments, the linker peptide comprises an amino acid linker and a foldon. In some embodiments, the linker peptide comprises an amino acid linker and a scaffold. In some embodiments, the linker peptide comprises a foldon and a scaffold. In some embodiments, the amino acid linker comprises 2 to 49 amino acids. In some embodiments, the amino acid linker is a glycine serine linker, a glycine proline linker, a glycine threonine linker, a alanine serine linker, any combination of two amino acids, or a combination thereof. In some embodiments, the linker peptide has an amino acid sequence of any one of SEQ ID NOs: 18-57. In some embodiments, the nucleic acid encodes a self-assembling peptide, in addition to other peptides. In some embodiments, the self-assembling sequence encodes a self- assembling peptide. In some embodiments, the self-assembling peptide is selected from the group comprising lumazine synthase, MS2 coat protein, hepatitis B surface antigen (HBsAg) from Hepatitis B Virus, hepatitis B core antigen (HBcAg) from Hepatitis B virus, human papillomavirus L1 (HPV L1) protein, matrix protein M1 from influenza A virus, ferritin, riboflavin synthase, a dihydrolipoyl acetyltransferase (E2p), or a combination thereof, including their codon optimized nucleic acid sequences, fragments, mutants, variants, comparable equivalents or functional analogs thereof. In some embodiments, the ferritin comprises ferritin subunit or ferritin peptide. In some embodiments, the ferritin peptide is obtained or derived from Listeria innocua or Helicobacter pylori ferritin. In some embodiments, the ferritin peptide is obtained or derived from Listeria innocua ferritin, or its fragment, mutant, variant, comparable equivalent, or functional analogs thereof. In some embodiments, the ferritin peptide is obtained or derived from Helicobacter pylori ferritin, or its fragment, mutant, variant, comparable equivalent, or functional analogs thereof. In some embodiments, the dihydrolipoyl acetyltransferase (E2p) is obtained or derived from Bacillus stearothermophilus or its fragment, mutant, variant, comparable equivalent, or functional analogs thereof. In some embodiments, the lumazine synthase is obtained or derived from Aquifex species (for example, Aquifex aeolicus) or Bacillus species (for example, Bacillus subtilis), or its fragment, mutant, variant, comparable equivalent, or functional analogs thereof. In some embodiments, the MS2 coat protein is obtained or derived from Emesvirus zinderi, or its fragment, mutant, variant, comparable equivalent, or functional analogs thereof. In some embodiments, the self-assembling peptide has an amino acid sequence of any one of SEQ ID NOs: 7-17 or 99-102. In some embodiments, the nucleic acid encodes a cleavage peptide, in addition to other peptides. In some embodiments, the nucleic acid encodes one or more cleavage peptides, in addition to other peptides. In some embodiments, the cleavage sequence encodes one or more cleavage peptides, for example, cleavage peptide-1, cleavage peptide-2, and so on. In some embodiments, the one or more cleavage peptides are optionally connected to each other by a linker peptide. In some embodiments, the cleavage peptide is a golgi specific cleavage peptide or self-cleaving peptide. In some embodiments, the cleavage peptide has an amino acid sequence of any one of SEQ ID NOs: 58-73. In some embodiments, the nucleic acid encodes a signal peptide, in addition to other peptides. In some embodiments, the nucleic acid encodes one or more signal peptide, in addition to other peptides. In some embodiments, the signal sequence encodes a signal peptide. In some embodiments, one or more signal peptide is present on the amino-terminus of the receptor binding domain. In some embodiments, one or more signal peptide is present on the amino-terminus of the polypeptide. In some embodiments, the signal peptide is present on the amino terminus of one or more of the polypeptides in a multisubunit peptide. In some embodiments, the signal peptide is present on the amino terminus of all or some of the polypeptides in a multisubunit peptide. In some embodiments, the signal peptide is present on the amino-terminus of the first polypeptide in a multisubunit peptide. In some embodiments, the nucleic acid encodes a second signal peptide on the amino-terminus of the receptor binding domain. In some embodiments, the nucleic acid encodes a second signal peptide on the amino-terminus of the polypeptide. In some embodiments, the nucleic acid encodes a second signal peptide on the amino-terminus of one or more of the polypeptides in a multisubunit peptide. In some embodiments, the nucleic acid further encodes a second signal peptide on the amino-terminus of all or some polypeptides in a multisubunit peptide. In some embodiments, the signal peptide has an amino acid sequence of any one of SEQ ID NOs: 74-93. In some embodiments, the receptor binding domain sequence encodes a receptor binding domain wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, the receptor binding domain is encoded by a codon optimized nucleic acid sequence, or fragments, mutants, variants, comparable equivalents, or functional analogs thereof. In some embodiments, the receptor binding domain is obtained or derived from SARS-CoV-2 or any of its strains, variants, or subvariants, with one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof. In some embodiments, the receptor binding domain has an amino acid sequence of any one of SEQ ID NOs: 2-6, including its codon optimized nucleic acid sequence, or fragments, mutants, variants, comparable equivalents, or functional analogs thereof. In some embodiments, the receptor binding domain has an amino acid sequence of any one of SEQ ID NOs: 2-6. In another aspect, provided herein is a lipid nanoparticle composition comprising a cationic lipid, a phospholipid, a sterol, a PEG-lipid, and the nucleic acid according to any one of the preceding embodiments or paragraphs. In some embodiments, the cationic lipid comprises an ionizable lipid. In some embodiments, the cationic lipid is present in an amount from 10 mol percent to 70 mol percent. In some embodiments, the phospholipid is present in an amount from 2 mol percent to 65 mol percent. In some embodiments, the sterol is present in an amount from 20 mol percent to 65 mol percent. In some embodiments, the PEG-lipid is present in an amount from 0.2 mol percent to 2.0 mol percent. In some embodiments, the lipid nanoparticle composition additionally comprises an ionizable polymer. In some embodiments, the ionizable polymer is present in an amount from 1 mol percent to 25 mol percent. In some embodiments, the ionizable polymer is selected from the group comprising a chitosan, chitosan derivatives, a cellulose derivative, a poly-L-lysine (PLL), protamine, polyethyleneimine, and / or their derivatives or a combination thereof. In some embodiments, the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), or SM- 102, or ALC-0315, or a combination thereof. In another aspect, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof the nucleic acid disclosed herein. In another aspect, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof the receptor binding domain disclosed herein. In another aspect, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof the polypeptide as disclosed herein. In another aspect, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof the multisubunit peptide disclosed herein. In another aspect, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof the lipid nanoparticle composition disclosed herein. In another aspect, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof, the vaccine comprising the nucleic acid disclosed herein. In another aspect, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof, the vaccine comprising the receptor binding domain disclosed herein. In another aspect, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof, the vaccine comprising the polypeptide as disclosed herein. In another aspect, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof, the vaccine comprising the multisubunit peptide disclosed herein. In another aspect, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof, the vaccine comprising the lipid nanoparticle composition disclosed herein. In another aspect, provided herein is use of the nucleic acid disclosed herein, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. In another aspect, provided herein is use of the receptor binding domain disclosed herein, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. In another aspect, provided herein is use of the polypeptide disclosed herein, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. In another aspect, provided herein is use of the multisubunit peptide disclosed herein, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. In another aspect, provided herein is use of the lipid nanoparticle composition disclosed herein, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. In another aspect, provided herein is use of the vaccine comprising the nucleic acid disclosed herein, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. In another aspect, provided herein is use of the vaccine comprising the receptor binding domain disclosed herein, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. In another aspect, provided herein is use of the vaccine comprising the polypeptide disclosed herein, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. In another aspect, provided herein is use of the vaccine comprising the multisubunit peptide disclosed herein, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. In another aspect, provided herein is use of the vaccine comprising the lipid nanoparticle composition disclosed herein, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. In another aspect, provided herein is a receptor binding domain encoded by the nucleic acid disclosed herein. In another aspect, provided herein is a polypeptide encoded by the nucleic acid disclosed herein. In another aspect, provided herein is a multisubunit peptide encoded by the nucleic acid disclosed herein. In another aspect, provided herein is a polypeptide comprising a receptor binding domain, a self-assembling peptide, and a linker peptide connecting the receptor binding domain with the self-assembling peptide. In another aspect, provided herein is a multisubunit peptide comprising two or more polypeptides, wherein some or all polypeptides comprises either a receptor binding domain, a linker peptide, and a self-assembling peptide, or a linker peptide, a receptor binding domain, a linker peptide, and a self-assembling peptide, or a combination thereof, wherein one polypeptide is connected to another polypeptide by a cleavage peptide, wherein the multisubunit peptide includes a signal peptide upstream (amino-terminus) of one or more of the polypeptides, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, the signal peptide is present on the amino-terminus of the first polypeptide. In some embodiments, the signal peptide is present on the amino-terminus of some or each of the polypeptides. In another aspect, provided herein is a polypeptide nanoparticle comprising at least 2 or up to 500 polypeptides disclosed herein. In some embodiments, the polypeptides are homologous polypeptides, heterologous polypeptides, oligomeric complexes, or a combination thereof. In some embodiments, the polypeptide nanoparticle is icosahedral, helical, spherical, rod-like or a combination thereof. In another aspect, provided herein is a nucleic acid sequence comprising two or more polynucleotide sequences, wherein some or all polynucleotide sequences comprises either a receptor binding domain sequence, a linker sequence, and a self-assembling sequence, or a linker sequence, a receptor binding domain sequence, a linker sequence, and a self- assembling sequence, or a combination thereof, wherein one polynucleotide sequence is connected to another polynucleotide sequence by a cleavage sequence, wherein the nucleic acid sequence includes a signal sequence upstream of one or more of the polynucleotide sequences, wherein the receptor binding domain sequence comprises a mutation at: (a) a codon encoding an amino acid R at the position corresponding to the position 28 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid R with an amino acid T, (b) a codon encoding an amino acid K at the position corresponding to the position 38 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid V or T, (c) a codon encoding an amino acid K at the position corresponding to the position 126 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid T, (d) a codon encoding an amino acid F at the position corresponding to the position 138 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid F with an amino acid (e) a codon encoding an amino acid A at the position corresponding to the position 157 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid V, (f) a codon encoding an amino acid V at the position corresponding to the position 165 of the SEQ ID NO: 1, wherein the mutation is a deletion, (g) a codon encoding an amino acid E at the position corresponding to the position 166 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid E with an amino acid A, or K, or P, (h) a codon encoding an amino acid Q at the position corresponding to the position 175 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid Q with an amino acid E, (i) a codon encoding an amino acid S at the position corresponding to the position 176 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid S with an amino acid P, (j) a codon encoding an amino acid A at the position corresponding to the position 202 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid G, or a combination thereof. In some embodiments, the linker sequence connects the signal sequence with the first polynucleotide sequence. In some embodiments, the signal sequence is present upstream of all or some of the polynucleotide sequences. In some embodiments, the signal sequence is present upstream of the first polynucleotide sequence. In some embodiments, the signal sequence is present upstream of all polynucleotide sequences. In some embodiments, the linker sequence connects the receptor binding domain sequence with the self-assembling sequence in a polynucleotide sequence. In some embodiments, one linker sequence connects the cleavage sequence with the receptor binding domain sequence and another linker sequence connects the receptor binding domain sequence with the self-assembling sequence in a polynucleotide sequence. In some embodiments, the nucleic acid sequence is a DNA or an RNA. In some embodiments, the nucleic acid sequence is an mRNA. In some embodiments, the nucleic acid sequence encodes a receptor binding domain as disclosed herein. In some embodiments, the nucleic acid sequence encodes a polypeptide. In some embodiments, the nucleic acid sequence encodes a multisubunit peptide. In some embodiments, the nucleic acid is encapsulated or formulated in a lipid nanoparticle composition. In some embodiments, the nucleic acid sequence is obtained or synthesized through one or more in vitro transcription (IVT) process. In some embodiments, the nucleic acid sequence (for example, mRNA) is synthesized or obtained through a single in vitro transcription (IVT) process or step. In some embodiments, the disclosure relates to a nucleic acid sequence encoding a receptor binding domain, polypeptide, or multisubunit peptide as disclosed herein. In some embodiments, the disclosure relates to a vaccine comprising a nucleic acid sequence encoding the receptor binding domain, polypeptide, or multisubunit peptide as disclosed herein. In some embodiments, the disclosure also relates to a nucleic acid sequence encoding a multisubunit peptide, wherein the multisubunit peptide comprises two or more polypeptides, wherein some or all polypeptides comprises either a receptor binding domain, a linker peptide, and a self-assembling peptide or a linker peptide, a receptor binding domain, a linker peptide, and a self-assembling peptide, or a combination thereof, wherein one polypeptide is connected to another polypeptide by a cleavage peptide, wherein the multisubunit peptide includes a signal peptide upstream (amino-terminus) of one or more of the polypeptides, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, a signal peptide is present upstream (amino-terminus) of all or some of the polypeptides in a multisubunit peptide. In some embodiments, a signal peptide is present upstream (amino-terminus) of the first polypeptide in a multisubunit peptide. In some embodiments, a signal peptide is present upstream (amino-terminus) of all the polypeptides in a multisubunit peptide. In some embodiments, the disclosure also relates to a vaccine comprising a nucleic acid sequence encoding a multisubunit peptide, wherein the multisubunit peptide comprises two or more polypeptides, wherein some or all polypeptides comprises either a receptor binding domain, a linker peptide, and a self-assembling peptide or a linker peptide, a receptor binding domain, a linker peptide, and a self-assembling peptide, or a combination thereof, wherein one polypeptide is connected to another polypeptide by a cleavage peptide, wherein the multisubunit peptide includes a signal peptide upstream (amino-terminus) of one or more of the polypeptides, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, a signal peptide is present upstream (amino-terminus) of all or some of the polypeptides in a multisubunit peptide. In some embodiments, a signal peptide is present upstream (amino-terminus) of the first polypeptide in a multisubunit peptide. In some embodiments, a signal peptide is present upstream (amino-terminus) of all the polypeptides in a multisubunit peptide. In some embodiments, the disclosure also relates to a multisubunit peptide comprising two or more polypeptides, wherein some or all polypeptides comprises either a receptor binding domain, a linker peptide, and a self-assembling peptide or a linker peptide, a receptor binding domain, a linker peptide, and a self-assembling peptide, or a combination thereof, wherein one polypeptide is connected to another polypeptide by a cleavage peptide, wherein the multisubunit peptide includes a signal peptide upstream (amino-terminus) of one or more of the polypeptides, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, a signal peptide is present upstream (amino-terminus) of all or some of the polypeptides in a multisubunit peptide. In some embodiments, a signal peptide is present upstream (amino-terminus) of the first polypeptide in a multisubunit peptide. In some embodiments, a signal peptide is present upstream (amino-terminus) of all the polypeptides in a multisubunit peptide. In some embodiments, the disclosure also relates to a vaccine comprising a multisubunit peptide, wherein the multisubunit peptide comprises two or more polypeptides, wherein some or all polypeptides comprises either a receptor binding domain, a linker peptide, and a self-assembling peptide or a linker peptide, a receptor binding domain, a linker peptide, and a self-assembling peptide, or a combination thereof, wherein one polypeptide is connected to another polypeptide by a cleavage peptide, wherein the multisubunit peptide includes a signal peptide upstream (amino-terminus) of one or more of the polypeptides, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, a signal peptide is present upstream (amino-terminus) of all or some of the polypeptides in a multisubunit peptide. In some embodiments, a signal peptide is present upstream (amino-terminus) of the first polypeptide in a multisubunit peptide. In some embodiments, a signal peptide is present upstream (amino-terminus) of all the polypeptides in a multisubunit peptide. In some embodiments, the linker peptide connects the receptor binding domain with the self-assembling peptide. In some embodiments, the linker peptide connects the signal peptide with the first polypeptide in a multisubunit peptide. In some embodiments, the linker peptide connects the receptor binding domain with the self-assembling peptide in a polypeptide. In some embodiments, one linker peptide connects the cleavage peptide with the receptor binding domain and another linker peptide connects the receptor binding domain with the self-assembling peptide of a polypeptide in the multisubunit peptide. In some embodiments, the multisubunit peptide comprise homologous polypeptides. In some other embodiments, the multisubunit peptide comprise heterologous polypeptides. In some embodiments, multisubunit peptide comprise homologous polypeptides, heterologous polypeptides, or a combination thereof. In some embodiments, the disclosure relates to a polypeptide nanoparticle comprising one or more homologous polypeptides, one or more heterologous polypeptides, one or more oligomeric complex, or a combination thereof. In some embodiments, the homologous polypeptides, heterologous polypeptides, or oligomeric complexes comprise either a receptor binding domain, a linker peptide, and a self-assembling peptide, or a linker peptide, a receptor binding domain, a linker peptide, and a self-assembling peptide, or a combination thereof, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, the polypeptides may have some residues (amino acids) of the cleavage peptide. In some embodiments, the polypeptides in a polypeptide nanoparticle may also have some residues (amino acids) of cleavage peptide. In some embodiments, the disclosure relates to a polypeptide nanoparticle formed from the self-assembly of two or more polypeptides, wherein some or all polypeptides comprises either a receptor binding domain, a linker peptide, and a self-assembling peptide, or a linker peptide, a receptor binding domain, a linker peptide, and a self-assembling peptide or a combination thereof, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, the disclosure relates to a polypeptide nanoparticle formed from the self-assembly of two or more polypeptides, wherein the polypeptide comprises a receptor binding domain, a self-assembling peptide, and a linker peptide connecting the receptor binding domain with the self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, the polypeptides in the polypeptide nanoparticle may also have some residues (amino acids) of cleavage peptide. In some embodiments, the polypeptide nanoparticle comprises of homologous polypeptides, heterologous polypeptides, oligomeric complexes, or a combination thereof. In some aspects, provided herein is a nucleic acid sequence disclosed herein, encapsulated or formulated in a lipid nanoparticle composition. In some aspects, the lipid nanoparticle composition comprises a cationic lipid, a phospholipid, a sterol, a PEG lipid and the nucleic acid sequence as described herein. In some embodiments, the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315, or a combination thereof. In some aspects, provided herein is a vaccine comprising the nucleic acid sequence disclosed herein, encapsulated or formulated in a lipid nanoparticle composition. In some aspects, the lipid nanoparticle composition comprises a cationic lipid, a phospholipid, a sterol, a PEG lipid and the nucleic acid sequence as disclosed herein. In some embodiments, the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315, or a combination thereof. In some other aspects, the lipid nanoparticle composition comprises an ionizable polymer, a cationic lipid, a phospholipid, a sterol, a PEG-lipid and the nucleic acid sequence as disclosed herein. In some embodiments, the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315, or a combination thereof. In some aspects, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof the nucleic acid sequence as disclosed herein. In some aspects, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof a vaccine comprising the nucleic acid sequence as disclosed herein. In some aspects, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof the lipid nanoparticle composition comprising a cationic lipid, a phospholipid, a sterol, a PEG-lipid and the nucleic acid sequence as disclosed herein. In some embodiments, the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315, or a combination thereof. In some aspects, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof the lipid nanoparticle composition comprising an ionizable polymer, a cationic lipid, a phospholipid, a sterol, a PEG-lipid and the nucleic acid sequence as disclosed herein. In some embodiments, the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315, or a combination thereof. In some aspects, the disclosure relates to use of a lipid nanoparticle composition comprising a cationic lipid, a phospholipid, a sterol, a PEG-lipid, and the nucleic acid sequence as disclosed herein in the manufacture of a medicament for the treatment or prevention of a disease in a subject. In some embodiments, the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315, or a combination thereof. In some aspects, the disclosure relates to use of a vaccine comprising a lipid nanoparticle composition, wherein the lipid nanoparticle composition comprises a cationic lipid, a phospholipid, a sterol, a PEG-lipid, and the nucleic acid sequence as disclosed herein, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. In some embodiments, the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315, or a combination thereof. In some embodiments, the receptor binding domain is obtained or derived from SARS-CoV-2 or any of its strains, variants, or subvariants. In some embodiments, the receptor binding domain comprises one or mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof. In some embodiments, the receptor binding domain sequence includes codon optimized sequences, fragments, variants, mutants, comparable equivalents, or functional analogs thereof. In some embodiments, the receptor binding domain sequence encodes a receptor binding domain. In some embodiments, the receptor binding domain sequence or receptor binding domain is modified or unmodified. In some embodiments, the receptor binding domain sequence is modified or unmodified. In some embodiments, the receptor binding domain is modified or unmodified. In some embodiments, the receptor binding domain may have immunostimulatory or immunomodulatory effect. In some embodiments, the nucleic acid includes a self-assembling sequence. In some embodiments, the nucleic acid encodes a self-assembling peptide, in addition to other peptides, as applicable. In some embodiments, the self-assembling sequence encodes a self- assembling peptide. In some embodiments, the self-assembling peptide includes, but not limited to, lumazine synthase, MS2 coat protein, hepatitis B surface antigen (HBsAg) from Hepatitis B Virus, hepatitis B core antigen (HBcAg) from hepatitis B virus, human papillomavirus L1 (HPV L1) protein, matrix protein M1 from influenza A virus, ferritin peptide, riboflavin synthase, a dihydrolipoyl acetyltransferase (E2p), or a combination thereof, including their fragments, mutants, variants, comparable equivalents, or functional analogs thereof. In some embodiments, the ferritin peptide is obtained or derived from Listeria innocua or Helicobacter pylori. In some embodiments, the ferritin peptide is a Listeria innocua ferritin, or its fragment, mutant, variant, comparable equivalent, or functional analogs thereof. In some embodiments, the ferritin peptide is a Helicobacter pylori ferritin or its fragment, mutant, variant, comparable equivalent, or functional analog thereof. In some embodiments, the dihydrolipoyl acetyltransferase (E2p) is obtained or derived from Bacillus stearothermophilus, or its fragment, mutant, variant, comparable equivalent, or functional analogs thereof. In some embodiments, the lumazine synthase is obtained or derived from Aquifex species (for example, Aquifex aeolicus) or Bacillus species (for example, Bacillus subtilis), or its fragment, mutant, variant, comparable equivalent, or functional analogs thereof. In some embodiments, the MS2 coat protein is obtained or derived from Emesvirus zinderi, or its fragment, mutant, variant, comparable equivalent, or functional analogs thereof. In some embodiments, the nucleic acid includes a linker sequence. In some embodiments, the nucleic acid encodes a linker peptide, in addition to other peptides, as applicable. In some embodiments, the linker sequence encodes a linker peptide. In some embodiments, the linker peptide connects the receptor binding domain with the self- assembling peptide. In some embodiments, the linker peptide connects the receptor binding domain with the self-assembling peptide in a polypeptide. In some embodiments, the linker peptide connects the signal peptide with the first polypeptide in a multisubunit peptide. In some embodiments, one linker peptide connects the cleavage peptide with the receptor binding domain and another linker peptide connects the receptor binding domain with the self-assembling peptide of a polypeptide in a multisubunit peptide. The linker peptide is an amino acid linker, a foldon, a scaffold or a combination thereof. In some embodiments, the nucleic acid includes a cleavage sequence. In some embodiments, the nucleic acid encodes a cleavage peptide, in addition to other peptides, as applicable. In some embodiments, the nucleic acid encodes a cleavage peptide in a multisubunit peptide, in addition to the other peptides. In some embodiments, the cleavage sequence encodes a cleavage peptide. The cleavage peptide connects one polypeptide with another polypeptide, for example, adjacent polypeptide in a multisubunit peptide. The cleavage peptide carries a cleavage site. In some embodiments, the cleavage peptide facilitates the action of cellular proteases to cleave the multisubunit peptide into individual polypeptides. In some embodiments, the cleavage peptide self cleaves (for example, without bond formation during translation of nucleic acid) the multisubunit peptide into individual polypeptides. In some embodiments, the cleavage peptide comprises two or more cleavage peptides (for example, cleavage peptide-1, cleavage peptide-2 and so on), optionally connected via a linker, wherein one cleavage peptide is a substrate for cellular proteases and the other cleavage peptide is a self cleaving peptide. In some embodiments, the cleavage peptide self cleaves into individual polypeptides or cleaved by the action of cellular proteases. In some embodiments, the cleavage peptide is a substrate for golgi specific proteases. In some embodiments, remnants of cleavage peptide are present in a polypeptide. In some embodiments, the nucleic acid includes a signal sequence. In some embodiments, the nucleic acid encodes a signal peptide, in addition to other peptides, as applicable. In some embodiments, the signal sequence encodes a signal peptide. In some embodiments, the signal peptide is present upstream (amino-terminus) of the receptor binding domain. In some embodiments, the signal peptide is present upstream (amino- terminus) of the polypeptide. In some embodiments, the signal peptide is present upstream (amino-terminus) of one or more polypeptides in a multisubunit peptide. In some embodiments, the signal peptide is present upstream (amino-terminus) of the first polypeptide in a multisubunit peptide. In some embodiments, the signal peptide is present upstream (amino-terminus) of some polypeptides in a multisubunit peptide. In some embodiments, the signal peptide is present upstream (amino-terminus) of all polypeptides in a multisubunit peptide. In some embodiments, the signal peptide transports the multisubunit peptide to cell organelles. In some embodiments, the signal peptide transports the multisubunit peptide to golgi body or golgi apparatus via endoplasmic reticulum. In some embodiments, the signal peptide is a golgi targeting signal peptide. In some aspects, the present disclosure also includes a method of transforming a cell with the nucleic acid sequence disclosed herein. In some aspects, the present disclosure also includes a vector comprising a nucleic acid sequence disclosed herein. BRIEF DESCRIPTION OF THE DRAWINGS Figure 1 – shows representative schematic illustration of nucleic acid expressing or encoding either receptor binding protein (RBD), polypeptide, or multisubunit peptide. The polypeptide comprises a receptor binding domain (RBD), a self-assembling peptide (SAP), and a linker peptide (LP) connecting the RBD and the SAP. The RBD, LP, and SAP are in N-terminus to C-terminus order. The polypeptide additionally have one or more signal peptide on the N-terminus. The multisubunit peptide comprises plurality of polypeptides (PP) separated by cleavage peptide (CP), wherein each polypeptide (PP) comprises either a receptor binding domain (RBD), a linker peptide (LP), and a self-assembling peptide (SAP) or a linker peptide (LP), a receptor binding domain (RBD), a linker peptide (LP), and a self- assembling peptide (SAP), or a combination thereof. Multiple polypeptides are connected through a cleavage peptide (CP) such that between any two polypeptides there is present a cleavage peptide in a multisubunit peptide. The multisubunit peptide additionally have one or more signal peptide (SP) on one or more of the polypeptides. In a polypeptide the RBD, the LP and the SAP or the LP, the RBD, the LP and the SAP are in N-terminus to C-terminus order in a multisubunit peptide. The letter ‘n’ represents any number between 1 to 98. The receptor binding protein expressed or encoded by the nucleic acid, either alone or as one of the components or constituents of polypeptide or multisubunit peptide, comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. Figure 2 – shows a western blot of cell lysate (lane 3) showing expression of nucleic acid sequence of example 1 encoding the polypeptide of SEQ ID NO: 94 using polyclonal anti-spike RBD antibody against SARS-CoV-2. Lanes 1 and 2 are protein ladder and negative control respectively. Figure 3 – shows a western blot of cell lysate (lane 3) showing expression of nucleic acid sequence of example 2 encoding the polypeptide of SEQ ID NO: 95 using polyclonal anti-spike RBD antibody against SARS-CoV-2. Lanes 1 and 2 are protein ladder and negative control respectively. Figure 4 – shows a western blot of cell lysate (lane 3) showing expression of nucleic acid sequence of example 4 encoding the polypeptide of SEQ ID NO: 97 using polyclonal anti-spike RBD antibody against SARS-CoV-2. Lanes 1 and 2 are protein ladder and negative control respectively. Figure 5 – shows a western blot of cell lysate (lane 3) showing expression of nucleic acid sequence of example 5 encoding the polypeptide of SEQ ID NO: 98 using polyclonal anti-spike RBD antibody against SARS-CoV-2. Lanes 1 and 2 are protein ladder and negative control respectively. Figures 6a and 6b – shows neutralization of different pseudoviruses by the antibodies generated against the polypeptide of SEQ ID NO: 94 encoded by the nucleic acid sequence of example 1. Figures 7a and 7b – shows neutralization of different pseudoviruses by the antibodies generated against the polypeptide of SEQ ID NO: 95 encoded by the nucleic acid sequence of example 2. Figure 8 – shows neutralization of different pseudoviruses by the antibodies generated against the polypeptide of SEQ ID NO: 96 encoded by the nucleic acid sequence of example 3. Figures 9a. 9b, and 9c – shows neutralization of different pseudoviruses by the antibodies generated against the polypeptide of SEQ ID NO: 98 encoded by the nucleic acid sequence of example 5. Figure 10 – shows a western blot of cell lysate (lane 2) showing expression of nucleic acid sequence of example 7 encoding the polypeptide of SEQ ID NO: 103 using polyclonal anti-spike RBD antibody against SARS-CoV-2. Lanes 1 and 3 are protein ladder and negative control respectively. Figure 11 – shows neutralization of different pseudoviruses by the antibodies generated against the polypeptide of SEQ ID NO: 103 encoded by the nucleic acid sequence of example 7. DETAILED DESCRIPTION Unless defined otherwise, technical, and scientific terms used herein have the same meaning as commonly understood by one of person skill in the art. Some of the terms are defined briefly here below; the definitions should not be construed in a limiting sense. The singular forms “a”, “an” and “the” as used in the specification also include plural aspects unless the context dictates otherwise. Similarly, any singular term used in the specification also mean plural or vice versa unless the context dictates otherwise. As used herein in the claim(s), when used in conjunction with the word “comprising”, the words “a” or “an” may mean one or more than one. As used herein “another” may mean at least a second or more. It must be noted that the words “comprising” or any of its form such as “comprise” or “comprises”, “having” or any of its forms such as “have” or “has”, “including” or any of its forms such as “include” or “includes”, or “containing” or any of its forms such as “contain” or “contains” are open-ended and do not exclude additional unrecited elements or method steps. Wherever any quantity or range is stated one skilled in the art will recognize that quantity or range within 10 or 20 percent of the stated values can also be expected to be appropriate and reasonable and included within the scope of the invention. Unless otherwise defined herein, scientific, and technical terms used in connection with the present invention shall have the meanings that are commonly understood by those of ordinary skilled in the art. Generally, nomenclatures used in connection with, and techniques of, cell and tissue culture, molecular biology, immunology, microbiology, protein, adjuvant, pharmaceutical biotechnology, and biopharmaceutical manufacturing described herein are those well known and commonly used in the art. The methods and techniques of the present invention are generally performed according to conventional methods well known in the art and as described in various general and more specific references that are cited and discussed throughout the present specification. The term “composition”, “formulation”, “lipid nanoparticle composition”, or “lipid nanoparticle” has been used interchangeably to mean a nanoparticle, nanostructure, vesicle, liposome, composition or formulation comprising one or more lipid components (for example, a cationic lipid, a phospholipid, a sterol, and a PEG-lipid), and / or an ionizable polymer component. In some embodiments, the lipid nanoparticle comprises a cationic lipid, a phospholipid, a sterol, a PEG-lipid, and a nucleic acid. In some embodiments, the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315, or a combination thereof. In some embodiments, the lipid nanoparticle comprises one or more lipid components, an ionizable polymer component, and a nucleic acid. In some embodiments, the nucleic acid associated with the lipid nanoparticle is a DNA, an mRNA, a micro RNA, a small interfering RNA, a small nucleolar RNA, a small nuclear RNA, a long non-coding RNA or a combination thereof. In some embodiments, the lipid nanoparticle composition contains one or more pharmaceutical carriers or excipients, such as but not limited to, buffering agents, stabilizers, tonicity modifiers, surfactants, chelating agents, salts, anti-oxidants, diluents, and / or preservatives, or a combination thereof. The term lipid nanoparticle also denotes lipid nanoparticles that are devoid of any encapsulated nucleic acid (empty lipid nanoparticles or ghost lipid nanoparticles). In some embodiments, the lipid nanoparticle composition comprises lipid nanoparticles with encapsulated nucleic acid as well as empty lipid nanoparticles. In some embodiments, the composition or formulation includes receptor binding domain or polypeptide or polypeptide nanoparticles along with pharmaceutically acceptable carriers or excipients, such as but not limited, to buffering agents, stabilizers, tonicity modifiers, surfactants, chelating agents, salts, anti-oxidants, diluents, and / or preservative, or a combination thereof. The term “therapeutic”, “therapeutic agent”, “prophylactic”, “prophylactic agent”, or “drug” has been used interchangeably to mean a compound (such as nucleic acid sequence, polypeptide, receptor binding domain, multisubunit peptide) or composition having a biological effect or a combination of biological effects that prevents, inhibits, eliminates or prevents the progression of a disease or other aberrant biological processes in a subject, for example, an animal or human. The term “preventing” is art-recognized, and when used in relation to a condition, such as an infection is well understood in the art, and includes administration of a composition, which reduces the frequency or severity, or delays the onset, of one or more symptoms of the medical condition in a subject relative to a subject who does not receive the composition. Thus, the prevention of a condition, such as an infection, includes, for example, the reduction of the frequency or severity of one or more symptoms of the medical condition in a population of patients receiving a therapy relative to a control population that did not receive the therapy, e.g., by a statistically and / or clinically significant amount. Similarly, the prevention of an infection includes reducing the likelihood that a patient receiving a therapy will develop the infection or related symptoms, relative to a patient who does not receive the therapy. The term “molar percent”, “mol percent”, “molar %”, or “mol %” have been used interchangeably to mean number of moles of a component expressed as percentage relative to total moles of all lipid components present in the lipid nanoparticle compositions described herein. For example, 50 mol % cationic lipid means, 50 mol % of cationic lipid is present in the lipid nanoparticle composition and other lipid components together constitute remaining 50 mol % such that the total amount of all the lipid components constitute 100 mol %. In some embodiments, mol % also denotes to mean number of moles of a component expressed as percentage relative to total moles of all lipid components (such as cationic lipid, phospholipid, sterol and PEG-lipid) and ionizable polymer component(s) present in the lipid nanoparticle composition described herein. For example, 50 mol % of cationic lipid means, 50 mol % of cationic lipid is present in the lipid nanoparticle composition and other lipids components and ionizable polymer components together constitute the remaining 50 mol % such that the total amount of all the lipid components and ionizable polymer components constitute 100 mol %. The term “N / P ratio”, “N:P ratio”, “lipid to nucleic acid ratio”, or “cationic lipid to nucleic acid ratio” have been used interchangeably herein and means the ratio (molar ratio) of the positive charges in the cationic lipid relative to the negative charges in the nucleic acid (such as the nucleic acid sequence disclosed herein) in a lipid nanoparticle. In some embodiments, the N / P ratio refers to the ratio of protonable nitrogen present in the cationic lipid relative to the phosphate present in the nucleic acid in a lipid nanoparticle. In some embodiments, the N / P ratio is between 1 to 18 (i.e., 1:1 to 18:1). For example, a N / P ratio of 18 refers to the presence of 18 protonable nitrogen of the cationic lipid relative to 1 phosphate of the nucleic acid in a lipid nanoparticle. The terms “antibody” and “antibodies” have been used interchangeably herein and means any antibody or antibody fragment (whether produced naturally or recombinantly) which retains antigen binding activity. This includes a monoclonal or polyclonal antibody, a single chain antibody, a Fab fragment of a monoclonal or polyclonal antibody, a chimeric antibody, a humanized antibody, a human antibody, a bispecific antibody, a multispecific antibody, or a nanobody. The term “buffer” as used herein means those agents that maintains the pH of a solution in a desired range. The term “cell” as used herein means a single cell or a population of cells or plurality of cells. The term “biologically effective amount” or “therapeutically effective amount” as used herein means an amount of an agent, for example, a therapeutic, drug, therapeutic agent, prophylactic agent, diagnostic agent, composition, etc., that is sufficient, when administered to a subject suffering from or susceptible to an infection, disease, disorder, and / or condition, to treat, prevent, diagnose, improve symptoms of, and / or delay the onset of the infection, disease, disorder, and / or condition. A therapeutically effective amount herein may vary according to factors such as the disease state, age, sex, and weight of the patient. As used herein, the term “treating” or “treatment” includes reducing, arresting, or reversing the symptoms, clinical signs, or underlying pathology of a condition to stabilize or improve a subject's condition or to reduce the likelihood that the subject’s condition will worsen as much as if the subject did not receive the treatment. Treatment may be administered to a subject who does not exhibit signs of a disease and / or exhibits only early signs of the disease for the purpose of decreasing the risk of developing pathology associated with the disease. The term “subject” as used herein refers to an animal or human, for example, a living mammal and may be interchangeably used with the term “patient”. Examples of mammals include, but are not limited to, any member of the mammalian class: humans, non-human primates such as chimpanzees, and other apes and monkey species; farm animals such as cattle, horses, sheep, goats, swine; domestic animals such as rabbits, dogs, and cats; laboratory animals including rodents, such as rats, mice, ferrets, and guinea pigs, and the like. The term does not denote a particular age or gender. As used herein, an individual “at risk” of developing a particular disease, disorder, or condition may or may not have detectable disease or symptoms of disease, and may or may not have displayed detectable disease or symptoms of disease prior to the treatment methods described herein. “At risk” denotes that an individual has one or more risk factors, which are measurable parameters that correlate with development of a particular disease, disorder, or condition, as known in the art. An individual having one or more of these risk factors has a higher probability of developing a particular disease, disorder, or condition than an individual without one or more of these risk factors. The term “disease” as used herein, means an interruption, cessation, or disorder of body function, system, or organ. Non limiting examples of disease include malignant diseases, autoimmune diseases, inherited diseases, metabolic disorders, or infectious diseases. The term “vaccine” as used herein means a substance or composition comprising an antigen or immunogen for eliciting an immune response in a subject against the antigen or the immunogen. The term vaccine is also understood to mean a substance or composition comprising an antigen or immunogen that activates or stimulates an immune cell. In some cases, the antigen or immunogen is a peptide, a protein, a polysaccharide, or a combination thereof. In some cases, the antigen or immunogen is encoded by a nucleic acid, for example, a DNA, an RNA, or an mRNA. In some embodiments, the vaccine comprises a nucleic acid that encodes an antigen or an immunogen. In some embodiments, the vaccine comprises a nucleic acid as disclosed herein. In some embodiments, the vaccine comprises a nucleic acid encoding the receptor binding domain as disclosed herein. In some embodiments, the vaccine comprises a nucleic acid encoding the polypeptide as disclosed herein. In some embodiments, the vaccine comprises a nucleic acid encoding the multisubunit peptide as disclosed herein. In some embodiments, the vaccine comprises a receptor binding domain as disclosed herein. In some embodiments, the vaccine comprises a polypeptide as disclosed herein. In some embodiments, the vaccine comprises a multisubunit peptide as disclosed herein. As used herein, administration “conjointly” with another compound or composition includes simultaneous administration and / or administration at different times. Conjoint administration also encompasses administration as a co-formulation or administration as separate compositions, including at different dosing frequencies or intervals, and using the same route of administration or different routes of administration. The term “nucleic acid sequence” or “nucleic acid” have been used interchangeably and mean a sequence of nucleotides that encode either a receptor binding domain, a polypeptide, or a multisubunit peptide. In some embodiments, the nucleic acid sequence or nucleic acid includes a receptor binding domain sequence. In some embodiments, the nucleic acid sequence or nucleic acid includes a receptor binding domain sequence, a linker sequence, and a self-assembling sequence. In some embodiments, the nucleic acid sequence or nucleic acid comprises two or more polynucleotide sequences wherein some or all polynucleotide sequences comprises either a receptor binding domain sequence, a linker sequence, and a self-assembling sequence, or a linker sequence, a receptor binding domain sequence, a linker sequence, and a self-assembling sequence, or a combination thereof, wherein one polynucleotide sequence is connected to another polynucleotide sequence by a cleavage sequence, wherein the nucleic acid sequence includes a signal sequence upstream of one or more polynucleotide sequences. The receptor binding domain sequence comprises a mutation at: (a) a codon encoding an amino acid R at the position corresponding to the position 28 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid R with an amino acid (b) a codon encoding an amino acid K at the position corresponding to the position 38 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid V or T, (c) a codon encoding an amino acid K at the position corresponding to the position 126 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid T, (d) a codon encoding an amino acid F at the position corresponding to the position 138 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid F with an amino acid L, (e) a codon encoding an amino acid A at the position corresponding to the position 157 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid V, (f) a codon encoding an amino acid V at the position corresponding to the position 165 of the SEQ ID NO: 1, wherein the mutation is a deletion, (g) a codon encoding an amino acid E at the position corresponding to the position 166 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid E with an amino acid A, or K, or P, (h) a codon encoding an amino acid Q at the position corresponding to the position 175 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid Q with an amino acid E, (i) a codon encoding an amino acid S at the position corresponding to the position 176 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid S with an amino acid P, (j) a codon encoding an amino acid A at the position corresponding to the position 202 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid G, or a combination thereof. In some embodiments, the signal sequence is present upstream of the receptor binding domain sequence or the first polynucleotide sequence. In some embodiments, the signal sequence is present upstream of some polynucleotide sequences. In some embodiments, the signal sequence is present upstream of each of the polynucleotide sequences. In some embodiments, the polynucleotide sequence comprises a receptor binding domain sequence, a linker sequence, and a self-assembling sequence. In some embodiments, the polynucleotide sequence may comprise a linker sequence, a receptor binding domain sequence, a linker sequence, and a self-assembling sequence. Thus, in some embodiments, one linker sequence connects cleavage sequence with the receptor binding domain sequence and another linker sequence connects the receptor binding domain sequence with the self- assembling sequence in a polynucleotide sequence. In some embodiments, the linker sequence connects signal sequence with the polynucleotide sequence. In some embodiments, the nucleic acid sequence may comprise multiple repeats of polynucleotide sequences wherein each polynucleotide sequence may comprise either a receptor binding domain sequence, a linker sequence, and a self-assembling sequence, or a linker sequence, a receptor binding domain sequence, a linker sequence and a self- assembling sequence, or a combination thereof, such that total number of polynucleotide sequences in a nucleic acid sequence are not more than 100, wherein the receptor binding domain sequence comprises a mutation at: (a) a codon encoding an amino acid R at the position corresponding to the position 28 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid R with an amino acid T, (b) a codon encoding an amino acid K at the position corresponding to the position 38 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid V or T, (c) a codon encoding an amino acid K at the position corresponding to the position 126 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid T, (d) a codon encoding an amino acid F at the position corresponding to the position 138 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid F with an amino acid L, (e) a codon encoding an amino acid A at the position corresponding to the position 157 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid V, (f) a codon encoding an amino acid V at the position corresponding to the position 165 of the SEQ ID NO: 1, wherein the mutation is a deletion, (g) a codon encoding an amino acid E at the position corresponding to the position 166 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid E with an amino acid A, or K, or P, (h) a codon encoding an amino acid Q at the position corresponding to the position 175 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid Q with an amino acid E, (i) a codon encoding an amino acid S at the position corresponding to the position 176 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid S with an amino acid P, (j) a codon encoding an amino acid A at the position corresponding to the position 202 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid G, or a combination thereof. In some embodiments, the linker sequence connects signal sequence with the first polynucleotide sequence. In some embodiments, the signal sequence is present upstream of each of some or all of the polynucleotide sequences. In some embodiments, the nucleic acid sequence encodes multisubunit peptide. In some embodiments, the nucleic acid sequence or the nucleic acid encodes receptor binding domain, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, the nucleic acid sequence or the nucleic acid encodes a polypeptide comprising a receptor binding domain, a self-assembling peptide, and a linker peptide connecting the receptor binding domain with the self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. The terms “multisubunit peptide” as used herein means two or more polypeptides wherein some or all polypeptides comprises either a receptor binding domain, a linker peptide, and a self-assembling peptide, or a linker peptide, a receptor binding domain, a linker peptide and a self-assembling peptide, or a combination thereof, wherein one polypeptide is connected to another polypeptide by a cleavage peptide, wherein the multisubunit peptide includes a signal peptide upstream (amino-terminus) of one or more polypeptides, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, the signal peptide is present on the amino-terminus of the first polypeptide in a multisubunit peptide. In some embodiments, the signal peptide is present on the amino-terminus of some polypeptides in a multisubunit peptide. In some embodiments, the signal peptide is present on the amino-terminus of each of the polypeptides in a multisubunit peptide. In some embodiments, the polypeptide may comprise a receptor binding domain, a linker peptide, and a self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, the polypeptide may comprise a linker peptide, a receptor binding domain, a linker peptide, and a self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. Thus, in some embodiments, one linker peptide connects the cleavage peptide with the receptor binding domain and another linker peptide connects the receptor binding domain with the self- assembling peptide in a multisubunit peptide. In some embodiments, the multisubunit peptide may either comprise a receptor binding domain, a linker peptide, and a self- assembling peptide, or a linker peptide, a receptor binding domain, a linker peptide, and a self-assembling peptide, or a combination thereof, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1, such that the total number of polypeptides in a multisubunit peptide are not more than 100. In some embodiments, the linker peptide connects the signal peptide with the polypeptide in a multisubunit peptide. In some embodiments, the signal peptide is present on the amino-terminus of each of some or all polypeptides in a multisubunit peptide. The multisubunit peptide may comprise homologous polypeptides or heterologous polypeptides. The term “polynucleotide sequence” as used herein means a sequence of nucleotides that encodes a polypeptide. The terms “protein” or “peptide” have been used interchangeably herein and mean a polymer of amino acids linked through peptide bonds, but do not imply any specific length. The term also includes fusion proteins, muteins, analogs or modified forms. The term “polypeptide” as used herein means a sequence of amino acids that comprises either a receptor binding domain, a linker peptide, and a self-assembling peptide or a linker peptide, a receptor binding domain, a linker peptide, and a self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, the polypeptide comprises a receptor binding domain, a linker peptide, and a self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, the polypeptide comprises a linker peptide, a receptor binding domain, a linker peptide, and a self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, the polypeptide comprises a receptor binding domain, a self-assembling peptide, and a linker peptide connecting the receptor binding domain with the self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, the polypeptide may have some residues (amino acids) of cleavage peptide. In some embodiments, the polypeptide comprises a signal peptide. The term “signal sequence” as used herein means a sequence of nucleotides that encodes a signal peptide. In some embodiments, signal peptide is encoded by nucleic acid disclosed herein, in addition to other peptides, as applicable. The term “signal peptide” as used herein means a sequence of amino acids that transports the receptor binding domain, or the polypeptide or the multisubunit peptide to specific cell organelles. In some embodiments, the signal peptide transports the receptor binding domain, the polypeptide or the multisubunit peptide to golgi apparatus or golgi body. In some embodiments, the signal peptide transports the receptor binding domain, the polypeptide, or the multisubunit peptide to golgi body via endoplasmic reticulum. In some embodiments, the signal peptide is present on the N-terminus (amino-terminus or upstream) of the receptor binding domain or the polypeptide. In some embodiments, the signal peptide is present on the N-terminus (amino-terminus) of one or more polypeptides in a multisubunit peptide. In some embodiments, the signal peptide is present on the N-terminus of some or all polypeptides in a multisubunit peptide. In some embodiments, the signal peptide is present on the N-terminus of the first polypeptide in a multisubunit peptide. In some embodiments, the signal peptide is present on the N-terminus of some polypeptides in a multisubunit peptide. In some embodiments, the signal peptide is present on the N-terminus of all polypeptides in a multisubunit peptide. In some embodiments, the signal peptide is encoded by signal sequence or the nucleic acid. In some embodiments, the signal peptide is a golgi targeting signal peptide. In some embodiments, the signal peptide comprises one or more signal peptides, for example, signal peptide-1, signal peptide-2, and so on. In some embodiments, the signal peptide optionally comprises a linker peptide between two signal peptides. The term “cleavage sequence” as used herein means a sequence of nucleotides that encodes a cleavage peptide. In some embodiments, the cleavage peptide is encoded by nucleic acid disclosed herein, in addition to other peptides, as applicable. The term “cleavage peptide” as used herein means a sequence of amino acids that facilitates the action of cellular proteases to cleave the multisubunit peptide into individual polypeptides or self cleaves into individual polypeptides in a multisubunit peptide. The cleavage peptide is present between any two polypeptides in a multisubunit peptide. It connects one polypeptide with another polypeptide, for example, adjacent polypeptide, in a multisubunit peptide. The cleavage peptide carries one or more cleavage sites. In some embodiments, the cleavage peptide is a substrate for proteases. In some embodiments, cleavage peptide undergoes self-cleavage (for example, without bond formation during translation of nucleic acid) in a multisubunit peptide to result in individual polypeptides. In some embodiments, the cleavage peptide is a substrate for golgi specific proteases. In some embodiments, the cleavage peptide comprises one or more cleavage peptides, for example, cleavage peptide-1, cleavage peptide-2 and so on. In some embodiments, the cleavage peptide optionally comprises a linker peptide between two cleavage peptides. In some embodiments, the cleavage peptide self cleaves into individual polypeptides or is cleaved by the action of cellular proteases into individual polypeptides in a multisubunit peptide. In some embodiments, the cleavage peptide is a substrate for cellular proteases. In some embodiments, the cleavage peptide is a substrate for golgi specific proteases. In some embodiments, the cleavage peptide is a self cleaving peptide. In some embodiments, the cleavage peptide comprises two or more cleavage peptides (for example, cleavage peptide- 1, cleavage peptide-2 and so on), optionally linked by a linker peptide, wherein one cleavage peptide is a substrate for cellular proteases and the other cleavage peptide is a self cleaving peptide. The term “linker sequence” as used herein means a sequence of nucleotides that encodes a linker peptide. In some embodiments, the linker peptide is encoded by nucleic acid disclosed herein, in addition to other peptides, as applicable. The term “linker peptide” or “peptide linker” have been used interchangeably to mean a sequence of amino acids that either connects the receptor binding domain with the self-assembling peptide, connects the signal peptide with the receptor binding domain, connects the cleavage peptide with the receptor binding domain, connects the signal peptide with the polypeptide, connects two signal peptides, or connects two cleavage peptides. In some embodiments, the linker peptide connects the receptor binding domain with the self- assembling peptide in a polypeptide. In some embodiments, the linker peptide connects the signal peptide with the polypeptide in a multisubunit peptide. In some embodiments, the linker peptide connects the receptor binding domain with the self-assembling peptide of a polypeptide in a multisubunit peptide. In some embodiments, one linker peptide connects the cleavage peptide with the receptor binding domain and another linker peptide connects the receptor binding domain with the self-assembling peptide of a polypeptide in a multisubunit peptide. In some embodiments, one linker peptide connects the cleavage peptide with the receptor binding domain and another linker peptide connects the receptor binding domain with the self-assembling peptide in a multisubunit peptide. In some embodiments, one linker peptide connects the cleavage peptide with the receptor binding domain and another linker peptide connects the signal peptide with the receptor binding domain in a multisubunit peptide. In some embodiments, the linker peptide connects two cleavage peptides in a multisubunit peptide. In some embodiments, the linker peptide connects two signal peptides. In some embodiments, the linker peptide is an amino acid linker, a foldon, a scaffold or a combination thereof. In some embodiments, the linker peptide is an amino acid linker. In some embodiments, the linker peptide is a foldon. In some embodiments, the linker peptide is a scaffold. In some embodiments, the linker peptide comprises an amino acid linker and a foldon. In some embodiments, the linker peptide comprises an amino acid linker and a scaffold. In some embodiments, the linker peptide comprises a foldon and a scaffold. In some embodiments, the linker peptide comprises an amino acid linker, a foldon, and a scaffold. The term “amino acid linker sequence” as used herein means a sequence of nucleotides that encodes an amino acid linker. In some embodiments, the amino acid linker is encoded by nucleic acid as disclosed herein, in addition to other peptides, as applicable. The term “amino acid linker” as used herein means a sequence of amino acids that provides structural integrity to polypeptide such that the components of the polypeptide remain, as far as possible, in their native or stable conformation. In some embodiments, amino acid linker also helps in orientation of a polypeptide such that the domains or epitopes on the receptor binding domain are exposed or displayed for interaction or communication with cells or biomolecules or immune system in the absence of foldon or scaffold. In some embodiments, the amino acid linker connects two cleavage peptides in a multisubunit peptide. Some of the non-limiting examples of amino acid linkers includes, glycine serine linker, glycine proline linker, glycine threonine linker, alanine serine linker, any combination of two amino acids or a combination thereof. In some embodiments, amino acid linker is about 2-49 amino acid long. The term “glycine serine linker sequence” as used herein means a sequence of nucleotides that encodes a glycine serine linker. In some embodiments, the glycine serine linker is encoded by nucleic acid as disclosed herein, in addition to other peptides, as applicable. The term “glycine serine linker” as used herein means a sequence of amino acid comprising one or more glycine (G) and serine (S) in any combinations without any preference of order or limitation on number of appearances of either glycine or serine. In some embodiments, the glycine serine linker is few amino acids in length to several amino acids in length. The term “foldon sequence” as used herein means a sequence of nucleotides that encodes a foldon. In some embodiments, the foldon is encoded by nucleic acid disclosed herein, in addition to other peptides, as applicable. The term “foldon” as used herein means a sequence of amino acids that enables two or more homologous polypeptides or two or more heterologous polypeptides to organise to form an oligomeric complex. In some embodiments, the foldon also helps in orientation of a polypeptide such that the domains or epitopes on the receptor binding domain are exposed or displayed for interaction or communication with cells or biomolecules or immune system. The term “scaffold sequence” as used herein means a sequence of nucleotides that encodes a scaffold. In some embodiments, the scaffold is encoded by nucleic acid disclosed herein, in addition to other peptides, as applicable. The term “scaffold” as used herein means a sequence of amino acids that provides structural and / or functional integrity or support to the receptor binding domain and helps in orientation of receptor binding domain such that the domains or epitopes of the receptor binding domain are exposed or displayed for interaction or communication with cells or biomolecules or immune system. The term “oligomeric complex” as used herein means a complex formed by two or more homologous polypeptides or two or more heterologous polypeptides. In some embodiments, the oligomeric complex has at least two homologous polypeptides, at least three homologous polypeptides, at least four homologous polypeptides, at least five homologous polypeptides, or at least six homologous polypeptides and so on. In some embodiments, the oligomeric complex has at least two heterologous polypeptides, at least three heterologous polypeptides, at least four heterologous polypeptides, at least five heterologous polypeptides, or at least six heterologous polypeptides and so on. The term “self-assembling sequence” as used herein means a sequence of nucleotides that encodes a self-assembling peptide. In some embodiments, the self-assembling peptide is encoded by nucleic acid disclosed herein, in addition to other peptides, as applicable. The term “self-assembling peptide” as used herein means a sequence of amino acids that enables the polypeptides to self-assemble into a polypeptide nanoparticle. The term “self-assembly” or “self-assemble” or “self-assembling” has been used interchangeably to means the ability of polypeptides to undergo multimerization to form a polypeptide nanoparticle. In some embodiments, the polypeptide nanoparticle has at least two polypeptides (dimer or 2-mer), at least three polypeptides (trimer or 3-mer), at least four polypeptides (tetramer or 4-mer), at least five polypeptides (pentamer or 5-mer), at least six polypeptides (hexamer or 6-mer), at least seven polypeptides (heptamer or 7-mer), at least eight polypeptides (octamer or 8-mer), and so on. In some embodiments, the polypeptide nanoparticle is up to 500-mers. In some embodiments, hydrogen bonds, disulfide bonds, hydrophobic interactions, electrostatic interactions, and / or Van der Waals forces combine to maintain self-assembled structure. The term “multimerization” as used herein means association of two or more units of homologous polypeptides, heterologous polypeptides, oligomeric complexes, or their combination. The term “polypeptide nanoparticle” as used herein means a nanoparticle formed by self-assembly of polypeptides. In some embodiments, the polypeptide nanoparticle comprises two or more homologous polypeptides, or two or more heterologous polypeptides, one or more oligomeric complexes, or a combination thereof. The term “homologous polypeptides” as used herein means polypeptides that have identical receptor binding domain. For example, if two polypeptides have identical receptor binding domain (i.e., when both the receptor binding domains have 100% identity with respect to their amino acid sequence) they are considered to be homologous polypeptides. In some embodiments, multisubunit peptide comprises homologous polypeptides. The term “heterologous polypeptide” as used herein means polypeptides that have different receptor binding domain. For example, if two polypeptides in the multisubunit peptide have different or non-identical receptor binding domains (i.e., when both the receptor binding domains differ with respect to at least a single amino acid in their sequence), they are considered to be heterologous polypeptides. In some embodiments, multisubunit peptide comprises heterologous polypeptides. The term “upstream”, “amino-terminus”, or “N-terminus” has been used interchangeably in the context of amino acid sequences (protein, peptide, polypeptide, or any other sequence composed of amino acids) or the nucleic acid sequences (DNA, RNA or any other sequence composed of nucleotides) to mean amino end of an amino acid sequence or the 5-prime end of a nucleic acid sequence respectively. The term “fragment” as used herein, whether in the context of a nucleic acid, nucleotide, protein, polypeptide, or peptide, means any length of the nucleic acid, protein, polypeptide, or peptide sequence except the full length of the respective nucleic acid, protein, polypeptide, or peptide sequence. Fragment includes such portions of nucleic acid, protein, polypeptide, or peptide that are capable of treating, preventing, diagnosing, improving symptoms of, and / or delay the onset of an infection, disease, disorder, and / or condition. A fragment is also understood to mean an immunogenic fragment of the protein, polypeptide or peptide, or a fragment of nucleic acid encoding an immunogenic fragment of the protein, peptide, or polypeptide. The term “variant” as used herein, whether in the context of a nucleic acid, nucleotide, protein, polypeptide, or peptide sequence, means homologs, orthologs, paralogs, mutants or analogs of respective nucleic acid, protein, polypeptide, or peptide sequence. The term “mutant” as used herein, whether in the context of a nucleic acid, nucleotide, protein, polypeptide, or peptide sequence, means a sequence which is not a reference sequence identified by SEQ ID NO: 1. A mutant is also understood to mean a nucleic acid, nucleotide, protein, polypeptide, or peptide sequence that carries a mutation. The term “mutation” as used herein means, a change or modification in the sequence of nucleic acid or amino acid in comparison to a reference sequence (for example SEQ ID NO: 1 as herein) and includes insertion (typically represented as “insK100” which means insertion of amino acid lysine at 100thposition), deletion (typically represented as “K100del” or “K∆100” which means deletion of amino acid lysine at 100thposition), substitution (typically represented as “K100V” which means substitution of amino acid lysine with amino acid valine), or a combination thereof. Mutations are introduced to impart desirable properties upon the nucleic acid, nucleotide, protein, polypeptide, or peptide sequence. This includes, for example, enabling the nucleic acid, nucleotide, protein, polypeptide, or peptide sequence to elicit an immune response. The term “sequence” as used herein means nucleic acid sequences, nucleic acids, polynucleotides, amino acid sequences, proteins, polypeptides, or peptides, depending upon the context in which the term sequence is used, to mean a sequence of nucleotides or amino acids. In the context of nucleic acid, polynucleotide, or nucleotide sequence, the sequence is represented by a single letter code representing the nitrogenous base, for example A, T, G, C, or U. In the context of amino acid sequences, proteins, polypeptides, or peptides the sequence is represented by a single letter amino acid code as generally understood by persons skilled in the art. If the single letter amino acid code is represented by the letter “X”, it means the amino acid at that position is either absent or substituted by any other amino acid. In the present disclosure, amino acids are typically represented by their single letter amino acid codes, for example A for alanine, R for arginine, N for asparagine, D for aspartic acid, C for cystine, E for glutamic acid, Q for glutamine, G for glycine, H for histidine, I for isoleucine, L for leucine, K for lysine, M for methionine, F for phenylalanine, P for proline, S for serine, T for threonine, W for tryptophan, Y for tyrosine, V for valine and X for any of the amino acid. Alternatively, amino acids can also be represented by their three letter codes or by full name as generally known to a person skilled in the art. The term “percentage identity”, “percent identity”, “%age identity”, or “% identity” have been used interchangeably and means the extent of identity between two sequences (e.g. nucleic acid sequences or amino acid sequences). Percent identity can be determined by aligning two sequences, introducing gaps to maximize identity between the sequences. Percent identity should generally be calculated between the same types of sequences for example nucleic acids, i.e. for DNA sequences or RNA sequences or amino acid sequences. The alignment of sequences (nucleic acid or amino acid) can be performed with the appropriate pair wise sequence alignment programs. Identity can be calculated between two sequences by multiplying the number of matches in the pair by 100 and dividing by the length of the aligned region, including gaps. Gaps at the end of sequences are not included, and internal gaps are included in the length. In some embodiments, the nucleic acid sequence or the amino acid sequence, as the case may be, shares at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity with the sequences disclosed herein. In some embodiments, the nucleic acid sequence or the amino acid sequence, as the case may be, shares at least 50% to 60%, at least 60% to 70%, at least 70% to 80%, at least 80% to 90%, or at least 90% to 100% identity with the sequences disclosed herein. The term “functional analog” or “functional analogue” have been used interchangeably, whether in the context of nucleic acid sequence or amino acid (protein or peptide) sequence, and mean all sequences which essentially performs similar function compared to the sequence being referred. For example, functional analogs of a receptor binding domain include all sequences, irrespective of their percentage identity, which essentially perform at least one function similar to the function the receptor binding domain performs and carries at least one of the mutations disclosed herein. The term “comparable equivalent” in the context of nucleic acid sequences, amino acid sequences, proteins, polypeptides, or peptides, as disclosed herein, means structurally or functionally similar or identical nucleic acid sequences, amino acid sequences, proteins, polypeptides, or peptides compared to the nucleic acid sequences or amino acid sequences being referred. The term “receptor binding domain sequence” or “RBD sequence” have been used interchangeably and means a sequence of nucleotides that encodes a receptor binding domain or RBD. In some embodiments, the receptor binding domain is encoded by nucleic acid disclosed herein, in addition to other peptides, as applicable. The term “receptor binding domain” or “RBD” have been used interchangeably and means either a full length S1 subunit of the spike protein or a fragment thereof of SARS- CoV-2, including mutant, derivative or variant thereof that retains the ability to interact with the host cell receptors. In some embodiments, the receptor binding domain interacts with angiotensin-converting enzyme 2 (ACE2) receptor, dipeptidyl peptidase 4 (DPP4) receptor, 9-O-acetylated sialic acid (9-O-Ac-Sia) receptor or a combination thereof. The RBD also includes any fragments, mutants, derivatives, variants, comparable equivalents, or functional analogs of the RBD. The term RBD also includes the receptor binding domain of all SARS- CoV-2 strains, variants, or sub-variants. The RBD disclosed herein comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, the receptor binding domain includes, mutants, fragments, comparable equivalents, functional analogs of receptor binding domain. The term “SARS-CoV-2” as used herein mean severe acute respiratory syndrome coronavirus-2. The term SARS-CoV-2 also includes all strains, variants, and sub-variants or mutants of SARS-CoV-2. The term “COVID-19” or “coronavirus disease 2019” as used herein means a disease caused by SARS-CoV-2, typically characterized by symptoms such as fever, chills, cough, shortness of breath, tiredness, body ache, headache, loss of appetite, loss of smell, sore throat, congestion or runny nose, nausea or vomiting, including long COVID. Nucleic acid sequence and receptor binding domain, polypeptide, and multisubunit peptide In the present disclosure, the nucleic acid sequence or nucleic acid encodes either a receptor binding domain, a polypeptide or a multisubunit peptide as the case may be. In some embodiments, the nucleic acid sequence or the nucleic acid encodes a receptor binding domain, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, the nucleic acid encodes a signal peptide on the amino- terminus of the receptor binding domain. In some embodiments, the nucleic acid sequence or nucleic acid encodes a polypeptide comprising a receptor binding domain, a self-assembling peptide, and a linker peptide connecting the receptor binding domain and the self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments the nuclei acid encodes a signal peptide on the amino-terminus of the polypeptide. In some embodiments, the receptor binding domain, the linker peptide, and the self-assembling peptide are in N-terminus to C-terminus order in a polypeptide. In some embodiments, the nucleic acid sequence includes two or more polynucleotide sequences wherein some or all polynucleotide sequences comprises either a receptor binding domain sequence, a linker sequence, and a self-assembling sequence, or a linker sequence, a receptor binding domain sequence, a linker sequence, and a self- assembling sequence, wherein one polynucleotide sequence is connected to the another polynucleotide sequence by a cleavage sequence, wherein the nucleic acid sequence includes a signal sequence upstream of one or more polynucleotide sequences, wherein the receptor binding domain sequence comprises a mutation at: (a) a codon encoding an amino acid R at the position corresponding to the position 28 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid R with an amino acid T, (b) a codon encoding an amino acid K at the position corresponding to the position 38 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid V or T, (c) a codon encoding an amino acid K at the position corresponding to the position 126 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid T, (d) a codon encoding an amino acid F at the position corresponding to the position 138 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid F with an amino acid L, (e) a codon encoding an amino acid A at the position corresponding to the position 157 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid V, (f) a codon encoding an amino acid V at the position corresponding to the position 165 of the SEQ ID NO: 1, wherein the mutation is a deletion, (g) a codon encoding an amino acid E at the position corresponding to the position 166 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid E with an amino acid A, or K, or P, (h) a codon encoding an amino acid Q at the position corresponding to the position 175 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid Q with an amino acid E, (i) a codon encoding an amino acid S at the position corresponding to the position 176 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid S with an amino acid P, (j) a codon encoding an amino acid A at the position corresponding to the position 202 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid G, or a combination thereof. In some embodiments, the signal sequence is present upstream of the receptor binding domain sequence. In some embodiments, the signal sequence is present upstream of the polynucleotide sequence. In some embodiments, the signal sequence is present upstream of all or some polynucleotide sequences. In some embodiments, the signal sequence is present upstream of the first polynucleotide sequence. In some embodiments, the signal sequence is present upstream of some polynucleotide sequences. In some embodiments, the signal sequence is present upstream of each of the polynucleotide sequences. In some embodiments, the polynucleotide sequence comprises a receptor binding domain sequence, a linker sequence, and a self-assembling sequence, wherein the receptor binding sequence comprises a mutation at: (a) a codon encoding an amino acid R at the position corresponding to the position 28 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid R with an amino acid T, (b) a codon encoding an amino acid K at the position corresponding to the position 38 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid V or T, (c) a codon encoding an amino acid K at the position corresponding to the position 126 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid T, (d) a codon encoding an amino acid F at the position corresponding to the position 138 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid F with an amino acid L, (e) a codon encoding an amino acid A at the position corresponding to the position 157 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid V, (f) a codon encoding an amino acid V at the position corresponding to the position 165 of the SEQ ID NO: 1, wherein the mutation is a deletion, (g) a codon encoding an amino acid E at the position corresponding to the position 166 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid E with an amino acid A, or K, or P, (h) a codon encoding an amino acid Q at the position corresponding to the position 175 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid Q with an amino acid E, (i) a codon encoding an amino acid S at the position corresponding to the position 176 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid S with an amino acid P, (j) a codon encoding an amino acid A at the position corresponding to the position 202 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid G, or a combination thereof. In some embodiments, the polynucleotide sequence comprises a linker sequence, a receptor binding domain sequence, a linker sequence, and a self-assembling sequence, wherein the receptor binding domain sequence comprises a mutation at: (a) a codon encoding an amino acid R at the position corresponding to the position 28 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid R with an amino acid T, (b) a codon encoding an amino acid K at the position corresponding to the position 38 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid V or T, (c) a codon encoding an amino acid K at the position corresponding to the position 126 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid T, (d) a codon encoding an amino acid F at the position corresponding to the position 138 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid F with an amino acid L, (e) a codon encoding an amino acid A at the position corresponding to the position 157 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid V, (f) a codon encoding an amino acid V at the position corresponding to the position 165 of the SEQ ID NO: 1, wherein the mutation is a deletion, (g) a codon encoding an amino acid E at the position corresponding to the position 166 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid E with an amino acid A, or K, or P, (h) a codon encoding an amino acid Q at the position corresponding to the position 175 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid Q with an amino acid E, (i) a codon encoding an amino acid S at the position corresponding to the position 176 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid S with an amino acid P, (j) a codon encoding an amino acid A at the position corresponding to the position 202 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid G, or a combination thereof. In some embodiments, the nucleic acid sequence comprises one polynucleotide sequence comprising a receptor binding domain sequence, a linker sequence and a self- assembling sequence, and another polynucleotide sequence comprising a linker sequence, a receptor binding domain sequence, a linker sequence, and a self-assembling sequence, wherein the receptor binding domain sequence comprises a mutation at: (a) a codon encoding an amino acid R at the position corresponding to the position 28 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid R with an amino acid T, (b) a codon encoding an amino acid K at the position corresponding to the position 38 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid V or T, (c) a codon encoding an amino acid K at the position corresponding to the position 126 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid T, (d) a codon encoding an amino acid F at the position corresponding to the position 138 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid F with an amino acid L, (e) a codon encoding an amino acid A at the position corresponding to the position 157 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid V, (f) a codon encoding an amino acid V at the position corresponding to the position 165 of the SEQ ID NO: 1, wherein the mutation is a deletion, (g) a codon encoding an amino acid E at the position corresponding to the position 166 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid E with an amino acid A, or K, or P, (h) a codon encoding an amino acid Q at the position corresponding to the position 175 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid Q with an amino acid E, (i) a codon encoding an amino acid S at the position corresponding to the position 176 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid S with an amino acid P, (j) a codon encoding an amino acid A at the position corresponding to the position 202 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid G, or a combination thereof. In some embodiments, the nucleic acid sequence either comprises a receptor binding domain sequence, a linker sequence and a self-assembling sequence, or a linker sequence, a receptor binding domain sequence, a linker sequence, and a self-assembling sequence or a combination thereof, wherein the receptor binding domain sequence comprises a mutation at: (a) a codon encoding an amino acid R at the position corresponding to the position 28 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid R with an amino acid T, (b) a codon encoding an amino acid K at the position corresponding to the position 38 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid V or T, (c) a codon encoding an amino acid K at the position corresponding to the position 126 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid T, (d) a codon encoding an amino acid F at the position corresponding to the position 138 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid F with an amino acid L, (e) a codon encoding an amino acid A at the position corresponding to the position 157 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid V, (f) a codon encoding an amino acid V at the position corresponding to the position 165 of the SEQ ID NO: 1, wherein the mutation is a deletion, (g) a codon encoding an amino acid E at the position corresponding to the position 166 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid E with an amino acid A, or K, or P, (h) a codon encoding an amino acid Q at the position corresponding to the position 175 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid Q with an amino acid E, (i) a codon encoding an amino acid S at the position corresponding to the position 176 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid S with an amino acid P, (j) a codon encoding an amino acid A at the position corresponding to the position 202 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid G, or a combination thereof, such that the total number of polynucleotide sequences in a nucleic acid sequence are not more than 100. In some embodiments, the linker sequence connects the signal sequence with the polynucleotide sequence. In some embodiments, one linker sequence connects the cleavage sequence with the receptor binding domain sequence and another linker sequence connects the receptor binding domain sequence with the self-assembling sequence in a polynucleotide sequence. Some exemplary illustrations of receptor binding domain, polypeptide, and multisubunit peptide encoded by the nucleic acid sequences disclosed herein are provided in figure 1. Nucleic acid is a polymer comprising two or more nucleotides for example, deoxyribonucleotides or ribonucleotides, either in an unmodified or modified form. The nucleic acid may be either single stranded or double stranded, linear, or circular. The term nucleic acid also encompasses fragments, variants, mutants, or codon optimized sequences of deoxyribonucleotides, ribonucleotides, or functional analogs thereof. The term “nucleotide” as used herein means a ribonucleotide or deoxyribonucleotide. If the term nucleotide is used in the context of RNA, it refers to ribonucleotide, and if it is used in the context of DNA, it refers to deoxyribonucleotide. In some embodiments, the nucleic acid sequence is a DNA, an RNA, or an mRNA. The nucleic acid sequence may be few nucleotides long to several thousand nucleotides long. Deoxyribonucleic acid (DNA) The term “deoxyribonucleic acid” or “DNA” has been used interchangeably herein and means a polymer of deoxyribonucleotides. The DNA may be either single stranded or double stranded, linear, or circular. In some embodiments, the nucleic acid sequence is a DNA. In some embodiments, the DNA encodes a receptor binding domain, a polypeptide, or a multisubunit peptide described herein. Ribonucleic acid (RNA) The term “ribonucleic acid” or “RNA” has been used interchangeably herein and means a polymer of ribonucleotides. The RNA may be either single stranded or double stranded, linear, or circular. The term RNA also includes messenger RNA (mRNA). In some embodiments, the nucleic acid sequence is an mRNA. In some embodiments, the mRNA encodes a receptor binding domain as disclosed herein. In some embodiments, the mRNA encodes a polypeptide as disclosed herein. In some embodiments, the mRNA encodes a multisubunit peptide as disclosed herein. In some embodiments, the mRNA is unmodified or modified or a combination of both. The modification may be in the nucleobase of the nucleotide, or sugar moiety of the nucleotide, or the phosphate of the nucleotide. In some embodiments, mRNA is produced using recombinant expression system, or chemically synthesized or obtained through in vitro transcription. In some embodiments, the mRNA is obtained through single in vitro transcription (IVT) process. In some embodiments, the mRNA is circular. In other embodiments, the mRNA is linear. In some embodiments, the mRNA is self-amplifying or self-replicating. Self- amplifying or self-replicating mRNA as used herein means an mRNA that self-replicate upon delivery into the cells. Such mRNAs typically contain a replicase sequence, usually derived from an alphavirus, which enables amplification of the original strand of mRNA encoding the protein of interest upon delivery into the cells (Beissert, Tim et al. Molecular Therapy (2020) 28:119-128). The present disclosure provides mRNAs which are few hundred nucleotides long to several thousand nucleotides long. State of the art discourages using long mRNAs for vaccines and therapeutics. Longer mRNA molecules are more susceptible to degradation, which can compromise their stability and reduce their effectiveness in experimental and therapeutic context. Besides, longer mRNAs are also harder to transcribe accurately as the RNA polymerase used during the IVT reaction is inherently vulnerable to introduce errors within the transcribed mRNA. Additionally, long mRNA molecules are more prone to form complex secondary and tertiary structures, which can interfere with their intended function, reduce their efficiency, complicates the production process, and may even lead to unintended outcomes. Therefore, longer mRNAs are avoided in the art owing to their inherent complexities and challenges. In some embodiments, mRNA is few hundred nucleotides long to several thousand nucleotides long. In some embodiments, mRNA is about 0.3 kb, 0.4 kb, 0.5 kb, 0.6 kb, 0.7 kb, 0.8 kb, 0.9 kb, 1 kb, 1.5 kb, 2 kb, 2.5 kb, 3 kb, 3.5 kb, 4 kb, 4.5 kb, 5 kb, 5.5 kb, 6 kb, 6.5 kb, 7.0 kb, 7.5 kb, 8 kb, 8.5 kb, 9 kb, 9.5 kb, 10 kb, 10.5 kb, 11 kb, 11.5 kb, 12 kb, 12.5 kb, 13 kb, 13.5 kb, 14 kb, 14.5 kb, 15 kb, 16 kb, 17 kb, 18 kb, 19 kb, 20 kb, 21 kb, 22 kb, 23 kb, 24 kb, 25 kb, 26 kb, 27 kb, 28 kb, 29 kb, 30 kb in length, or a fraction thereof. In some embodiments, mRNA is about 0.3 to 30 kb, 0.3 to 25 kb, 0.3 to 20 kb in length, or any range therein. In some embodiments, mRNA is about 0.3 to 20 kb, 0.3 to 18 kb, 0.3 to 16 kb, 0.3 to 14 kb, 0.3 to 12 kb, 0.3 to 10 kb, 0.3 to 9 kb, 0.3 to 8 kb, 0.3 to 7 kb, 0.3 to 6 kb, 0.3 to 5 kb in length, or any range therein. In some embodiments, mRNA is about 0.3 kb to about 1 kb, about 1 kb to about 2 kb, about 2 kb to about 3 kb, about 3 kb to about 4 kb, about 4 kb to about 5 kb, about 5 kb to about 6 kb, about 6 kb to about 7 kb, about 7 kb to about 8 kb, about 8 kb to about 9 kb, about 9 kb to about 10 kb, about 10 kb to about 11 kb, about 11 kb to about 12 kb, about 12 kb to about 13 kb, about 13 kb to about 14 kb, about 14 kb to about 15 kb, about 15 kb to about 16 kb, about 16 kb to about 17 kb, about 17 kb to about 18 kb, about 18 kb to about 19 kb, about 19 kb to about 20 kb, about 20 kb to about 21 kb, about 21 kb to about 22 kb, about 22 kb to about 23 kb, about 23 kb to about 24 kb, about 24 kb to about 25 kb, about 25 kb to about 26 kb, about 26 kb to about 27 kb, about 27 kb to about 28 kb, about 28 kb to about 29 kb, about 29 kb to about 30 kb in length, or any range therein. Receptor binding domain sequence and receptor binding domain S1 subunit of SARS-CoV-2 contains the receptor binding domain either on the N- terminal region or the C-terminal region. RBD interact with the host cell receptors. In one of the embodiments, the RBD includes full length S1 subunit of the spike protein or fragment thereof of a SARS-CoV-2, including mutant, derivative, or variant thereof that retains the ability to interact with the host cell receptor. In some embodiments, the receptor binding domain interacts with angiotensin-converting enzyme 2 (ACE2) receptor or dipeptidyl peptidase 4 (DPP4) receptor, 9-O-acetylated sialic acid (9-O-Ac-Sia) receptor, or a combination thereof. In some embodiments, the nucleic acid includes a receptor binding domain sequence. Receptor binding domain of SARS-CoV-2 or any of the SARS-CoV-2 strain, variant, sub- variant, or mutant, may be used in accordance with the disclosure herein. In some embodiments, the nucleic acid encodes a receptor binding domain, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, the receptor binding domain sequence comprises a mutation at: (a) a codon encoding an amino acid R at the position corresponding to the position 28 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid R with an amino acid T, (b) a codon encoding an amino acid K at the position corresponding to the position 38 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid V or T, (c) a codon encoding an amino acid K at the position corresponding to the position 126 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid T, (d) a codon encoding an amino acid F at the position corresponding to the position 138 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid F with an amino acid L, (e) a codon encoding an amino acid A at the position corresponding to the position 157 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid V, (f) a codon encoding an amino acid V at the position corresponding to the position 165 of the SEQ ID NO: 1, wherein the mutation is a deletion, (g) a codon encoding an amino acid E at the position corresponding to the position 166 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid E with an amino acid A, or K, or P, (h) a codon encoding an amino acid Q at the position corresponding to the position 175 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid Q with an amino acid E, (i) a codon encoding an amino acid S at the position corresponding to the position 176 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid S with an amino acid P, (j) a codon encoding an amino acid A at the position corresponding to the position 202 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid G, or a combination thereof. In some embodiments, the receptor binding domain is identical in two or more polypeptides, for example homologous polypeptides. In some embodiments, the receptor binding domain is different in two or more polypeptides, for example as in heterologous polypeptides. In some embodiments, the receptor binding domain may be few amino acids long to several hundred amino acids long. Exemplary receptor binding domain includes the ones represented by the following amino acid sequences or comparable equivalents, including their codon optimized nucleic acid sequences, fragments, mutants, variants, or functional analogs thereof. RVQPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFS TFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIAPGQTGKIADYNYKLPDDFTG CVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFN CYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNF (SEQ ID NO: 1); RVQPTESIVRFPNVTNLCPFHEVFNATRFASVYAWNRTRISNCVADYSVLYNFAPF FAFKCYGVSPTKLNDLCFTNVYADSFVIKGNEVSQIAPGQTGNIADYNYKLPDDFT GCVIAWNSNKLDSTHSGNYDYWYRSLRKSKLKPFERDISTEIYQAGNKPCKGPGP NCYFPLQSYGFRPTYGVGHQPYRVVVLSFELLHGPATVCGPKKSTNLVKNKCVNF (SEQ ID NO: 2); RVQPTESIVRFPNVTNLCPFHEVFNATTFASVYAWNRTRISNCVADYSVLYNFAPF FAFKCYGVSPTKLNDLCFTNVYADSFVIKGNEVSQIAPGQTGNIADYNYKLPDDFT GCVIAWNSNKLDSKHSGNYDYWYRSLRKSKLKPFERDISTEIYQAGNKPCKGKGP NCYFPLQSYGFRPTYGVGHQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNF (SEQ ID NO: 3); RVQPTESIVRFPNVTNLCPFHEVFNATTFASVYAWNRTRISNCVADYSVLYNFAPF FAFKCYGVSPTKLNDLCFTNVYADSFVIKGNEVSQIAPGQTGNIADYNYKLPDDFT GCVIAWNSNKLDSKHSGNYDYWYRSLRKSKLKPFERDISTEIYQAGNKPCKGKGP NCYFPLESYGFRPTYGVGHQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNF (SEQ ID NO: 4); RVQPTESIVRFPNITNLCPFHEVFNATTFASVYAWNRVRISNCVADYSVIYNFAPFF AFKCYGVSPTKLNDLCFTNVYADSFVIRGNEVSQIAPGQTGNIADYNYKLPDDFTG CVIAWNSNKLDSKPSGNYNYRYRLLRKSKLKPFERDISTEIYQVGNKPCNGVAGP NCYSPLQPYGFRPTYGVGHQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNF (SEQ ID NO: 5); RVQPTESIVRFPNVTNLCPFHEVFNATRFASVYAWNRTRISNCVADYSVLYNFAPF FAFKCYGVSPTKLNDLCFTNVYADSFVIKGNEVSQIAPGQTGNIADYNYKLPDDFT GCVIAWNSNKLDSKHSGNYDYWYRSFRKSKLKPFERDISTEIYQAGNKPCKGKGP NCYFPLQSYGFRPTYGVGHQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNF (SEQ ID NO: 6); In some embodiments, the receptor binding domain share at least 50% identity (provided it at least carries one of the mutations disclosed herein) with the sequences disclosed herein above or comparable equivalents, including their codon optimized nucleic acid sequences, fragments, mutants, variants, or functional analogs thereof. A person skilled in the art will be able to include any RBD sequence of SARS-CoV-2 with the mutations as disclosed herein in accordance with the disclosure. Given any disclosed amino acid sequence of the RBD carrying the mutations as disclosed herein, a person skilled in the art would be able to deduce all possible DNA or RNA sequences that encodes the above receptor binding domains. Such DNA or RNA sequences are deemed to be incorporated in this disclosure. In some embodiments, the receptor binding domain is encoded by a nucleic acid sequence which may be either a DNA, an RNA, or an mRNA. In some embodiments, the receptor binding domain is encoded by a receptor binding domain sequence which may be either a DNA, an RNA, or an mRNA. Self-assembling sequence and self-assembling peptide In some embodiments, the nucleic acid encodes a self-assembling peptide in addition to a receptor binding domain and a linker peptide in a polypeptide. In some embodiments, the nucleic acid encodes a multisubunit peptide, which includes a self-assembling peptide. In some embodiments, the nucleic acid includes a self-assembling sequence. In some embodiments, the nucleic acid sequence and multisubunit peptide includes self-assembling sequence and self-assembling peptide respectively. In some embodiments, the nucleic acid includes a self-assembling sequence encoding self-assembling peptide. The self-assembling sequence comprises of a sequence of nucleotides, either deoxyribonucleotides or ribonucleotides, that encodes a self-assembling peptide. The self- assembling sequence includes codon optimized sequences, fragments, mutants, variants, comparable equivalents, functional analogs, or a combination thereof. In some embodiments, the self-assembling peptide is encoded by a nucleic acid sequence which may be either a DNA, an RNA, or an mRNA. In some embodiments, the self-assembling sequence is a DNA, an RNA, or an mRNA. Any self-assembling peptide that is capable of self-assembling into a polypeptide nanoparticle can be employed in accordance with the present disclosure. In some embodiments self-assembling peptide is a full-length protein or its fragment, mutant, or variant thereof. In some embodiments, the self-assembling peptide includes, but not limited to, lumazine synthase, MS2 coat protein, hepatitis B surface antigen (HBsAg) from Hepatitis B Virus, hepatitis B core antigen (HbcAg) from Hepatitis B virus, human papillomavirus L1 (HPV L1) protein, matrix protein M1 from influenza A virus, ferritin, riboflavin synthase, a dihydrolipoyl acetyltransferase (E2p), or a combination thereof, including their codon optimized nucleic acid sequences, fragments, mutants, variants, comparable equivalent, or functional analogs thereof. In some embodiments, the self-assembling peptide is a ferritin peptide. Ferritin is one of the ubiquitous proteins found in nature. It is produced by all living organisms including archaea, bacteria, algae, higher plants, and animals. Each ferritin protein is generally composed of 12 or 24 subunits or peptides which self-assembles into a ferritin nanoparticle. In some aspects, the nucleic acid encodes a polypeptide comprising a receptor binding domain, a linker peptide, and a ferritin peptide. In some aspects, the nucleic acid sequence and multisubunit peptide includes ferritin sequence and ferritin peptide respectively. The ferritin sequence comprises of a sequence of nucleotides, either deoxyribonucleotides or ribonucleotides, that encodes a ferritin peptide. In some embodiments, the ferritin sequence is a DNA, an RNA, or an mRNA. Any ferritin peptide that is capable of self-assembling into a nanoparticle can be employed in accordance with the present disclosure. In some embodiments, the ferritin peptide is obtained or derived from Helicobacter pylori ferritin, including their codon optimized nucleic acid sequences, fragments, mutants, variants, comparable equivalents, or functional analogs thereof. In some embodiments, the ferritin peptide is obtained or derived from Listeria innocua ferritin, including their codon optimized nucleic acid sequences, fragments, mutants, variants, comparable equivalents, or functional analogs thereof. In some embodiments, the self-assembling peptide is lumazine synthase. In some embodiments, the lumazine synthase is obtained or derived from Aquifex species (for example, Aquifex aeolicus) or Bacillus species (for example, Bacillus subtilis), including their codon optimized nucleic acid sequences, fragments, mutants, variants, comparable equivalents, or functional analogs thereof. In some embodiments, the self-assembling peptide is dihydrolipoyl acetyltransferase (E2p). In some embodiments, the dihydrolipoyl acetyltransferase (E2p) is obtained or derived from Bacillus stearothermophilus, including their codon optimized nucleic acid sequences, fragments, mutants, variants, comparable equivalents, or functional analogs thereof. In some embodiments, the self-assembling peptide is MS2 coat protein. In some embodiments, the MS2 coat protein is obtained or derived from Emesvirus zinderi, including their codon optimized nucleic acid sequences, fragments, mutants, variants, comparable equivalents, or functional analogs thereof. Exemplary self-assembling peptides includes, but not limited to, the ones represented by the following amino acid sequences or comparable equivalents, or a combination thereof, including codon optimized sequences, fragments, mutants, variants, or functional analogs thereof: LSKDIIKLLNEQVNKEMNSSNLYMSMSSWCYTHSLDGAGLFLFDHAAEEYEHAK KLIIFLNENNVPVQLTSISAPEHKFEGLTQIFQKAYEHEQHISESINNIVDHAIKSKDH ATFNFLQWYVAEQHEEEVLFKDILDKIELIGNENHGLYLADQYVKGI (SEQ ID NO: 7); LSKDIIKLLNEQVNKEMNSSNLYMSMSSWCYTHSLDGAGLFLFDHAAEEYEHAK KLIIFLNENNVPVQLTSISAPEHKFEGLTQIFQKAYEHEQHISESINNIVDHAIKSKDH ATFNFLQWYVAEQHEEEVLFKDILDKIELIGNENHGLYLADQYVKGIRRKR (SEQ ID NO: 8); LSKDIIKLLNEQVNKEMNSSNLYMSMSSWCYTHSLDGAGLFLFDHAAEEYEHAK KLIIFLNENNVPVQLTSISAPEHKFEGLTQIFQKAYEHEQHISESINNIVDHAIKSKDH ATFNFLQWYVAEQHEEEVLFKDILDKIELIGNENHGLYLADQYVKGIAKSRKS (SEQ ID NO: 9); MQIYEGKLTAEGLRFGIVASRFNHALVDRLVEGAIDCIVRHGGREEDITLVRVPGS WEIPVAAGELARKEDIDAVIAIGVLIRGATPHFDYIASEVSKGLANLSLELRKPITFG VITADTLEQAIERAGTKHGNKGWEAALSAIEMANLFKSLR (SEQ ID NO: 10); MTKKVGIVDTTFARVDMASIAIKKLKELSPNIKIIRKTVPGIKDLPVACKKLLEEEG CDIVMALGMPGKAEKDKVCAHEASLGLMLAQLMTNKHIIEVFVHEDEAKDDKEL DWLAKRRAEEHAENVYYLLFKPEYLTRMAGKGLRQGFEDAGPARE (SEQ ID NO: 11); MTEKEKMLAEKWYDANFDQYLINERARAKDICFELNHTRPSATNKRKELIDQLFQ TTTDNVSISIPFDTDYGWNVKLGKNVYVNTNCYFMDGGQITIGDNVFIGPNCGFYT ATHPLNFHHRNEGFEKAGPIHIGSNTWFGGHVAVLPGVTIGEGSVIGAGSVVTKDI PPHSLAVGNPCKVVRKIDNDLPSETLNDETIK (SEQ ID NO: 12); MENTTSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFQGGAPTCPGQNSQSPT SNHSPTSCPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLLPGTSTT GTGPCRTCTIPAQGTSMFPSCCCTKPSDGNCTCIPIPSSWAFARFLWEWASVRFSW LSLLVPFVQWFAGLSPTVWLSVIWMMWYRGPSLYNTLSPFLPLLPISFCLWVYI (SEQ ID NO: 13); MIFVLGGCRHKLVCSPAPCNFFHLCLIISCSCPTVHASKLCLGWLWGMHIDPYKEF GASVELLSFLPSDFFPSIRDLLDTASALYREALESPEHCSPHHTALRQAILCWGELM NLATWVGSNLEDPASRELVVSYVNVNMGLKIRQLLWFHISCLTFGRETVLEYLVS FGVWIRTPPAYRPPNAPILSTLPETTVVRRRGRSPRRRTPSPRRRRSQSPRRRRSQSR ESQC (SEQ ID NO: 14); MSLWLPSEATVYLPPVPVSKVVSTDEYVARTNIYYHAGTSRLLAVGHPYFPIKKPN NNKILVPKVSGLQYRVFRIHLPDPNKFGFPDTSFYNPDTQRLVWACVGVEVGRGQ PLGVGISGHPLLNKLDDTENASAYAANAGVDNRECISMDYKQTQLCLIGCKPPIGE HWGKGSPCTNVAVNPGDCPPLELINTVIQDGDMVDTGFGAMDFTTLQANKSEVP LDICTSICKYPDYIKMVSEPYGDSLFFYLRREQMFVRHLFNRAGAVGENVPDDLYI KGSGSTANLASSNYFPTPSGSMVTSDAQIFNKPYWLQRAQGHNNGICWGNQLFVT VVDTTRSTNMSLCAAISTSETTYKNTNFKEYLRHGEEYDLQFIFQLCKITLTADVM TYIHSMNSTILEDWNFGLQPPPGGTLEDTYRFVTSQAIACQKHTPPAPKEDPLKKY TFWEVNLKEKFSADLDQFPLGRKFLLQAGLKAKPKFTLGKRKATPTTSSTSTTAKR KKRKL (SEQ ID NO: 15); MSLLTEVETYVLSIVPSGPLKAEIAQRLEDVFAGKNTDLEALMEWLKTRPILSPLTK GILGFVFTLTVPSERGLQRRRFVQNALNGNGDPNNMDRAVKLYRKLKREITFHGA KEIALSYSAGALASCMGLIYNRMGAVTTEVAFGLVCATCEQIADSQHRSHRQMVT TTNPLIRHENRMVLASTTAKAMEQMAGSSEQAAEAMEVASQARQMVQAMRAIG THPRSSAGLKDDLLENLQAYQKRMGVQMQRFK (SEQ ID NO: 16); AAAKPATTEGEFPETREKMSGIRRAIAKAMVHSKHTAPHVTLMDEADVTKLVAH RKKFKAIAAEKGIKLTFLPYVVKALVSALREYPVLNTAIDDETEEIIQKHYYNIGIA ADTDRGLLVPVIKHADRKPIFALAQEINELAEKARDGKLTPGEMKGASCTITNIGS AGGQWFTPVINHPEVAILGIGRIAEKPIVRDGEIVAAPMLALSLSFDHRMIDGATAQ KALNHIKRLLSDPELLLM (SEQ ID NO: 17); ASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQN RKYTIKVEVPKVATQTVGGVELPVAAWRSYLNMELTIPIFATNSDCELIVKAMQG LLKDGNPIPSAIAANSGIY (SEQ ID NO: 99); QIYEGKLTAEGLRFGIVASRFNHALVDRLVEGAIDCIVRHGGREEDITLVRVPGSW EIPVAAGELARKEDIDAVIAIGVLIRGATPHFDYIASEVSKGLAQLSLELRKPITFGVI TADTLEQAIERAGTKHGNKGWEAALSAIEMANLFKSLR (SEQ ID NO: 100); NIIQGNLVGTGLKIGIVVGRFNDFITSKLLSGAEDALLRHGVDTNDIDVAWVPGAF EIPFAAKKMAETKKYDAIITLGTVIRGATTHYDYVCNEAAKGIAQAAQTTGVPVIF GIVTTENIEQAIETAGTKAGNKGVDCAVSAIEMANLQRSFE (SEQ ID NO: 101); KTINSVDTKEFLNHQVANLNVFTVKIHQIHWYMRGHNFFTLHEKMDDLYSEFGEQ MDEVAERLLAIGGSPFSTLKEFLENASVEEAPYTKPKTMDQLMEDLVGTLELLRD EYKQGIELTDKEGDDVTNDMLIAFKASIDKHIWMFKAFLGKAPLE (SEQ ID NO: 102). In some embodiments, the self-assembling peptide shares at least 50% identity with the sequences disclosed herein above or comparable equivalents, or a combination thereof, including their codon optimized nucleic acid sequences, fragments, mutants, variants, or functional analogs thereof. Given the disclosed amino acid sequences of the self-assembling peptides, a person skilled in the art would be able to deduce all possible DNA or RNA sequences that encodes the above self-assembling peptides. Such DNA or RNA sequences are deemed to be incorporated in this disclosure. In some embodiments, the self-assembling peptide is encoded by a nucleic acid sequence which may be either a DNA, an RNA, or an mRNA. In some embodiments, the self-assembling peptide is encoded by the self-assembling sequence which may be either a DNA, an RNA, or an mRNA. Linker sequence and linker peptide In some embodiments the nucleic acid sequence, and the polypeptide, or the multisubunit peptide includes linker sequence and linker peptide respectively. In some embodiments, the nucleic acid includes a linker sequence. The linker sequence comprises a sequence of nucleotides, either deoxyribonucleotides or ribonucleotides, that encodes a linker peptide. The linker sequence includes codon optimized sequences, fragments, mutants, variants, comparable equivalents, functional analogs, or a combination thereof. In some embodiments, the linker peptide is encoded by a nucleic acid sequence which may be either a DNA, an RNA, or an mRNA. In some embodiments, the linker sequence is a DNA, an RNA, or an mRNA. In some embodiments, the linker peptide connects the receptor binding domain with the self-assembling peptide, connects the signal peptide with the receptor binding domain, connects the cleavage peptide with the receptor binding domain, connects the signal peptide with the polypeptide, connects two signal peptides, or connects two cleavage peptides. In some embodiments, the linker peptide connects the receptor binding domain with the self-assembling peptide in a polypeptide. In some embodiments, the linker peptide connects the signal peptide with the linker peptide of a polypeptide in a multisubunit peptide. In some embodiments, the linker peptide connects the receptor binding domain with the self-assembling peptide in a polypeptide. In some embodiments, the linker peptide connects the signal peptide with a polypeptide. In some embodiments, the linker peptide of the polypeptide connects the signal peptide with the receptor binding domain of the polypeptide in a multisubunit peptide. In some other embodiments, the linker peptide connects the signal peptide with the first polypeptide in a multisubunit peptide. In some embodiments, one linker peptide connects the cleavage peptide with the receptor binding domain and another linker peptide connects the receptor binding domain with the self- assembling peptide in a multisubunit peptide. In some embodiments, the linker peptide connects two signal peptides. In some embodiments, the linker peptide connects two cleavage peptides in a multisubunit peptide. Any suitable linker peptides can be employed in accordance with the present disclosure. In some embodiments, the linker peptide is an amino acid linker, a foldon, a scaffold or a combination thereof. In some embodiments, the linker peptide is an amino acid linker. In some embodiments, the linker peptide is a foldon. In some embodiments, the linker peptide is a scaffold. In some embodiments, linker peptide consists of a combination of an amino acid linker and a foldon. In some embodiments, linker peptide consists of a combination of an amino acid linker and a scaffold. In some embodiments, linker peptide consists of a combination of a foldon and scaffold. In some embodiments, linker peptide consists of a combination of an amino acid linker, a foldon, and a scaffold. In some embodiments, the amino acid linker comprises about 2-49 amino acids, 2- 40 amino acids, 2-40 amino acids, 2-20 amino acids, 2-15 amino acids, or 2-10 amino acids. In some embodiments, the amino acid linker comprises a glycine serine linker, a glycine proline linker, a glycine threonine linker, an alanine serine linker, any combination of two amino acids, or a combination thereof. The glycine proline linker comprises of glycine (G) and proline (P) amino acids consecutively without any preference of order of appearance of either glycine or proline. In some embodiments, the glycine proline linker is 2-49 amino acids in length. The glycine threonine linker comprises of glycine (G) and threonine (T) amino acids consecutively without any preference of order of appearance of either glycine or threonine. In some embodiments, the glycine threonine linker is 2-49 amino acids in length. The alanine serine linker comprises of alanine (A) and serine (S) amino acids consecutively without any preference of order of appearance of either alanine or serine. In some embodiments, the alanine serine linker is 2-49 amino acids in length. The glycine serine linker comprises of glycine (G) and serine (S) amino acids consecutively without any preference of order of appearance of either glycine or serine. In some embodiments, the glycine serine linker is 2-49 amino acids in length. Exemplary amino acid linkers include, but not limited to, the ones represented by the following amino acid sequences or comparable equivalents, or their combinations, including their codon optimized nucleic acid sequences, fragments, mutants, variants, or functional analogs thereof: GSG (SEQ ID NO: 18); GSGG (SEQ ID NO: 19); GGSGG (SEQ ID NO: 20); GGSGGGGSGG (SEQ ID NO: 21); GGSGGGGSGGGGSGG (SEQ ID NO: 22); SGGSGG (SEQ ID NO: 23); GGGGSGGGGS (SEQ ID NO: 24); GGGGSGGGGSGGGGS (SEQ ID NO: 25); In some embodiments, the amino acid linkers share at least 50% identity with the sequences disclosed herein above or comparable equivalents, or a combination thereof, including their codon optimized nucleic acid sequences, fragments, mutants, variants, or functional analogs thereof. Given the disclosed amino acid sequences of the amino acid linkers, a person skilled in the art would be able to deduce all possible DNA or RNA sequences that encodes the above amino acid linkers. Such DNA or RNA sequences are deemed to be incorporated in this disclosure. In some embodiments, the glycine serine linker is encoded by a nucleic acid sequence which may be either a DNA, an RNA, or an mRNA. In some embodiments, the amino acid linker is encoded by an amino acid linker sequence which may be either a DNA, an RNA, or an mRNA. In some embodiments, the linker peptide is a foldon. In some embodiments, foldon comprises of a sequence of amino acids encoded by a foldon sequence. In some embodiments, the nucleic acid includes a foldon sequence. The foldon sequence includes codon optimized sequences, fragments, mutants, variants, functional analogs, comparable equivalents, or a combination thereof. A foldon enables two or more homologous polypeptides or two or more heterologous polypeptides to organise to form an oligomeric complex. In some embodiments, foldon also helps in orientation of a polypeptide such that the domains or epitopes on the receptor binding domain are exposed or displayed for interaction or communication with cells or biomolecules or immune system. Exemplary foldons include, but not limited to, the ones represented by the following amino acid sequences or comparable equivalents, or a combination thereof, including their codon optimized nucleic acid sequences, fragments, mutants, variants, or functional analogs thereof: YIPEAPRDGQAYVRKDGEWVLLSTFL (SEQ ID NO: 26); HENEISHHAKEIERLQKEIERHKQSIKKLKQSE (SEQ ID NO: 27); In some embodiments, the foldon shares at least 50% identity with the sequences disclosed herein above or comparable equivalents, or a combination thereof, including their codon optimized nucleic acid sequences, fragments, mutants, variants, or functional analogs thereof. Given the disclosed amino acid sequences of the foldons, a person skilled in the art would be able to deduce all possible DNA or RNA sequences that encodes the above foldons. Such DNA or RNA sequences are deemed to be incorporated in this disclosure. In some embodiments, the foldon is encoded by a nucleic acid sequence which may be either a DNA, an RNA, or an mRNA. In some embodiments, the foldon is encoded by a foldon sequence which may be either a DNA, an RNA, or an mRNA. In some embodiments, the linker peptide is a scaffold. In some embodiments, scaffold comprises of a sequence of amino acids encoded by a scaffold sequence. In some embodiments, the nucleic acid includes a scaffold sequence. The scaffold sequence includes codon optimized sequences, fragments, mutants, variants, or a combination thereof. A scaffold provides structural and / or functional integrity or support to the receptor binding domain and may also help in orientation of receptor binding domain such that the domains or epitopes of the receptor binding domain are exposed or displayed for interaction or communication with cells or biomolecules or immune system. Exemplary scaffolds include, but not limited to, the ones represented by the following amino acid sequences or comparable equivalents, or a combination thereof, including their codon optimized nucleic acid sequences, fragments, mutants, variants, or functional analogs thereof: VDNKFNKEMRNAYWEIALLPNLNNQQKRAFIRSLYDDPSQSANLLAEAKKLNDA QAPK (SEQ ID NO: 28); QDSTSDLIPAPPLSKVPLQQNFQDNQFHGKWYVVGKAGNHDLREDKDPRKMQAT IYELKEDKSYNVTNVRFVHKKCNYRIWTFVPGSQPGEFTLGNIKSWPGLTSWLVR VVSTNYNQHAMVFFKRVYQNRELFEITLYGRTKELTNELKENFIRFSKSLGLPENH IVFPVPIDQCIDGSAWSHPQFEK (SEQ ID NO: 29); VSDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKST ATISGLKPGVDYTITVYAVTGRGDSPASSKPISINYRT (SEQ ID NO: 30); GCPRILMRCKQDSDCLAGCVCGPNGFCG (SEQ ID NO: 31); MRGSHHHHHHGSDLGKKLLEAARAGQDDEVRILMANGADVNATDNDGYTPLHL AASNGHLEIVEVLLKNGADVNASDLTGITPLHLAAATGHLEIVEVLLKHGADVNA YDNDGHTPLHLAAKYGHLEIVEVLLKHGADVNAQDKFGKTAFDISIDNGNEDLAE ILQ (SEQ ID NO: 32); MRGSHHHHHHGSVKVKFFWNGEEKEVDTSKIVWVKRAGKSVLFIYDDNGKNGY GDVTEKDAPKELLDMLARAEREKKL (SEQ ID NO: 33); MLPAPKNLVVSEVTEDSARLSWDDPAAFYESFLIQYQESEKVGEAIVLTVPGSERS YDLTGLKPGTEYTVSIYGVHNVYKDTNMRGLPLSAIFTTGGHHHHHH (SEQ ID NO: 34); ETDICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKV CAPV (SEQ ID NO: 35); MIPGGLSEAKPATPEIQEIVDKVKPQLEEKTNETYGKLEAVQYKTQVVAGTNYYIK VRAGDNKYMHLKVFKSLPGQNEDLVLTGYQVDKNKDDELTGF (SEQ ID NO: 36); PCSAFEFHCLSGECIHSSWRCDGGPDCKDKSDEENCA (SEQ ID NO: 37); MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLS DYNIQKESTLHLVLRLRGG (SEQ ID NO: 38); MGSIIFLEDRAFQGRIYGCTTDCPNLQPYFSRCNSIVVQSGCWMIYERPNYQGHQY FLRRGEYPDYQQWMGLSDSIRSCCLIPPHSGAYRMKIYDRDELRGQMSELTDDCL SVQDRFHLTEIHSLNVLEGSWILYEMPNYRGRQYLLRPGEYRRFLDWGAPNAKVG SLRRVMDLYLEHHHHHH (SEQ ID NO: 39); AGHRIAWLLMMGHPRQQLAIIFGIGVSTLYRYFPA (SEQ ID NO: 40); AFSKSEEARHSSLERECIEEICDHAEAWDIMM (SEQ ID NO: 41); RECDYCGTDIEPGTGGMAVHGDGATTHFCSHRCAWDAMMGAEARNLEWTDTA R (SEQ ID NO: 42); CSQNEYFDSLLHACIPCQLRCSGAPHRCAWDCMM (SEQ ID NO: 43); EHIPGTLAARLSHRAAWDLMMHSLDASQGTATGPRGIFTAEDALKLVQLKQTGK TFPTYKCGHRFAWDCMMGSGLNGAACFAVKIADLPVYSCECAIGFMGQRCEYKE (SEQ ID NO: 44); ACYGHRCAWDCMMLGFSSGKCINSKCKCYK (SEQ ID NO: 45); GEYVVEKVLDKRVVKGKVEYLLKWKGFSDEDNTWEPDENLDGHRLAWDFMMA DVYEVEAILADRVNKNGINEYYIKWAGYDWYDNTWEPEQNLFGAGHRLAWWM MR (SEQ ID NO: 46); AGTIKITQTRSAIGRLPAHKATLLGLGLRRIGHTVEREDGHRIAWDIMMVSFMVKV EG (SEQ ID NO: 47); GIPCGESCGSPCISSAIGCSCKLINTNGSWHIVCYRN (SEQ ID NO: 48); GKCPETFDAWYCLNDAHCFAVLINTNGSWHIVYSCECAIGFMGQRCEYKE (SEQ ID NO: 49); QEEADRTVFVGNLEARVREEILYELFLQAGPLTKVTICKDREGKPKSFGFVCFKHP ESVSYAIALAGLINLNGSWIIVSGPSSG (SEQ ID NO: 50); NEEDAGKMFVGGLSWDTSKKDLKDYFTKFGEVVDCTIKMDPNTGRSRGFGFILFK DAASVEKVLDAGLHNLNGSWIIPKKA (SEQ ID NO: 51); SGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDEQGSKGYGFVHFETQEAAER AIAKMGLMNLNGSWVIVGRFKSRKE (SEQ ID NO: 52); PSRVVYLGSIPYDQTEEQILDLCSNVGPVINLKMMFDPQTGRSKGYAFIEFRDLESS ASAVGALGLYNLNGSWLICGYSSNSDISGVSLEHHHH (SEQ ID NO: 53); LAILVFGYPETMANQVIAYFQEFGTILEDFEVLRKPQAMTVGLQDRQFVPIFSGNS WTKITYDNPASAVDALAEGLANFNGSWLLVIPYTKDAVERLQ (SEQ ID NO: 54); RLVNCNGSWLIGLDRPPYPGAKGEDIYNNVSRKAWDEWQKHQTMLINERRLNM MNAEDRKFLQQEMDKFLSGEDY (SEQ ID NO: 55); FAVESIEKLRNRNGSWEILVKWRGWSPKYNTWEPEENIG (SEQ ID NO: 56); MRDFFVITNSLYNFNGSWYIKGAVLHVSPTQKRAFWVIADQENFIKQVNKNIEYV EKQASPAFLQRIVEIYQVKFEGKNVG (SEQ ID NO: 57); In some embodiments, the scaffold shares at least 50% identity with the sequences disclosed herein above or comparable equivalents, or a combination thereof, including their codon optimized nucleic acid sequences, fragments, mutants, variants, or functional analogs thereof. Given the disclosed amino acid sequences of the scaffold, a person skilled in the art would be able to deduce all possible DNA or RNA sequences that encodes the above scaffold. Such DNA or RNA sequences are deemed to be incorporated in this disclosure. In some embodiments, the scaffold is encoded by a nucleic acid sequence which may be either a DNA, an RNA, or an mRNA. In some embodiments, the scaffold is encoded by the scaffold sequence which may be either a DNA, an RNA, or an mRNA. In some embodiments, the linker peptide comprises an amino acid linker and a foldon. In some embodiments, the linker peptide comprises an amino acid linker followed by a foldon. In another embodiment, the linker peptide comprises a foldon followed by an amino acid linker. In some embodiments, the linker peptide comprises an amino acid followed by a foldon and another amino acid linker. In some embodiments, the linker peptide comprises a foldon followed by an amino acid linker and another foldon. In some embodiments, the linker peptide comprises an amino acid linker and a scaffold. In some embodiments, the linker peptide comprises an amino acid linker and a scaffold. In some embodiments, the linker peptide comprises an amino acid linker followed by a scaffold. In some embodiments, the linker peptide comprises a scaffold followed by an amino acid linker. In some embodiments, the linker peptide comprises an amino acid linker followed by a scaffold and another amino acid linker. In some embodiments, the linker peptide comprises a scaffold followed by an amino acid linker and another scaffold. In some embodiments, the linker peptide comprises a foldon and a scaffold. In some embodiments, the linker peptide comprises a foldon followed by a scaffold. In some embodiments, the linker peptide comprises a scaffold followed by a foldon. In some embodiments, the linker peptide comprises a foldon followed by a scaffold and another foldon. In some embodiments, linker peptide comprises a scaffold followed by a foldon and another scaffold. In some embodiments, the linker peptide comprises an amino acid linker, a foldon and a scaffold. In some embodiments, the linker peptide comprises an amino acid linker followed by a foldon, and a scaffold. In some embodiments, the linker peptide comprises a foldon followed by an amino acid linker, and a scaffold. In some embodiments, the linker peptide comprises a scaffold followed by an amino acid linker, and a foldon. In some embodiments, the linker peptide comprises a first amino acid linker followed by a foldon, a second amino acid linker followed by scaffold, and a third amino acid linker. In some embodiments, the linker peptide comprises a first amino acid linker followed by a scaffold, a second amino acid linker followed by a foldon, and a third amino acid linker. In some embodiments, the linker peptide comprises a scaffold followed by a first amino acid linker, and a foldon followed by a second amino acid linker. In some embodiments, the linker peptide comprises a first amino acid linker followed by a scaffold, and a second amino acid linker followed by a foldon. Cleavage sequence and cleavage peptide In some embodiments, the nucleic acid includes a cleavage sequence. In some embodiments, the nucleic acid sequence and multisubunit peptide includes cleavage sequence and cleavage peptide respectively. The cleavage sequence comprises a sequence of nucleotides, either deoxyribonucleotides or ribonucleotides, that encodes a cleavage peptide. The cleavage sequence includes codon optimized sequences, fragments, mutants, variants, comparable equivalents, functional analogs, or a combination thereof. In some embodiments, the cleavage peptide is encoded by a nucleic acid sequence which may be either a DNA, an RNA, or an mRNA. In some embodiments, the cleavage sequence is a DNA, an RNA, or an mRNA. The cleavage peptide connects one polypeptide with another polypeptide, for example, the adjacent polypeptide in a multisubunit peptide. The cleavage peptide carries one or more cleavage sites. In some embodiments, the cleavage peptide comprises one or more cleavage peptides, for example cleavage peptide-1, cleavage peptide-2 and so on. In some embodiments, the cleavage peptide optionally comprises a linker peptide between two cleavage peptides in a multisubunit peptide. In some embodiments, the cleavage peptide facilitates the action of cellular proteases to cleave the multisubunit peptide into individual polypeptides or self cleaves into individual polypeptides. In some embodiments, the resulting polypeptides may comprise either a receptor binding domain, a linker peptide and a self-assembling peptide or a linker peptide, a receptor binding domain, a linker peptide and a self-assembling peptide or a combination thereof. In some embodiments, the polypeptide, in addition to these peptides, may also have some residues (amino acids) of cleavage peptide. Any cleavage peptide that is susceptible to the action of cellular proteases or a cleavage peptide that has the ability to undergo self- cleavage can be employed in accordance with the present disclosure. In some embodiments, the cleavage peptide is a substrate for cellular proteases. In some embodiments, the cleavage peptide is a substrate for golgi specific proteases. In some embodiments, the cleavage peptide is a self cleaving peptide. In some embodiments, the cleavage peptide comprises two or more cleavage peptides (for example, cleavage peptide- 1, cleavage peptide-2 and so on), optionally linked by a linker peptide, wherein one cleavage peptide is a substrate for cellular proteases and the other cleavage peptide is a self cleaving peptide. In some embodiments, the cleavage peptide is a golgi specific cleavage peptide i.e., susceptible to action of golgi specific proteases. Exemplary cleavage peptide includes, but not limited to, the one represented by the following amino acid sequence or comparable equivalents, or a combination thereof, including their codon optimized nucleic acid sequences, fragments, mutants, variants, or functional analogs thereof: RRKRSVS (SEQ ID NO: 58); GIRRKRSVSH (SEQ ID NO: 59); VQREKRAVGI (SEQ ID NO: 60); SIRHKREPSV (SEQ ID NO: 61); KRRQRRRPPQ (SEQ ID NO: 62); KIRRRRDVVD (SEQ ID NO: 63); HNRTKRSTDG (SEQ ID NO: 64); RKRRKRELET (SEQ ID NO: 65); THRTRRSTSD (SEQ ID NO: 66); SRRKRRSAST (SEQ ID NO: 67); NLRRRRDLVD (SEQ ID NO: 68); LRRRRRDAGN (SEQ ID NO: 69); ATNFSLLKQAGDVEENPGP (SEQ ID NO: 70); EGRGSLLTCGDVEENPGP (SEQ ID NO: 71); QCTNYALLKLAGDVESNPGP (SEQ ID NO: 72); SVSGSGATNFSLLKQAGDVEENPGP (SEQ ID NO: 73); In some embodiments, the cleavage peptide shares at least 50% identity with the sequence disclosed herein above or comparable equivalents, or a combination thereof, including their codon optimized nucleic acid sequences, fragments, mutants, variants, or functional analogs thereof. Given the disclosed amino acid sequences of the cleavage peptide, a person skilled in the art would be able to deduce all possible DNA or RNA sequences that encodes the above cleavage peptide. Such DNA or RNA sequences are deemed to be incorporated in this disclosure. In some embodiments, the cleavage peptide is encoded by a nucleic acid sequence which may be either a DNA, an RNA, or an mRNA. In some embodiments, the cleavage peptide is encoded by a cleavage sequence which may be either a DNA, an RNA, or an mRNA. Signal sequence and signal peptide In some embodiments, the nucleic acid includes a signal sequence. In some embodiments nucleic acid sequence and receptor binding domain, polypeptide, or multisubunit peptide includes signal sequence and signal peptide respectively. In some embodiments, the nucleic acid sequence includes a signal sequence. The signal sequence comprises a sequence of nucleotides, either deoxyribonucleotides or ribonucleotides, that encodes a signal peptide. The signal sequence includes codon optimized sequences, fragments, mutants, variants, comparable equivalents, functional analogs, or a combination thereof. In some embodiments, the signal peptide is encoded by a nucleic acid sequence which may be either a DNA, an RNA, or an mRNA. In some embodiments, the signal sequence is a DNA, an RNA, or an mRNA. In some embodiments, the signal peptide is present upstream (N-terminus or amino- terminus) of a receptor binding domain. In some embodiments, the signal peptide is present upstream (N-terminus or amino-terminus) of a polypeptide. In some embodiments, the signal peptide is present upstream (N-terminus or amino-terminus) of one or more polypeptides in a multisubunit peptide. In some embodiments, the signal peptide may be present on the N- terminus of all or some polypeptides in a multisubunit peptide. In some embodiments, the signal peptide is present on the N-terminus of the first polypeptide in a multisubunit peptide. In some embodiments, the signal peptide is present upstream (N-terminus) of some polypeptides in a multisubunit peptide. In some embodiments, the signal peptide is present upstream (N-terminus) of each of the polypeptides in a multisubunit peptide. In some embodiments, the signal peptide transports the receptor binding domain, polypeptide or multisubunit peptide, as applicable, to cell organelles. In some embodiments, the signal peptide transports the receptor binding domain, polypeptide or multisubunit peptide to golgi body or golgi apparatus / complex. In some embodiments, the signal peptide transports the receptor binding domain to cell organelles, preferably golgi body. In some embodiments, the signal peptide transports the polypeptide to cell organelles, preferably golgi body. In some embodiments, the signal peptide transports the multisubunit peptide to cell organelles, preferably golgi body. In some embodiments, the signal peptide transports the receptor binding domain, polypeptide or multisubunit peptide to golgi body via endoplasmic reticulum. Any signal peptide that transports the receptor binding domain, polypeptide or multisubunit peptide to golgi bodies can be employed in accordance with the present disclosure. In some embodiments, the signal peptide is a golgi targeting signal peptide i.e., directs the receptor binding domain, polypeptide or multisubunit peptide ultimately to golgi complex. Exemplary signal peptide includes, but not limited to, the one represented by the following amino acid sequence or comparable equivalents, or a combination thereof, including their codon optimized nucleic acid sequences, fragments, mutants, variants, or functional analogs thereof: MPSSVSWGILLLAGLCCLVPVSLAEDPQGDAA (SEQ ID NO: 74); MGSSVSWGILLLAGLCCLVPVSLAEDPQGDAA (SEQ ID NO: 75); MASSVSWGILLLAGLCCLVPVSLAEDPQGDAA (SEQ ID NO: 76); MDMRAPAGIFGFLLVLFPGYRS (SEQ ID NO: 77); MKWVTFISLLFLFSSAYS (SEQ ID NO: 78); MDWTWRVFCLLAVTPGAHP (SEQ ID NO: 79); MAWSPLFLTLITHCAGSWA (SEQ ID NO: 80); MTRLTVLALLAGLLASSRA (SEQ ID NO: 81); MARPLCTLLLLMATLAGALA (SEQ ID NO: 82); MRSLVFVLLIGAAFA (SEQ ID NO: 83); MSRLFVFILIALFLSAIIDVMS (SEQ ID NO: 84); MGMRMMFIMFMLVVLATTVVS (SEQ ID NO: 85); MRAFLFLTACISLPGVFG (SEQ ID NO: 86); MKFQSTLLLAAAAGSALA (SEQ ID NO: 87); MASSLYSFLLALSIVYIFVAPTHS (SEQ ID NO: 88); MKTHYSSAILPILTLFVFLSINPSHG (SEQ ID NO: 89); MESVSSLFNIFSTIMVNYKSLVLALLSVSNLKYARG (SEQ ID NO: 90); MKAAQILTASIVSLLPIYTSA (SEQ ID NO: 91); MIKLKFGVFFTVLLSSAYA (SEQ ID NO: 92); MGVKVLFALICIAVAEA (SEQ ID NO: 93). In some embodiments, the signal peptide shares at least 50% identity with the sequence disclosed herein above or comparable equivalents, or a combination thereof, including their codon optimized nucleic acid sequences, fragments, mutants, variants, or functional analogs thereof. Given the disclosed amino acid sequences of the signal peptide, a person skilled in the art would be able to deduce all possible DNA or RNA sequences that encodes the above signal peptide. Such DNA or RNA sequences are deemed to be incorporated in this disclosure. In some embodiments, the signal peptide is encoded by a nucleic acid sequence which may be either a DNA, an RNA, or an mRNA. In some embodiments, the signal peptide is encoded by a signal sequence which may be either a DNA, an RNA, or an mRNA. Synthesis of nucleic acid sequences Nucleic acid sequence according to the present disclosure can be either a DNA, an RNA, or an mRNA. The nucleic acid sequence as described herein can be synthesized by molecular biology or genetic engineering techniques well known in the art, for example, using recombinant expression system, chemical synthesis, or in vitro transcription (IVT). In some embodiments, the nucleic acid sequence is obtained or synthesized through a single IVT process or step. In some embodiments, the nucleic acid sequence obtained or synthesized through single IVT process or step is an mRNA. In some embodiments, the nucleic acid sequence is a messenger RNA (mRNA). The mRNA encodes a multisubunit peptide as described herein. Typically, an mRNA includes at least a coding region (which encodes the multisubunit peptide), a 5’ UTR, a 3’ UTR, a 5’ cap and a 3’ poly(A) tail. UTR (untranslated regions) flanks the coding region or open reading frame (ORF). The 5’ UTR and the 3’ UTR are sections of the mRNA before the start codon and after the stop codon respectively. The 5’ UTR has a cap (5’ cap) consisting of altered nucleotides. mRNA also contains a polyadenylated region at its 3’ end having adenine nucleotides called poly(A) tail. In some embodiments, the mRNA is unmodified or modified or a combination of both. The modification may be in the nucleobase of the nucleotide, or sugar moiety of the nucleotide, or the phosphate of the nucleotide. In some embodiments, unmodified mRNA comprises naturally occurring nucleosides, for example, adenosine, guanosine, cytidine, and uridine. mRNA comprises one or more modified nucleosides, for example, adenosine analog, guanosine analog, cytidine analog, or uridine analog. In some embodiments, the one or more modified nucleosides is a nucleoside analog selected from 2-aminoadenosine, 3-methyl adenosine, 7-deazaadenosine, 7-deazaguanosine, 8-oxoadenosine, or 8-oxoguanosine or a combination thereof. In some embodiments, the one or more modified nucleosides is a uridine analog selected from propynyl-uridine, pseudouridine, C5-bromouridine, C5-fluorouridine, C5- iodouridine, C5-propynyl-uridine, 5-aza-uridine, 2-thio-5-aza-uridine, 2-thio-uridine, 4- thio-pseudouridine, 2-thio-pseudouridine, 5-hydroxy-uridine, 3-methyl-uridine, 5- carboxymethyl-uridine, 1-carboxymethyl-pseudouridine, 1-methyl-3-(3-amino-3- carboxypropyl)pseudouridine, 2-thio-2’-O-methyl-uridine, 5-methoxycarbonylmethyl-2’- O-methyl-uridine, 5-carboxymethylaminomethyl-2’-O-methyl-uridine, 3,2’-O-dimethyl- uridine, 5-propynyl-uridine, 1-propynyl-pseudouridine, 5-taurinomethyl-uridine, 1- taurinomethyl-pseudouridine, 5-taurinomethyl-2-thio-uridine, 1-taurino-4-thio- pseudouridine, 1-methyl-pseudouridine, 4-thio-1-methyl-pseudouridine, 2-thio-1-methyl- pseudouridine, 1-methyl-1deaza-pseudouridine, 2-thio-1-methyl-1-deaza-pseudouridine, dihydro-uridine, dihydro-pseudouridine, 2-thio-dihydro-uridine, 2-thio-dihydro- pseudouridine, 2-methoxy-uridine, 2-methoxy-4-thio-uridine, 4-methoxy-pseudouridine, or 4-methoxy-2-thio-pseudouridine, or a combination thereof. In some embodiments, the one or more modified nucleosides is a cytidine analog selected from 5-methylcytidine, C5-propynyl-cytidine, C5-methylcytidine, pseudoisocytidine, 1-methyl-pseudoisocytidine, pyrrolo-pseudoisocytidine, 4-thio- pseudoisocytidine, 4-thio-1-methyl-pseudoisocytidine, 4-thio-1-methyl-1-deaza- pseudoisocytidine, 1-methyl-1-1deaza-pseudoisocytidine, 4-methoxy-1-methyl- pseudoisocytidine, or a combination thereof. Methods for making modified nucleosides are well known in the art. In some embodiments, the modified nucleoside is pseudouridine, for example, 1- methyl-pseudouridine, 1-propynyl-pseudouridine, 1-carboxymethyl-pseudouridine, 1- methyl-3-(3-amino-3-carboxypropyl)pseudouridine, 4-methoxy-pseudouridine, or 4- methoxy-2-thio-pseudouridine 4-thio-pseudouridine, 2-thio-pseudouridine, 4-thio-1- methyl-pseudouridine, 2-thio-1-methyl-pseudouridine, dihydro-pseudouridine, or a combination thereof. In some embodiments, mRNA is produced using recombinant expression system, chemically synthesized, or obtained through in vitro transcription. In some embodiments, the nucleic acid sequence is obtained through a single IVT process. mRNAs according to the present disclosure may be synthesized via in vitro transcription (IVT). Briefly, IVT is typically performed with a DNA template containing a promoter, a pool of ribonucleotide triphosphates, a buffer system that may include DTT and magnesium ions, and an appropriate RNA polymerase (e.g., T3, T7, or SP6 RNA polymerase), DNase I, pyrophosphatase, and / or RNase inhibitor. The exact conditions may vary according to the specific application. Methods of making mRNA through IVT reaction is well known in the art (see for example, Beckert, Bertrand and Masquida, Benoit Methods in Molecular Biology (2011) 703, 29-41; Brunelle, Julie L. and Green Rachel Methods in Enzymology (2013) 530, 101-114; Kamakaka, Rohinton T. and Kraus W. Lee Current Protocols in Cell Biology (1999) 11.6.1-11.6.17; Kanwal, Fariha et al. Cellular Physiology and Biochemistry (2018) 48:1915-1927; WO2018157153; WO2020185811; WO2022082001). In some embodiments, the in vitro transcription occurs in a single batch. In some embodiments, IVT reaction includes capping and tailing reactions either co-transcriptionally or separately. A cap analog is added to the in vitro transcription reaction and will be incorporated at the 5’ end of the mRNA during the reaction. Alternative method of capping involves adding the cap post-transcriptionally through an enzymatic reaction. The poly (A) tail can be incorporated into the DNA template sequence, and thus the poly (A) tail will be incorporated into the mRNA by T7 RNA polymerase during the in vitro transcription. Alternative method of tailing involves adding the poly (A) tail post-transcriptionally through an enzymatic reaction. In some embodiments, capping and tailing reactions are performed co-transcriptionally i.e., during the IVT reaction. In some embodiments, capping and tailing reactions are performed separately from IVT reaction i.e., post transcriptionally. mRNA produced as a result of IVT reaction may be purified using techniques well known in the art, such as, centrifugation, filtration and / or chromatographic techniques. The purification of mRNA may be accomplished before capping and tailing steps are performed or after capping and tailing. The synthesized mRNA may be purified by ethanol precipitation or filtration or chromatography methods. In some embodiments, tangential flow filtration is used to purify mRNA. In some embodiments, mRNA is purified by chromatographic step. In other embodiments, mRNA is purified by a combination of filtration and chromatography steps. In some embodiments, a suitable mRNA sequence is an mRNA sequence encoding a protein, peptide, polypeptide. In some embodiments, a suitable mRNA sequence is codon optimized for efficient expression in a host cell or organism. Codon optimization typically includes modifying a naturally-occurring or wild-type nucleic acid sequence encoding a peptide, polypeptide, or protein to achieve the highest possible expression of peptide, polypeptide, protein, or an antibody without altering the amino acid sequence. In some embodiments, the mRNA is circular. In other embodiments, the mRNA is linear. In some embodiments, the mRNA is self-amplifying or self-replicating. In some embodiments, mRNA is few hundred nucleotides long to several thousand nucleotides long. In some embodiments, mRNA is about 0.3 kb, 0.4 kb, 0.5 kb, 0.6 kb, 0.7 kb, 0.8 kb, 0.9 kb, 1 kb, 1.5 kb, 2 kb, 2.5 kb, 3 kb, 3.5 kb, 4 kb, 4.5 kb, 5 kb, 5.5 kb, 6 kb, 6.5 kb, 7.0 kb, 7.5 kb, 8 kb, 8.5 kb, 9 kb, 9.5 kb, 10 kb, 10.5 kb, 11 kb, 11.5 kb, 12 kb, 12.5 kb, 13 kb, 13.5 kb, 14 kb, 14.5 kb, 15 kb, 16 kb, 17 kb, 18 kb, 19 kb, 20 kb, 21 kb, 22 kb, 23 kb, 24 kb, 25 kb, 26 kb, 27 kb, 28 kb, 29 kb, 30 kb in length, or a fraction thereof. In some embodiments, mRNA is about 0.3 to 30 kb, 0.3 to 25 kb, 0.3 to 20 kb in length, or any range therein. In some embodiments, mRNA is about 0.3 to 20 kb, 0.3 to 18 kb, 0.3 to 16 kb, 0.3 to 14 kb, 0.3 to 12 kb, 0.3 to 10 kb, 0.3 to 9 kb, 0.3 to 8 kb, 0.3 to 7 kb, 0.3 to 6 kb, 0.3 to 5 kb in length, or any range therein. In some embodiments, mRNA is about 0.3 kb to about 1 kb, about 1 kb to about 2 kb, about 2 kb to about 3 kb, about 3 kb to about 4 kb, about 4 kb to about 5 kb, about 5 kb to about 6 kb, about 6 kb to about 7 kb, about 7 kb to about 8 kb, about 8 kb to about 9 kb, about 9 kb to about 10 kb, about 10 kb to about 11 kb, about 11 kb to about 12 kb, about 12 kb to about 13 kb, about 13 kb to about 14 kb, about 14 kb to about 15 kb, about 15 kb to about 16 kb, about 16 kb to about 17 kb, about 17 kb to about 18 kb, about 18 kb to about 19 kb, about 19 kb to about 20 kb, about 20 kb to about 21 kb, about 21 kb to about 22 kb, about 22 kb to about 23 kb, about 23 kb to about 24 kb, about 24 kb to about 25 kb, about 25 kb to about 26 kb, about 26 kb to about 27 kb, about 27 kb to about 28 kb, about 28 kb to about 29 kb, or about 29 kb to about 30 kb in length, or any range therein. In some embodiments, the nucleic acid, for example mRNA, encodes a receptor binding domain. In some embodiments, the nucleic acid, for example mRNA, encodes a polypeptide. In some embodiments, the nucleic acid, for example mRNA, encodes a multisubunit peptide. Polypeptide nanoparticle A polypeptide nanoparticle is formed by self-assembly of polypeptides. In some embodiments, a polypeptide nanoparticle may comprise homologous polypeptides, heterologous polypeptides, oligomeric complexes, or a combination thereof. In some embodiments, the polypeptide nanoparticle comprises homologous polypeptides. In some embodiments, the polypeptide nanoparticle comprises heterologous polypeptides. In some embodiments, the polypeptide nanoparticle comprises oligomeric complex. In some embodiments, the polypeptide disclosed herein comprise a receptor binding domain, a self-assembling peptide, and a linker peptide connecting the receptor binding domain with the self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, multisubunit peptide comprises multiple repeats of polypeptides comprising either a receptor binding domain, a linker peptide, and a self- assembling peptide or a linker peptide, a receptor binding domain, a linker peptide, and a self-assembling peptide, or a combination thereof, interspersed with cleavage peptide (see illustration in figure 1). In some embodiments, the total number of polypeptides present in a multisubunit peptide are up to 100 polypeptides. In some embodiments, one or more polypeptides in the multisubunit peptide has identical receptor binding domains (homologous polypeptides). In some embodiments, one or more polypeptides in the multisubunit peptide has different receptor binding domains (heterologous polypeptides). A multisubunit peptide as described herein is encoded by the nucleic acid sequence as disclosed herein. Each multisubunit peptide comprises two or more polypeptides, wherein some or all polypeptides comprises either a receptor binding domain, a linker peptide, and a self-assembling peptide or a linker peptide, a receptor binding domain, a linker peptide, and a self-assembling peptide or a combination thereof, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. The polypeptides are connected with each other through a cleavage peptide. In some embodiments, the multisubunit peptide includes a signal peptide upstream (N-terminus) of one or more polypeptides. In some embodiments, the multisubunit peptide includes a signal peptide upstream (N-terminus) of each of all or some polypeptides. In some embodiments, the multisubunit peptide optionally includes a signal peptide upstream (N-terminus) of each polypeptide. In some embodiments, the multisubunit peptide includes a signal peptide upstream (N- terminus) of some polypeptides. In some embodiments, the multisubunit peptide includes a signal peptide upstream (N-terminus) of all polypeptides. In some embodiments, polypeptide includes one or more signal peptides upstream (N-terminus) of the polypeptide. In some embodiments, the signal peptide transports the polypeptide outside the cell. In some embodiments, the signal peptide transports the polypeptide or the multisubunit peptide to golgi body or golgi apparatus. In some embodiments, the cellular proteases act on the cleavage site(s) present in the cleavage peptide or the cleavage peptide undergoes self-cleavage and cleaves the multisubunit peptide into individual polypeptides comprising either a receptor binding domain, a linker peptide, and a self-assembling peptide, or a linker peptide, a receptor binding domain, a linker peptide, and a self-assembling peptide, or a signal peptide, a receptor binding domain, a linker peptide, and a self-assembling peptide, or a signal peptide, a linker peptide, a receptor binding domain, a linker peptide, and a self-assembling peptide, or a combination thereof, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, the polypeptides may additionally also have some residues (amino acids) of cleavage peptide. In some embodiments, the linker peptide is an amino acid linker, a foldon, a scaffold, or a combination thereof. In some embodiments, the polypeptides are homologous polypeptides. In some embodiments, two or more homologous polypeptides or two or more heterologous polypeptides organise to form an oligomeric complex. In some embodiments, the oligomeric complex comprises at least two homologous polypeptides, at least three homologous polypeptides, at least four homologous polypeptides, at least five homologous polypeptides, at least six homologous polypeptides and so on. In some embodiments, the oligomeric complex comprises at least two heterologous polypeptides, at least three heterologous polypeptides, at least four heterologous polypeptides, at least five heterologous polypeptides, at least six heterologous polypeptides and so on. In some embodiments, the polypeptides are heterologous polypeptides. A polypeptide nanoparticle is formed by self-assembly of two or more homologous polypeptides, or two or more heterologous polypeptides, one or more oligomeric complexes, or their combination. In some embodiments, a polypeptide nanoparticle comprises homologous polypeptides, heterologous polypeptides, oligomeric complexes, or a combination thereof. In some embodiments, the polypeptide nanoparticles are symmetrical, non- symmetrical, asymmetrical, or a combination thereof. In some embodiments, the polypeptide nanoparticles are icosahedral, helical, spherical, rod-like or a combination thereof. In some embodiments, the polypeptide nanoparticles are enveloped or non- enveloped or a combination thereof. In some embodiments, the polypeptide nanoparticles are single layered or multi- layered or a combination thereof. In some of the embodiments, the polypeptide nanoparticle comprises at least 2 or up to 500 polypeptides. In some embodiments, the polypeptide nanoparticle comprises polypeptides between 2-5, 2-10, 2-20, 20-40, 40-60, 60-80, 80-100, 100-120, 120-140, 140-160, 160-180, 180- 200, 200-220, 220-240, 240-260, 260-280, 280-300, 300-320, 320-340, 340-360, 360-380, 380-400, 400-420, 420-440, 440-460, 460-480, or 480-500. In some embodiments, the polypeptide nanoparticle comprises polypeptides between 2-5, 2-10, 2-10, 10-20, 20-30, 30-40, 40-50, 50-60, 60-70, 70-80, 80-90, or 90-99. In one of the embodiments, the polypeptide nanoparticle comprises at least 2 or up to 500 homologous polypeptides. In some embodiments, the polypeptide nanoparticle comprises at least 2 or up to 500 heterologous polypeptides. In some embodiments, the polypeptide nanoparticle comprises two or more oligomeric complexes such that total number of polypeptides in the polypeptide nanoparticle are not more than 500. In some embodiments, the polypeptide nanoparticle comprises some homologous polypeptides and some heterologous polypeptides such that the total number of polypeptides in the polypeptide nanoparticle are not more than 500. In some embodiments, the polypeptide nanoparticle comprises some homologous polypeptides and some oligomeric complexes such that the total number of polypeptides in the polypeptide nanoparticle are not more than 500. In some embodiments, the polypeptide nanoparticle comprises some heterologous polypeptides and some oligomeric complexes such that the total number of polypeptides in the polypeptide nanoparticle are not more than 500. In some embodiments, the polypeptide nanoparticle comprises some homologous polypeptides, some heterologous polypeptides, some oligomeric complexes, or their combination such that the total number of polypeptides in the polypeptide nanoparticle are not more than 500. Lipid nanoparticles (LNP) composition The nucleic acid sequences as described herein may be encapsulated or formulated in a lipid nanoparticle composition. In some embodiments, the lipid nanoparticle composition comprises lipid components, ionizable polymer, or a combination thereof and a nucleic acid sequence as described herein. In some embodiments, the lipid nanoparticle composition comprises lipid components such as a cationic lipid, a phospholipid, a sterol, a PEG-lipid and a nucleic acid sequence as described herein. In another embodiment, the lipid nanoparticle composition comprises an ionizable polymer, a cationic lipid, a phospholipid, a sterol, a PEG-lipid and a nucleic acid sequence as described herein. In some embodiments, a vaccine comprising the lipid nanoparticle composition is provided herein. Lipid Components Lipid components of the lipid nanoparticle compositions may include one or more lipids, such as a cationic lipid, a phospholipid, a sterol, and a PEG-lipid. Cationic lipid Cationic lipid refers to a lipid that has a net positive charge at a selected pH. Cationic lipids generally comprises a hydrophilic head group that carries the charge and a hydrophobic tail. In some embodiments, the cationic lipid is a cationic lipid with an amine head group. The amine head group can be primary, secondary, tertiary or quaternary. The cationic lipid may comprise one (monoamine) or more (polyamine) such amine groups. In some embodiments, the cationic lipids are positively charged at pH below the pKa of the cationic lipid. In certain embodiments, the cationic lipids are neutral i.e., when pH is same or above the pKa of the cationic lipid. In some embodiments, the cationic lipids are positively charged at acidic pH i.e., pH 1.0 to pH 6.9. In certain embodiments, the cationic lipids are neutral at certain pH i.e., around physiological pH (pH 7.0 to pH 7.5). A cationic lipid that can exist in a positively charged or neutral form depending on the pH is commonly referred to as ionizable lipid. In some embodiments, the cationic lipids are ionizable such that they can exist in a positively charged or neutral form depending on the pH. In some embodiments, the cationic lipids are positively charged irrespective of the pH. In some embodiments, the cationic lipid present in the lipid nanoparticle composition comprises a cationic lipid disclosed in US provisional applications viz., 63 / 575930, 63 / 575934, 63 / 575938, 63 / 575939, and 63 / 575942 or their corresponding PCT application numbers viz., PCT / US2025 / 023592, PCT / US2025 / 023597, PCT / US2025 / 023602, PCT / US2025 / 023605, and PCT / US2025 / 023607 respectively. In some embodiments, the cationic lipid present in the lipid nanoparticle composition comprises a cationic lipid represented by formula (I) formula (I) or isomer, or salt thereof, wherein: R1 and R2 are independently chosen from H, -OH, C1-10 alkyl, C2-10 alkenyl, C2-10 alkynyl, saturated or unsaturated C3-10 cycloalkyl, C6-10 aryl, saturated or unsaturated C3-10 heterocycloalkyl containing 1-4 heteroatoms, C5-10heteroaryl containing 1-4 heteroatoms, - O-L7-R5, and -NR6R7, or R1 and R2 may combine together to form a saturated or unsaturated C3-10 cycloalkyl, C6-10 aryl, saturated or unsaturated C3-10heterocycloalkyl containing 1-4 heteroatoms, or C5-10heteroaryl containing 1-4 heteroatoms; R3 and R4 are independently chosen from branched or unbranched C1-26 alkyl, C2-26 alkenyl, C2-26alkynyl, –(CH2)m-A-(CH2)n-(CH3)y, and -CH((CH2)m-A-(CH2)n-(CH3)y)2, wherein each of m, n, and y is independently an integer ranging from 0 to 26; R5, R6, and R7 are independently chosen from H, -OH, C1-10 alkyl, C2-10 alkenyl, C2-10 alkynyl, saturated or unsaturated C3-10cycloalkyl, C6-10aryl, saturated or unsaturated C3-10heterocycloalkyl containing 1-4 heteroatoms, and C5-10heteroaryl containing 1-4 heteroatoms; each of L1, L2, L3, L4, L5, L6, and L7 is either absent or independently chosen from C1-10 alkylene, C2-10alkenylene, and C2-10alkynylene; X1 and X2 are independently chosen from -C(O)O-, -OC(O)-, -C(O)NH-, -NHC(O)-, - C(S)NH-, -NHC(S)-, -C(S)O-, -OC(S)-, -OC(O)NH-, -NHC(O)O-, -OP(O)(OH)O-, and - OP(O)(O-)O-; A is H, a bond, saturated or unsaturated C3-10cycloalkyl, C6-10aryl, saturated or unsaturated C3-10 heterocycloalkyl containing 1-4 heteroatoms, or C5-10 heteroaryl containing 1-4 heteroatoms; C(S)O-, -OC(S)-, -OC(O)NH-, -NHC(O)O-, -OP(O)(OH)O-, S, or N provided that when A1 is -CH2-, -C(O)O-, -OC(O)-, -C(O)NH-, -NHC(O)-, -C(S)NH-, -NHC(S)-, -C(S)O-, -OC(S)- , -OC(O)NH-, -NHC(O)O-, -OP(O)(OH)O-, or S, one of R1or R2is absent; and wherein each alkyl, alkenyl, alkynyl, alkylene, alkenylene, alkynylene, cycloalkyl, aryl, heterocycloalkyl, or heteroaryl is independently optionally substituted with one or more substituent. In some embodiments, the cationic lipid present in the lipid nanoparticle composition comprises a cationic lipid represented by formula (II) formula (II) or isomer, or salt thereof, wherein: represents either a single bond or a double bond; R1 and R2 are independently chosen from H, -OH, C1-10 alkyl, C2-10 alkenyl, C2-10 alkynyl, saturated or unsaturated C3-10 cycloalkyl, C6-10 aryl, saturated or unsaturated C3-10 heterocycloalkyl containing 1-4 heteroatoms, C5-10heteroaryl containing 1-4 heteroatoms, - O-L7-R5, and -NR6R7, or R1 and R2 may combine together to form a saturated or unsaturated C3-10 cycloalkyl, C6-10 aryl, saturated or unsaturated C3-10heterocycloalkyl containing 1-4 heteroatoms, or C5-10heteroaryl containing 1-4 heteroatoms; R3 and R4 are independently chosen from, branched or unbranched, C1-26 alkyl, C2-26 alkenyl, C2-26 alkynyl, –(CH2)m-A-(CH2)n-(CH3)y, and -CH((CH2)m-A-(CH2)n-(CH3)y)2, wherein each of m, n, and y is independently an integer ranging from 0 to 26; R5, R6, and R7 are independently chosen from H, -OH, C1-10 alkyl, C2-10 alkenyl, C2-10 alkynyl, saturated or unsaturated C3-10 cycloalkyl, C6-10 aryl, saturated or unsaturated C3-10 heterocycloalkyl containing 1-4 heteroatoms, and C5-10heteroaryl containing 1-4 heteroatoms; each of L1, L2, L3, L4, L5, L6, and L7 is either absent or independently chosen from C1-10 alkylene, C2-10alkenylene, and C2-10alkynylene; X1and X2are independently chosen from -C(O)O-, -OC(O)-, -C(O)NH-, -NHC(O)-, - C(S)NH-, -NHC(S)-, -C(S)O-, -OC(S)-, -OC(O)NH-, -NHC(O)O-, -OP(O)(OH)O-, and - OP(O)(O-)O-; A is H, a bond, saturated or unsaturated C3-10cycloalkyl, C6-10aryl, saturated or unsaturated C3-10 heterocycloalkyl containing 1-4 heteroatoms, or C5-10 heteroaryl containing 1-4 heteroatoms; C(S)O-, -OC(S)-, -OC(O)NH-, -NHC(O)O-, -OP(O)(OH)O-, S, or N provided that when A1 is -CH2-, -C(O)O-, -OC(O)-, -C(O)NH-, -NHC(O)-, -C(S)NH-, -NHC(S)-, -C(S)O-, -OC(S)- , -OC(O)NH-, -NHC(O)O-, -OP(O)(OH)O-, or S, one of R1or R2is absent; and wherein each alkyl, alkenyl, alkynyl, alkylene, alkenylene, alkynylene, cycloalkyl, aryl, heterocycloalkyl, or heteroaryl is independently optionally substituted with one or more substituent. In some embodiments, the cationic lipid present in the lipid nanoparticle composition comprises a cationic lipid represented by formula (III) formula (III) or isomer, or salt thereof, wherein: R1 and R2 are independently chosen from H, -OH, C1-10 alkyl, C2-10 alkenyl, C2-10 alkynyl, saturated or unsaturated C3-10cycloalkyl, C6-10aryl, saturated or unsaturated C3-10heterocycloalkyl containing 1-4 heteroatoms, C5-10 heteroaryl containing 1-4 heteroatoms, - O-L7-R5, and -NR6R7, or R1and R2may combine together to form a saturated or unsaturated C3-10cycloalkyl, C6-10aryl, saturated or unsaturated C3-10heterocycloalkyl containing 1-4 heteroatoms, or C5-10heteroaryl containing 1-4 heteroatoms; R3 and R4 are independently chosen from branched or unbranched C1-26 alkyl, C2-26 alkenyl, C2-26alkynyl, –(CH2)m-A-(CH2)n-(CH3)y, and -CH((CH2)m-A-(CH2)n-(CH3)y)2, wherein each of m, n, and y is independently an integer ranging from 0 to 26; R5, R6, and R7 are independently chosen from H, -OH, C1-10 alkyl, C2-10 alkenyl, C2-10 alkynyl, saturated or unsaturated C3-10cycloalkyl, C6-10aryl, saturated or unsaturated C3-10 heterocycloalkyl containing 1-4 heteroatoms, and C5-10heteroaryl containing 1-4 heteroatoms; each of L1, L2, L3, L4, L5 L6, and L7 is either absent or independently chosen from C1-10 alkylene, C2-10alkenylene, and C2-10alkynylene; X1 and X2 are independently chosen from -C(O)O-, -OC(O)-, -C(O)NH-, -NHC(O)-, - C(S)NH-, -NHC(S)-, -C(S)O-, -OC(S)-, -OC(O)NH-, -NHC(O)O-, -OP(O)(OH)O-, and - OP(O)(O-)O-; A is H, a bond, saturated or unsaturated C3-10 cycloalkyl, C6-10 aryl, saturated or unsaturated C3-10 heterocycloalkyl containing 1-4 heteroatom, or C5-10 heteroaryl containing 1-4 heteroatom; C(S)O-, -OC(S)-, -OC(O)NH-, -NHC(O)O-, -OP(O)(OH)O-, S, or N provided that when A1 is -CH2-, -C(O)O-, -OC(O)-, -C(O)NH-, -NHC(O)-, -C(S)NH-, -NHC(S)-, -C(S)O-, -OC(S)- , -OC(O)NH-, -NHC(O)O-, -OP(O)(OH)O-, or S, one of R1or R2is absent; and wherein each alkyl, alkenyl, alkynyl, alkylene, alkenylene, alkynylene, cycloalkyl, aryl, heterocycloalkyl, or heteroaryl is independently optionally substituted with one or more substituent. In some embodiments, the cationic lipid present in the lipid nanoparticle composition comprises a cationic lipid represented by formula (IV) formula (IV) or isomer, or salt thereof, wherein: represents either a single bond or a double bond; R1 and R2 are independently chosen from H, -OH, C1-10 alkyl, C2-10 alkenyl, C2-10 alkynyl, saturated or unsaturated C3-10 cycloalkyl, C6-10 aryl, saturated or unsaturated C3-10 heterocycloalkyl containing 1-4 heteroatoms, C5-10heteroaryl containing 1-4 heteroatoms, - O-L7-R5, and -NR6R7, or R1and R2may combine together to form a saturated or unsaturated C3-10cycloalkyl, C6-10aryl, saturated or unsaturated C3-10 heterocycloalkyl containing 1-4 heteroatoms, or C5-10 heteroaryl containing 1-4 heteroatoms; R3and R4are independently chosen from branched or unbranched C1-26alkyl, C2-26alkenyl, C2-26 alkynyl, –(CH2)m-A-(CH2)n-(CH3)y, and -CH((CH2)m-A-(CH2)n-(CH3)y)2, wherein each of m, n, and y is independently an integer ranging from 0 to 26; R5, R6, and R7are independently chosen from H, -OH, C1-10alkyl, C2-10alkenyl, C2-10alkynyl, saturated or unsaturated C3-10 cycloalkyl, C6-10 aryl, saturated or unsaturated C3-10 heterocycloalkyl containing 1-4 heteroatoms, and C5-10 heteroaryl containing 1-4 heteroatoms; each of L1, L2, L3, L4, L5, L6, and L7is either absent or independently chosen from C1-10alkylene, C2-10 alkenylene, and C2-10 alkynylene; X1 and X2 are independently chosen from -C(O)O-, -OC(O)-, -C(O)NH-, -NHC(O)-, - C(S)NH-, -NHC(S)-, -C(S)O-, -OC(S)-, -OC(O)NH-, -NHC(O)O-, -OP(O)(OH)O-, and - OP(O)(O-)O-; A is H, a bond, saturated or unsaturated C3-10 cycloalkyl, C6-10 aryl, saturated or unsaturated C3-10heterocycloalkyl containing 1-4 heteroatom, or C5-10heteroaryl containing 1-4 heteroatom; C(S)O-, -OC(S)-, -OC(O)NH-, -NHC(O)O-, -OP(O)(OH)O-, S, or N provided that when A1is -CH2-, -C(O)O-, -OC(O)-, -C(O)NH-, -NHC(O)-, -C(S)NH-, -NHC(S)-, -C(S)O-, -OC(S)- , -OC(O)NH-, -NHC(O)O-, -OP(O)(OH)O-, or S, one of R1 or R2 is absent; and wherein each alkyl, alkenyl, alkynyl, alkylene, alkenylene, alkynylene, cycloalkyl, aryl, heterocycloalkyl, or heteroaryl is independently optionally substituted with one or more substituent. In some embodiments, the cationic lipid present in the lipid nanoparticle composition comprises a cationic lipid represented by formula (V) formula (V) or isomer, or salt thereof, wherein: R3and R4are independently chosen from branched or unbranched C1-26alkyl, C2-26alkenyl, C2-26alkynyl, –(CH2)m-A-(CH2)n-(CH3)y, and -CH((CH2)m-A-(CH2)n-(CH3)y)2, wherein each of m, n, and y is independently an integer ranging from 0 to 26; (R10)q is chosen from H, -OH, optionally substituted C1-10 alkyl, C2-10 alkenyl, C2-10 alkynyl, saturated or unsaturated C3-10cycloalkyl, C6-10aryl, saturated or unsaturated C3-10heterocycloalkyl containing 1-4 heteroatoms, C5-10 heteroaryl containing 1-4 heteroatoms, - O-L7-R5, and -NR6R7, wherein q is an integer ranging from 0 to 5; R5, R6, and R7are independently chosen from H, -OH, C1-10alkyl, C2-10alkenyl, C2-10alkynyl, saturated or unsaturated C3-10cycloalkyl, C6-10aryl, saturated or unsaturated C3-10heterocycloalkyl containing 1-4 heteroatoms, and C5-10 heteroaryl containing 1-4 heteroatoms; each of L1, L2, L3, L4, and L7is either absent or independently chosen from C1-10alkylene, C2-10 alkenylene, and C2-10 alkynylene; X1 and X2 are independently chosen from -C(O)O-, -OC(O)-, -C(O)NH-, -NHC(O)-, - C(S)NH-, -NHC(S)-, -C(S)O-, -OC(S)-, -OC(O)NH-, -NHC(O)O-, -OP(O)(OH)O-, and - OP(O)(O-)O-; A is H, a bond, saturated or unsaturated C3-10 cycloalkyl, C6-10 aryl, saturated or unsaturated C3-10heterocycloalkyl containing 1-4 heteroatoms, or C5-10heteroaryl containing 1-4 heteroatoms; and wherein each alkyl, alkenyl, alkynyl, alkylene, alkenylene, alkynylene, cycloalkyl, aryl, heterocycloalkyl, heteroaryl is independently optionally substituted with one or more substituent. In some embodiments, the cationic lipid present in the lipid nanoparticle composition comprises a cationic lipid represented by formula (VI) formula (VI) or isomer, or salt thereof, wherein: R3 and R4 are independently chosen from branched or unbranched C1-26 alkyl, C2-26 alkenyl, C2-26 alkynyl, –(CH2)m-A-(CH2)n-(CH3)y, and -CH((CH2)m-A-(CH2)n-(CH3)y)2, wherein each of m, n, and y is independently an integer ranging from 0 to 26; each of L1, L2, L3, and L4is either absent or independently chosen from C1-10alkylene, C2-10alkenylene, and C2-10 alkynylene; X1and X2are independently chosen from -C(O)O-, -OC(O)-, -C(O)NH-, -NHC(O)-, - C(S)NH-, -NHC(S)-, -C(S)O-, -OC(S)-, -OC(O)NH-, -NHC(O)O-, -OP(O)(OH)O-, and OP(O)(O-)O-; A is H, a bond, saturated or unsaturated C3-10 cycloalkyl, C6-10 aryl, saturated or unsaturated C3-10heterocycloalkyl containing 1-4 heteroatoms, or C5-10heteroaryl containing 1-4 heteroatoms; and wherein each alkyl, alkenyl, alkynyl, alkylene, alkenylene, alkynylene, cycloalkyl, aryl, heterocycloalkyl, heteroaryl is independently optionally substituted with one or more substituent. In some embodiments, the cationic lipid present in the lipid nanoparticle composition comprises a cationic lipid represented by formula (VII) formula (VII) or isomer, or salt thereof, wherein: represents either a single bond or a double bond; R3and R4are independently chosen from, branched or unbranched, C1-26alkyl, C2-26alkenyl, C2-26 alkynyl, –(CH2)m-A-(CH2)n-(CH3)y, and -CH((CH2)m-A-(CH2)n-(CH3)y)2, wherein each of m, n, and y is independently an integer ranging from 0 to 26; (R10)qis chosen from H, -OH, -CH2OH, C1-10alkyl, C2-10alkenyl, C2-10alkynyl, saturated or unsaturated C3-10 cycloalkyl, C6-10 aryl, saturated or unsaturated C3-10 heterocycloalkyl containing 1-4 heteroatoms, C5-10 heteroaryl containing 1-4 heteroatoms, -O-L8-R5, and - NR6R7, wherein q is an integer ranging from 0 to 5; R5, R6, and R7 are independently chosen from H, -OH, C1-10 alkyl, C2-10 alkenyl, C2-10 alkynyl, saturated or unsaturated C3-10 cycloalkyl, C6-10 aryl, saturated or unsaturated C3-10 heterocycloalkyl containing 1-4 heteroatoms, and C5-10heteroaryl containing 1-4 heteroatoms; each of L1, L2, L3, L4, L5, L7, and L8 is either absent or independently chosen from C1-10 alkylene, C2-10 alkenylene, and C2-10 alkynylene; X1and X2are independently chosen from -C(O)O-, -OC(O)-, -C(O)NH-, -NHC(O)-, - C(S)NH-, -NHC(S)-, -C(S)O-, -OC(S)-, -OC(O)NH-, -NHC(O)O-, -OP(O)(OH)O-, and - OP(O)(O-)O-; A is H, a bond, saturated or unsaturated C3-10cycloalkyl, C6-10aryl, saturated or unsaturated C3-10heterocycloalkyl containing 1-4 heteroatoms, or C5-10heteroaryl containing 1-4 heteroatoms; Z is -CH2-, O, N, or S; A1is -CH2-, -C(O)O-, -OC(O)-, -C(O)NH-, -NHC(O)-, -C(S)NH-, -NHC(S)-, -C(S)O-, - OC(S)-, -OC(O)NH-, -NHC(O)O-, -OP(O)(OH)O-, S, or N; and wherein each alkyl, alkenyl, alkynyl, alkylene, alkenylene, alkynylene, cycloalkyl, aryl, heterocycloalkyl, or heteroaryl is independently optionally substituted with one or more substituent. In some embodiments, the cationic lipid present in the lipid nanoparticle composition comprises a cationic lipid represented by formula (VIII) formula (VIII) or isomer, or salt thereof, wherein: R3 and R4 are independently chosen from branched or unbranched C1-26 alkyl, C2-26 alkenyl, C2-26alkynyl, –(CH2)m-A-(CH2)n-(CH3)y, and -CH((CH2)m-A-(CH2)n-(CH3)y)2, wherein each of m, n, and y is independently an integer ranging from 0 to 26; (R10)q is chosen from H, -OH, -CH2OH, C1-10 alkyl, C2-10 alkenyl, C2-10 alkynyl, saturated or unsaturated C3-10cycloalkyl, C6-10aryl, saturated or unsaturated C3-10heterocycloalkyl containing 1-4 heteroatoms, C5-10 heteroaryl containing 1-4 heteroatoms, -O-L8-R5, and - NR6R7, wherein q is an integer ranging from 0 to 4; R5,R6, and R7are independently chosen from H, -OH, C1-10alkyl, C2-10alkenyl, C2-10alkynyl, saturated or unsaturated C3-10cycloalkyl, C6-10aryl, saturated or unsaturated C3-10heterocycloalkyl containing 1-4 heteroatoms, and C5-10 heteroaryl containing 1-4 heteroatoms; each of L1, L2, L3, L4, L5, L7, and L8is either absent or independently chosen from C1-10alkylene, C2-10 alkenylene, or C2-10 alkynylene; X1 and X2 are independently chosen from -C(O)O-, -OC(O)-, -C(O)NH-, -NHC(O)-, - C(S)NH-, -NHC(S)-, -C(S)O-, -OC(S)-, -OC(O)NH-, -NHC(O)O-, -OP(O)(OH)O-, and - OP(O)(O-)O-; A is H, a bond, saturated or unsaturated C3-10 cycloalkyl, C6-10 aryl, saturated or unsaturated C3-10heterocycloalkyl containing 1-4 heteroatoms, or C5-10heteroaryl containing 1-4 heteroatoms; Z is -CH2-, O, N, or S; A1 is -CH2-, -C(O)O-, -OC(O)-, -C(O)NH-, -NHC(O)-, -C(S)NH-, -NHC(S)-, -C(S)O-, - OC(S)-, -OC(O)NH-, -NHC(O)O-, -OP(O)(OH)O-, S, or N; and wherein each alkyl, alkenyl, alkynyl, alkylene, alkenylene, alkynylene, cycloalkyl, aryl, heterocycloalkyl, or heteroaryl is independently optionally substituted with one or more substituent. In some embodiments, the cationic lipid represented by formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), or formula (VIII) are substituted with substituents independently chosen from H, OH, Cl, Br, I, O, S, N, P, optionally substituted C1-6alkoxy, optionally substituted C1-6alkyl, optionally substituted C2-6 alkenyl, optionally substituted C2-6 alkynyl, optionally substituted saturated or unsaturated C3-10cycloalkyl, optionally substituted C6-10aryl, optionally substituted saturated or unsaturated C3-10 heterocycloalkyl containing 1-4 heteroatoms, optionally substituted C5-10 heteroaryl containing 1-4 heteroatoms or combination thereof. In some embodiments, substituent may further be substituted with H, -OH, Cl, Br, I, or C1-6 hydroxyalkyl. In some embodiments, N:P ratio or cationic lipid to nucleic acid ratio in LNP formulation is between 1 to 18, between 1 to 17, between 1 to 16, between 1 to 15, between 1 to 14, between 1 to 13, between 1 to 12, between 1 to 11, between 1 to 10, between 1 to 9, between 1 to 8, between 1 to 7, between 1 to 6, between 1 to 5, between 1 to 4, between 1 to 3, between 1 to 2, or any range therein. In some embodiments, N:P ratio or cationic lipid to nucleic acid ratio in LNP formulation is about 18, about 17, about 16, about 15, about 14, about 13, about 12, about 11, about 10, about 9, about 8, about 7, about 6, about 5, about 4, about 3, about 2, about 1, or any portion or fraction thereof. In some embodiments, other exemplary cationic lipids for use in the lipid nanoparticle compositions include, but are not limited to, N,N-dioleyl-N,N- dimethylammonium chloride (DODAC); N-(2,3-dioleyloxy)propyl)-N,N,N- trimethylammonium chloride (DOTMA); N,N-distearyl-N,N-dimethylammonium bromide(DDAB); N-(2,3dioleoyloxy)propyl)-N,N,N-trimethylammonium chloride (DOTAP); 3-(N—(N’,N’-dimethylaminoethane)-carbamoyl)cholesterol (DC-Chol), N-(l- (2,3-dioleoyloxy)propyl)N-2-(sperminecarboxamido)ethyl)-N,N- dimethylammoniumtrifluoracetate (DOSPA), dioctadecylamidoglycyl carboxyspermine (DOGS), 1,2-dioleoyl- 3-dimethylammonium propane (DODAP), N,N-dimethyl-2,3-dioleoyloxy)propylamine (DODMA), N-(1,2-dimyristyloxyprop-3-yl)-N,N-dimethyl-N-hydroxyethyl ammonium bromide (DMRIE), l,2-dilinoleyloxy-N,N-dimethylaminopropane (Dlin-DMA), 3- dimethylamino-2-(cholest-5-en-3-beta-oxybutan-4-oxy)-l-(cis,cis-9,12-oc- tadecadienoxy)propane (Clin-DMA), 2-[5’-(cholest-5-en-3-beta-oxy)-3’-oxapentoxy)-3- dimethyl-l-(cis,cis-9’,12’-octadecadienoxy)propane (CpLin-DMA), 2,3-Dilinoleoyloxy- N,N-dimethylpropylamine (Dlin-DAP), 1,2-N,N’-Dilinoleylcarbamyl-3- dimethylaminopropane (Dlincarb-DAP), l,2-Dilinoleoylcarbamyl-3-dimethylaminopropane (Dlin-CDAP), 2,2-dilinoleyl-4-dimethylaminomethyl-[l,3]-dioxolane (Dlin-K-DMA), heptatriaconta-6,9,28,31-tetraen-19-yl 4-(dimethylamino)butanoate (Dlin-MC3-DMA), heptadecane-9-yl 8-[2-hydroxyethyl-(6-oxo-6-undecoxyhexyl)amino]octanoate (SM-102), 6-[6-(2-hexyldecanoyloxy)hexyl-(4-hydroxybutyl)amino]hexyl 2-hexyldecanoate (ALC- 0315), nonyl 8-[(8-heptadecan-9-yloxy-8-oxooctyl)-(2-hydroxyethyl)amino]octanoate (SLP-0001), or a combination thereof. Methods of making cationic lipid and / or ionizable lipid or imparting the cationic lipid the ability to behave as an ionizable lipid are also disclosed in the art (WO2005121348; WO2009127060; WO2009086558; WO2010042877; WO2010144740; WO2011075656; WO2017049245; WO2017075531; WO2018118102; WO2015199952; Reynier P. et al. Journal of Drug Targeting (2004) 12: 25-38; Sabnis, Staci et al. Molecular Therapy (2018) 26: 1509-1519). In some embodiments, the cationic lipid present in the lipid nanoparticle composition comprises a cationic lipid disclosed in published patent application viz., WO2019 / 152557; WO2019 / 232095; WO2021 / 077067; WO2019 / 089828; US2019 / 0240354; US2010 / 0130588; US2021 / 0087135; US2021 / 0128488; US2020 / 0121809; US2013 / 0108685; US2013 / 0195920; US2015 / 0005363; US2014 / 0308304; US2017 / 0210697; and US2013 / 0053572. The proportion of cationic lipid present in the lipid nanoparticle compositions is from about 10 mol % to about 70 mol % or any range therein. In some embodiments, the proportion of cationic lipid present in the lipid nanoparticle compositions is from about 10 mol % to about 70 mol %, from about 10 mol % to about 65 mol %, from about 10 mol % to about 60 mol %, from about 10 mol % to about 55 mol %, from about 10 mol % to about 50 mol %, or any range therein. In some embodiments, the proportion of cationic lipid present in the lipid nanoparticle compositions is about 10 mol %, about 11 mol %, about 12 mol %, about 13 mol %, about 14 mol %, about 15 mol %, about 16 mol %, about 17 mol %, about 18 mol %, about 19 mol %, about 20 mol %, about 21 mol %, about 22 mol %, about 23 mol %, about 24 mol %, about 25 mol %, about 26 mol %, about 27 mol %, about 28 mol %, about 29 mol %, about 30 mol %, about 31 mol %, about 32 mol %, about 33 mol %, about 34 mol %, about 35 mol %, about 36 mol %, about 37 mol %, about 38 mol %, about 39 mol %, about 40 mol %, about 41 mol %, about 42 mol %, about 43 mol %, about 44 mol %, about 45 mol %, about 46 mol %, about 47 mol %, about 48 mol %, about 49 mol %, about 50 mol %, about 51 mol %, about 52 mol %, about 53 mol %, about 54 mol %, about 55 mol %, about 56 mol %, about 57 mol %, about 58 mol %, about 59 mol %, about 60 mol %, about 61 mol %, about 62 mol %, about 63 mol %, about 64 mol %, about 65 mol %, about 66 mol %, about 67 mol %, about 68 mol %, about 69 mol %, about 70 mol %, or any portion or fraction thereof. In some embodiments, the proportion of cationic lipid present in the lipid nanoparticle compositions is about 10 mol% to about 20 mol%, about 20 mol% to about 30 mol%, about 30 mol% to about 40 mol%, about 40 mol% to about 50 mol%, about 50 mol% to about 60 mol%, about 60 mol% to about 70 mol%, or any range therein. Phospholipids Phospholipid includes a lipid containing a hydrophilic head with a phosphate group and a hydrophobic tail composed of fatty acid chains attached to a glycerol or sphingosine backbone. Exemplary phospholipids for use in the lipid nanoparticle compositions include, but are not limited to, 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-distearoyl-sn-glycero-3- phosphocholine (DSPC), 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-dioleoyl-sn- glycero-3-phosphoethanolamine (DOPE), 1,2-diphytanoyl-sn-glycero-3- phosphoethanolamine (ME 16.0 PE), 1,2-distearoyl-sn-glycero-3-phosphoethanolamine, 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), 1-myristoyl-2-stearoyl-sn-glycero-3- phosphocholine (MSPC), 1-palmitoyl-2-myristoyl-sn-glycero-3-phosphocholine (PMPC), 1-palmitoyl-2-stearoyl-sn-glycero-3-phosphocholine (PSPC), 1-stearoyl-2-myristoyl-sn- glycero-3-Phosphocholine (SMPC), 1-Stearoyl-2-palmitoyl-sn-glycero-3-phosphocholine (SPPC), 1-stearoyl-2-oleoyl-sn-glycero-3-phosphocholine (SOPC), 1-stearoyl-2- docosahexaenoyl-sn-glycero-3-phosphocholine (SDPC), sphingomyelin, or a combination thereof. The proportion of phospholipid present in the lipid nanoparticle compositions is from about 2 mol % to about 65 mol %, from about 5 mol % to about 65 mol %, from about 10 mol % to about 65 mol %, from about 10 mol % to about 55 mol %, from about 10 mol % to about 50 mol %, or any range therein. In some embodiments, the proportion of phospholipid present in the lipid nanoparticle compositions is about 65 mol %, about 60 mol %, about 55 mol %, about 50 mol %, about 45 mol %, about 44 mol %, about 43 mol %, about 42 mol %, about 41 mol %, about 40 mol %, about 39 mol %, about 38 mol %, about 37 mol %, about 36 mol %, about 35 mol %, about 34 mol %, about 33 mol %, about 32 mol %, about 31 mol %, about 30 mol %, about 29 mol %, about 28 mol %, about 27 mol %, about 26 mol %, about 25 mol %, about 24 mol %, about 23 mol %, about 22 mol %, about 21 mol %, about 20 mol %, about 19 mol %, about 18 mol %, about 17 mol %, about 16 mol %, about 15 mol %, about 14 mol %, about 13 mol %, about 12 mol %, about 11 mol %, about 10 mol %, about 9 mol %, about 8 mol %, about 7 mol %, about 6 mol %, about 5 mol %, about 4 mol %, about 3 mol %, about 2 mol %, or any portion or fraction thereof. Sterol Lipid nanoparticle composition disclosed herein may include sterol and / or sterol derivatives. The term “sterol” as used herein include, but not limited to, cholesterol, sitosterol, fecosterol, ergosterol, campesterol, stigmasterol or their derivatives. In some embodiments, lipid nanoparticle composition comprises cholesterol and / or cholesterol derivatives. Non-limiting examples of cholesterol and cholesterol derivatives include 5α- cholestanol, 5β-coprostanol, cholesteryl-(2’-hydroxy)-ethyl ether, cholesteryl-(4’-hydroxy)- butyl ether, 6-ketocholestanol, 5α-cholestane, cholestenone, 5α-cholestanone, 5β- cholestanone, cholesteryl decanoate, or mixtures thereof. Methods of making cholesterol and cholesterol derivatives are well known in the art. The proportion of sterol present in the lipid nanoparticle compositions may be from about 20 mol % to about 65 mol % or any range therein. In some embodiments, the proportion of sterol present in the lipid nanoparticle compositions is from about 20 mol % to about 65 mol %, from about 25 mol % to about 65 mol %, from about 30 mol % to about 65 mol %, from about 31 mol % to about 60 mol %, from about 32 mol % to about 60 mol %, from about 33 mol % to about 60 mol %, from about 34 mol % to about 60 mol %, from about 35 mol % to about 60 mol %, or any range therein. In some embodiments, the proportion of sterol present in the lipid nanoparticle compositions is about 65 mol %, about 60 mol %, about 55 mol %, about 50 mol %, about 45 mol %, about 44 mol %, about 43 mol %, about 42 mol %, about 41 mol %, about 40 mol %, about 39 mol %, about 38 mol %, about 37 mol %, about 36 mol %, about 35 mol %, about 34 mol %, about 33 mol %, about 32 mol %, about 31 mol %, about 30 mol %, about 29 mol %, about 28 mol %, about 27 mol %, about 26 mol %, about 25 mol %, about 24 mol %, about 23 mol %, about 22 mol %, about 21 mol %, about 20 mol %, or any portion or fraction thereof. PEG-lipid The term PEG-lipid, pegylated lipid, PEG linked lipid, PEG conjugated lipid, PEG- lipid conjugate, PEG modified lipid have been used interchangeably to mean polyethylene glycol linked to a lipid moiety. The lipid moiety may be linked directly to the PEG molecule or through a linker. In some embodiments, a PEG-lipid comprises a PEG-modified phosphatidylethanolamines, PEG-modified phosphatidic acids, PEG-modified ceramides, PEG-modified dialkylamines, PEG-modified diacylglycerols, PEG-modified dialkylglycerols, and / or PEG-modified cholesterol, and / or mixtures thereof. The methods of making PEG-lipid are well known to persons skilled in the art. In some embodiments, PEG-lipid is selected from mPEG-Dimyristoyl glycerol (mPEG-DMG), mPEG-N,N-Ditetradecylacetamide (mPEG-DTA or ALC0159), mPEG- Cholesterol (mPEG-CLS), mPEG-DSPE, mPEG-DMPE, mPEG-DPPE, mPEG-DLPE, mPEG-DOPE, mPEG-DPPC, mPEG-DSPC, 1,2-Distearoyl-sn-Glycero-3- Phosphoethanolamine with conjugated methoxyl poly(ethylene glycol) (mPEG-DSPE), 1,2- dimyristoyl-rac-glycero-3-methoxypolyethylene glycol-2000 (mPEG2000-DMG), α-(3’- {[1,2-di(myristyloxy)propanoxy]carbonylamino}propyl)-ω-methoxy, polyoxyethylene (mPEG2000C-DMG), or mixtures thereof. The PEG moiety of the PEG-lipid may comprise an average molecular weight ranging from 0.5 kDa to 10 kDa. In some embodiments, the PEG-lipid has an average molecular weight of about 0.5 kDa to 5 kDa, about 0.5 kDa to 4 kDa, 0.5 kDa to 3 kDa, 0.5 kDa to 2 kDa. In preferred embodiments, the PEG-lipid has an average molecular weight of about 0.5 kDa to about 2 kDa. The proportion of PEG-lipid present in the lipid nanoparticle compositions may be from about 0.2 mol % to about 2.0 mol % or any range therein. In some embodiments, the proportion of PEG-lipid present in the lipid nanoparticle compositions is from about 0.2 mol % to about 2.0 mol %, from about 0.2 mol % to about 1.9 mol %, from about 0.2 mol % to about 1.8 mol %, from about 0.2 mol % to about 1.7 mol %, from about 0.2 mol % to about 1.6 mol %, from about 0.2 mol % to about 1.5 mol %, or any range therein. In some embodiments, the proportion of PEG-lipid present in the lipid nanoparticle compositions is about 0.2 mol %, about 0.3 mol %, about 0.4 mol %, about 0.5 mol %, about 0.6 mol %, about 0.7 mol %, about 0.8 mol %, about 0.9 mol %, about 1.0 mol %, about 1.1 mol %, about 1.2 mol %, about 1.3 mol %, about 1.4 mol %, about 1.5 mol %, about 1.6 mol %, about 1.7 mol %, about 1.8 mol %, about 1.9 mol %, about 2.0 mol %, or any portion or fraction thereof. In some embodiments, the lipid nanoparticle composition additionally contains an ionizable polymer. Ionizable polymer As used herein the term “polymer” means a compound formed from a plurality of repeating units called monomers. Polymers are produced through a process called polymerization wherein two or more monomers are linked through chemical bonds to form the polymer. In some embodiments, the polymer is branched or unbranched. In some embodiments, the polymer may be homopolymer, i.e., consisting of same type of repeat units or monomers, or heteropolymer, i.e., consisting of more than one type of repeat units or monomers. The terms heteropolymer and copolymer have been used interchangeably herein. The term “Ionizable polymer” as used herein means, a polymer that can exist in a positively charged or neutral form depending on the pH of the solution or environment, for example, ionizable polymer will be cationic (positively charged) when pH of the solution is below the pKa of the ionizable polymer and neutral (no charge) when pH of the solution is same or above the pKa of the ionizable polymer. In some embodiments, ionizable polymer is positively charge in acidic pH i.e., pH 1.0 to pH 6.9. In some embodiments, ionizable polymer is neutral (no charge) around physiological pH (pH 7.0 to pH 7.5). In some embodiments, the ionizable polymer is a biocompatible polymer or biodegradable polymer. The term “biocompatible polymer” and “biodegradable polymer” have been used interchangeably to mean a polymer that is substantially free from any deleterious effects when introduced into a living or biological system. Such polymers are capable of undergoing degradation when introduced into the living or biological systems and are not expected to produce significant toxicity or immunological response. In some embodiments, the lipid nanoparticle compositions comprise an ionizable polymer. The ionizable polymer may be selected from chitosan, chitosan derivatives, cellulose derivatives, poly-L-lysine (PLL), protamine, polyethyleneimine, their derivatives, or a combination thereof. In some embodiments, the ionizable polymer is positively charged at acidic pH i.e., pH 1.0 to 6.9 and is neutral around physiological pH (pH 7.0 to 7.5). The proportion of ionizable polymer present in the lipid nanoparticle compositions may be from about 1 mol % to about 25 mol %. In some embodiments, the proportion of ionizable polymer present in the lipid nanoparticle compositions is from about 1 mol % to about 25 mol %, from about 1 mol % to about 24 mol %, from about 1 mol % to about 23 mol %, from about 1 mol % to about 22 mol %, from about 1 mol % to about 21 mol %, from about 1 mol % to about 20 mol %, from about 1 mol % to about 19 mol %, from about 1 mol % to about 18 mol %, from about 1 mol % to about 17 mol %, from about 1 mol % to about 16 mol %, from about 1 mol % to about 15 mol %, or any range therein. In some embodiments, the proportion of ionizable polymer present in the lipid nanoparticle compositions is about 1 mol %, about 2 mol %, about 3 mol %, about 4 mol %, about 5 mol %, about 6 mol %, about 7 mol %, about 8 mol %, about 9 mol %, about 10 mol %, about 11 mol %, about 12 mol %, about 13 mol %, about 14 mol %, about 15 mol %, about 16 mol %, about 17 mol %, about 18 mol %, about 19 mol %, about 20 mol %, about 21 mol %, about 22 mol %, about 23 mol %, about 24 mol %, about 25 mol %, or any portion or fraction thereof. In some embodiments, the preferred ionizable polymer comprises chitosan, chitosan derivatives, cellulose derivatives, poly-L-lysine (PLL), protamine, polyethyleneimine, and / or their derivatives, or a combination thereof. Recombinant expression of receptor binding domain, polypeptide, and multisubunit peptide. The present disclosure also provides vectors carrying the nucleic acid disclosed herein and host cells transformed with such a vector, and expression of the nucleic acid to produce receptor binding protein, polypeptide, or multisubunit peptide. In some aspects, the nucleic acid disclosed herein can be used to encode the receptor binding domain, polypeptide, or multisubunit peptide through methods known in the art, for example, expressed in any suitable recombinant expression system. Vectors In some aspects, the present disclosure provides vectors (also referred to as expression vectors) comprising the nucleic acid disclosed herein. In certain embodiments, the expression vectors may comprise control sequences that govern transcription and translation, as well as nucleic acid sequences that serve other functions. In some embodiments, the receptor binding domain, polypeptide, or multisubunit peptide as disclosed herein may be expressed when a nucleic acid encoding the receptor binding domain, polypeptide, or multisubunit peptide are inserted into expression vectors such that the coding sequence is operably linked to transcriptional and translational control sequences. The common expression vectors are plasmids, viral vectors (bacteriophages, adenoviruses, retroviruses, lentiviruses etc), cosmids and artificial chromosomes. In some embodiments, the expression vector comprising the nucleic acid may encode the receptor binding domain, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, the expression vector comprising the nucleic acid may encode the polypeptide comprising a receptor binding domain, a self-assembling peptide, and a linker peptide connecting the receptor binding domain with the self- assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. In some embodiments, the expression vector comprising the nucleic acid may encode the multisubunit peptide disclosed herein. Host cells or Expression system In another aspect, the present disclosure provides host cells comprising an expression vector as described herein. Receptor binding domain, polypeptide, or multisubunit peptide can be expressed in a variety of cell types known in the art. In some embodiments, an expression vector encoding the receptor binding domain, polypeptide, or multisubunit peptide may be transfected into any host cell known in the art using any of the variety of methods known in the art. Expression vectors may be introduced into prokaryotic or eukaryotic cells using any transformation or transfection techniques known in the art. Some of the well known expression systems include, but not limited to, bacterial, mammalian, yeast, and insect cell systems. Any suitable expression system may be used to express the receptor binding domain, polypeptide, or multisubunit peptide disclosed herein. Fermentation The transformed cells are cultivated in a bioreactor under controlled conditions (temperature, pH, oxygen, nutrient supply etc) to maximize the production of the desired protein or peptide, such as the receptor binding domain, the polypeptide, or the multisubunit peptide as disclosed herein. For example, the cell may be cultivated by shake flask cultivation, small-scale or large-scale fermentation (including continuous, batch, fed-batch, or solid-state fermentations) in laboratory or industrial fermentors supplemented with suitable medium and under conditions allowing the receptor binding domain, polypeptide, or multisubunit peptide to be expressed and / or isolated. The cultivation takes place in a suitable nutrient medium comprising carbon and nitrogen sources and inorganic salts, using procedures known in the art. Suitable media are available from commercial suppliers or may be prepared according to methods well known in the art. If the desired receptor binding domain, polypeptide, or multisubunit peptide is secreted into the nutrient medium, they can be recovered directly from the medium. If the desired receptor binding domain, polypeptide, or multisubunit peptide is not secreted, it can be recovered from cell lysates. Conventional methods such as sonication, enzymatic lysis, centrifugation, precipitation, solubilization, filtration etc may be used to recover the desired receptor binding domain, polypeptide, or multisubunit peptide from the nutrient media or the cell lysates. Purification The recovered receptor binding domain, polypeptide, or multisubunit peptide may be subjected to one or more purification steps, for example, precipitation, sonication, centrifugation, filtration, chromatographic separation. The various chromatography techniques to purify receptor binding domain, polypeptide, or multisubunit peptide, disclosed herein, are well known in the art, for example, affinity chromatography, ion- exchange chromatography (cation or anion exchange), size exclusion chromatography, and hydrophobic interaction chromatography. One or more such techniques may be employed to obtain the receptor binding domain, polypeptide, or multisubunit peptide to the desired level of purity. Formulation The final step involves formulating the purified receptor binding domain, polypeptide, or multisubunit peptide into a stable and deliverable product. Well-known pharmaceutically acceptable excipients, such as but not limited to, buffering agents, stabilizers, tonicity modifiers, surfactants, chelating agents, salts, antioxidants, diluents, preservatives, or their combination may be used to formulate the purified protein or peptide. Method of treatment In some aspects, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof the nucleic acid sequence as disclosed herein. In some embodiments, the nucleic acid sequence encodes the receptor binding domain as disclosed herein. In some embodiments, the nucleic acid sequence encodes the polypeptide as disclosed herein. In some embodiments, the nucleic acid sequence encodes the multisubunit peptide as disclosed herein. In some aspects, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof the lipid nanoparticle composition comprising a cationic lipid, a phospholipid, a sterol, a PEG-lipid and the nucleic acid sequence as described herein. In some aspects, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof the lipid nanoparticle composition comprising a cationic lipid, a phospholipid, a sterol, a PEG-lipid and the nucleic acid sequence as disclosed herein, wherein the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315, or a combination thereof. In some aspects, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof the lipid nanoparticle composition comprising an ionizable polymer, a cationic lipid, a phospholipid, a sterol, a PEG-lipid and the nucleic acid sequence as disclosed herein. In some aspects, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof the lipid nanoparticle composition comprising an ionizable polymer, a cationic lipid, a phospholipid, a sterol, a PEG-lipid and the nucleic acid sequence as disclosed herein, wherein the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315, or a combination thereof. In some aspects, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof a vaccine comprising the nucleic acid as disclosed herein. In some aspects, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof a vaccine comprising the lipid nanoparticle composition, wherein the lipid nanoparticle composition comprises a cationic lipid, a phospholipid, a sterol, a PEG-lipid, and the nucleic acid as disclosed herein. In some aspects, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof a vaccine comprising the lipid nanoparticle composition, wherein the lipid nanoparticle composition comprises a cationic lipid, a phospholipid, a sterol, a PEG-lipid, and the nucleic acid as disclosed herein, wherein the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315, or a combination thereof. In some aspects, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof a vaccine comprising the lipid nanoparticle composition, wherein the lipid nanoparticle composition comprises an ionizable polymer, a cationic lipid, a phospholipid, a sterol, a PEG-lipid, and the nucleic acid as disclosed herein. In some aspects, provided herein is a method of treating or preventing a disease, comprising administering to a subject in need thereof a vaccine comprising the lipid nanoparticle composition, wherein the lipid nanoparticle composition comprises an ionizable polymer, a cationic lipid, a phospholipid, a sterol, a PEG-lipid, and the nucleic acid as disclosed herein, wherein the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315, or a combination thereof. In some aspects, the disclosure relates to use of the nucleic acid as disclosed herein in the manufacture of a medicament for the treatment or prevention of a disease in a subject. In some embodiments, the nucleic acid encodes the receptor binding domain as disclosed herein. In some embodiments, the nucleic acid encodes the polypeptide as described herein. In some embodiments, the nucleic acid encodes the multisubunit peptide as described herein. In some aspects, the disclosure relates to use of a lipid nanoparticle composition comprising a cationic lipid, a phospholipid, a sterol, a PEG-lipid, and the nucleic acid sequence as disclosed herein in the manufacture of a medicament for the treatment or prevention of a disease in a subject. In some aspects, the disclosure relates to use of a lipid nanoparticle composition comprising a cationic lipid, a phospholipid, a sterol, a PEG-lipid, and the nucleic acid sequence as disclosed herein, in the manufacture of a medicament for the treatment or prevention of a disease in a subject, wherein the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315, or a combination thereof. In some aspects, the disclosure relates to use of a lipid nanoparticle composition comprising an ionizable polymer, a cationic lipid, a phospholipid, a sterol, a PEG-lipid, and the nucleic acid sequence as disclosed herein, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. In some aspects, the disclosure relates to use of a lipid nanoparticle composition comprising an ionizable polymer, a cationic lipid, a phospholipid, a sterol, a PEG-lipid, and the nucleic acid sequence as disclosed herein in the manufacture of a medicament for the treatment or prevention of a disease in a subject, wherein the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315, or a combination thereof. In some embodiments, the disclosure relates to use of a vaccine comprising the nucleic acid as disclosed herein, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. In some embodiments, the disclosure relates to use of a vaccine comprising a lipid nanoparticle composition, wherein the lipid nanoparticle composition comprises a cationic lipid, a phospholipid, a sterol, a PEG-lipid, and the nucleic acid as disclosed herein, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. In some embodiments, the disclosure relates to use of a vaccine comprising a lipid nanoparticle composition, wherein the lipid nanoparticle composition comprises a cationic lipid, a phospholipid, a sterol, a PEG-lipid, and the nucleic acid as disclosed herein, in the manufacture of a medicament for the treatment or prevention of a disease in a subject, wherein the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC- 0315, or a combination thereof. In some embodiments, the disclosure relates to use of a vaccine comprising a lipid nanoparticle composition, wherein the lipid nanoparticle composition comprises an ionizable polymer, a cationic lipid, a phospholipid, a sterol, a PEG-lipid, and the nucleic acid as disclosed herein, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. In some embodiments, the disclosure relates to use of a vaccine comprising a lipid nanoparticle composition, wherein the lipid nanoparticle composition comprises an ionizable polymer, a cationic lipid, a phospholipid, a sterol, a PEG-lipid, and the nucleic acid as disclosed herein, in the manufacture of a medicament for the treatment or prevention of a disease in a subject, wherein the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315,or a combination thereof. In some embodiments, the disease is COVID-19 caused by SARS-CoV-2. In some embodiments, the nucleic acid sequence is present in biologically effective amount or therapeutically effective amount. In some embodiments, the biologically effective amount of the nucleic acid is between 0.1 µg to 2000 µg, 0.1 µg to 1800 µg, 0.1 µg to 1600 µg, 0.1 µg to 1400 µg, 0.1 µg to 1200 µg, 0.1 µg to 1000 µg, 0.1 µg to 950 µg, 0.1 µg to 900 µg, 0.1 µg to 850 µg, 0.1 µg to 800 µg, 0.1 µg to 750 µg, 0.1 µg to 700 µg, 0.1 µg to 650 µg, 0.1 µg to 600 µg, 0.1 µg to 550 µg, 0.1 µg to 500 µg, 0.1 µg to 450 µg, 0.1 µg to 400 µg, 0.1 µg to 350 µg, 0.1 µg to 300 µg, 0.1 µg to 250 µg, 0.1 µg to 200 µg, 0.1 to 175 µg, 0.1 to 150 µg, 0.1 to 125 µg, 0.1 to 100 µg, 0.1 µg to 90 µg, 0.1 µg to 80 µg, 0.1 µg to 70 µg, 0.1 µg to 60 µg, 0.1 µg to 50 µg, 0.1 µg to 40 µg, 0.1 µg to 30 µg, 0.1 µg to 20 µg, 0.1 µg to 10 µg, 0.1 µg to 5 µg, or any range therein. In some embodiments, the biologically effective amount of the nucleic acid is from about 0.1 µg to 1000 µg, 0.1 µg to 950 µg, 0.1 µg to 900 µg, 0.1 µg to 850 µg, 0.1 µg to 800 µg, 0.1 µg to 750 µg, 0.1 µg to 700 µg, 0.1 µg to 650 µg, 0.1 µg to 600 µg, 0.1 µg to 550 µg, 0.1 µg to 500 µg, or any range therein. In some embodiments, the biologically effective amount of the nucleic acid is 0.1 µg, 0.2 µg, 0.3 µg, 0.4 µg, 0.5 µg, 0.6 µg, 0.7µg, 0.8 µg, 0.9 µg, 1 µg, 2 µg, 3 µg, 4 µg, 5 µg, 6 µg, 7 µg, 8 µg, 9 µg, 10 µg, 15 µg, 20 µg, 25 µg, 30 µg, 35 µg, 40 µg, 45 µg, 50 µg, 55 µg, 60 µg, 65 µg, 70 µg, 75 µg, 80 µg, 85 µg, 90 µg, 95 µg, 100 µg, 110 µg, 120 µg, 130 µg, 140 µg, 150 µg, 160 µg, 170 µg, 180 µg, 190 µg, 200 µg, 220 µg, 240 µg, 260 µg, 280 µg, 300 µg, 350 µg, 400 µg, 450 µg, 500 µg, 600 µg, 700 µg, 800 µg, 900 µg, 1000 µg, 1100 µg, 1200 µg, 1300 µg, 1400 µg, 1500 µg, 1600 µg, 1700 µg, 1800 µg, 1900 µg, 2000 µg, or any portion or fraction thereof. Embodiments Some of the embodiments of the present disclosure, set out in the following numbered paragraphs are: Embodiment – Set 1 1. A receptor binding domain comprising one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. 2. The receptor binding domain according to paragraph 1, wherein the receptor binding domain has at least 50% identity compared to SEQ ID NO: 1. 3. The receptor binding domain according to any one of the paragraphs 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions K38T, F138L, V165del, E166P, A202G, or a combination thereof compared to SEQ ID NO: 1. 4. The receptor binding domain according to any one of the paragraphs 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions R28T, K38T, F138L, V165del, E166K, or a combination thereof compared to SEQ ID NO: 1. 5. The receptor binding domain according to any one of the paragraphs 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions R28T, K38V, F138L, A157V, E166A, S176P, or a combination thereof compared to SEQ ID NO: 1. 6. The receptor binding domain according to any one of the paragraphs 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions R28T, K38T, F138L, V165del, E166K, Q175E, or a combination thereof compared to SEQ ID NO: 1. 7. The receptor binding domain according to any one of the paragraphs 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions K38T, V165del, E166K, or a combination thereof compared to SEQ ID NO: 1. 8. The receptor binding domain according to any one of the paragraphs 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions R28T and F138L compared to SEQ ID NO: 1. 9. The receptor binding domain according to any one of the paragraphs 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions K38V or T, A157V, and S176P compared to SEQ ID NO: 1. 10. The receptor binding domain according to any one of the paragraphs 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions K126T, F138L, E166A or K or P, and A202G compared to SEQ ID NO: 1. 11. The receptor binding domain according to any one of the preceding paragraphs, wherein the receptor binding domain has an amino acid sequence of any one of SEQ ID NOs: 2-6. 12. The receptor binding domain according to paragraph 11, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 2. 13. The receptor binding domain according to paragraph 11, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 3. 14. The receptor binding domain according to paragraph 11, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 4. 15. The receptor binding domain according to paragraph 11, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 5. 16. The receptor binding domain according to paragraph 11, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 6. 17. The receptor binding domain according to any one of the preceding paragraphs, wherein the receptor binding domain comprises one or more signal peptide on the amino-terminus of the receptor binding domain. 18. A composition comprising the receptor binding domain according to any one of the preceding paragraphs and a pharmaceutically acceptable excipient. 19. The composition according to paragraph 18, wherein the pharmaceutically acceptable excipient is selected from the group comprising buffering agent, stabilizer, tonicity modifier, surfactant, chelating agent, salt, anti-oxidant, diluent, preservative, or a combination thereof. 20. A nucleic acid encoding the receptor binding domain according to any one of the paragraphs 1-17. 21. The nucleic acid according to paragraph 20, wherein the nucleic acid is a DNA, an RNA, or an mRNA. 22. A vector comprising the nucleic acid of paragraph 21. 23. A lipid nanoparticle composition comprising a cationic lipid, a phospholipid, a sterol, a PEG-lipid and the nucleic acid of paragraph 21. 24. The lipid nanoparticle composition according to paragraph 23, wherein the cationic lipid is present in an amount from 10 mol percent to 70 mol percent. 25. The lipid nanoparticle composition according to paragraph 23, wherein the phospholipid is present in an amount from 2 mol percent to 65 mol percent. 26. The lipid nanoparticle composition according to paragraph 23, wherein the sterol is present in an amount from 20 mol percent to 65 mol percent. 27. The lipid nanoparticle composition according to paragraph 23, wherein the PEG- lipid is present in an amount from 0.2 mol percent to 2.0 mol percent. 28. The lipid nanoparticle composition according to paragraph 23, additionally comprising an ionizable polymer. 29. The lipid nanoparticle composition according to paragraph 28, wherein the ionizable polymer is present in an amount from 1 mol percent to 25 mol percent. 30. The lipid nanoparticle composition according to any one of the paragraphs 23-29, wherein the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315, or a combination thereof. 31. The lipid nanoparticle composition according to paragraph 30, wherein the cationic lipid is represented by formula (I). 32. The lipid nanoparticle composition according to paragraph 30, wherein the cationic lipid is represented by formula (II). 33. The lipid nanoparticle composition according to paragraph 30, wherein the cationic lipid is represented by formula (III). 34. The lipid nanoparticle composition according to paragraph 30, wherein the cationic lipid is represented by formula (IV). 35. The lipid nanoparticle composition according to paragraph 30, wherein the cationic lipid is represented by formula (V). 36. The lipid nanoparticle composition according to paragraph 30, wherein the cationic lipid is represented by formula (VI). 37. The lipid nanoparticle composition according to paragraph 30, wherein the cationic lipid is represented by formula (VII). 38. The lipid nanoparticle composition according to paragraph 30, wherein the cationic lipid is represented by formula (VIII). 39. A vaccine comprising the receptor binding domain according to any one of the paragraphs 1-17. 40. A vaccine comprising the composition according to any one of the paragraphs 18- 19. 41. A vaccine comprising the nucleic acid according to paragraph 21. 42. A vaccine comprising the lipid nanoparticle composition according to any one of the paragraphs 23-38. 43. A method of treating or preventing a disease, comprising administering to a subject in need thereof the receptor binding domain according to any one of the paragraphs 1-17 or the vaccine according to paragraph 39. 44. A method of treating or preventing a disease, comprising administering to a subject in need thereof the composition according to any one of the paragraphs 18-19 or the vaccine according to paragraph 40. 45. A method of treating or preventing a disease, comprising administering to a subject in need thereof the nucleic acid according to paragraph 21 or the vaccine according to paragraph 41. 46. A method of treating or preventing a disease, comprising administering to a subject in need thereof the lipid nanoparticle composition according to any one of the paragraphs 23-38 or the vaccine according to paragraph 42. 47. The method according to any one of the paragraphs 43-46, wherein the disease is COVID-19. 48. Use of the receptor binding domain according to any one of the paragraphs1-17 or the vaccine according to paragraph 39, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. 49. Use of the composition according to any one of the paragraphs 18-19 or the vaccine according to paragraph 40, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. 50. Use of the nucleic acid according to paragraph 21 or the vaccine according to paragraph 41, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. 51. Use of the lipid nanoparticle according to any one of the paragraphs 23-38 or the vaccine according to paragraph 42, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. 52. The use according to any one of the paragraphs 48-51, wherein the disease is COVID-19. Embodiment – Set 2 1. A polypeptide comprising a receptor binding domain, a self-assembling peptide, and a linker peptide connecting the receptor binding domain and the self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. 2. The polypeptide according to paragraph 1, wherein the receptor binding domain has at least 50% identity compared to SEQ ID NO: 1. 3. The polypeptide according to any one of the paragraphs 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions K38T, F138L, V165del, E166P, A202G, or a combination thereof compared to SEQ ID NO: 1. 4. The polypeptide according to any one of the paragraphs 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions R28T, K38T, F138L, V165del, E166K, or a combination thereof compared to SEQ ID NO: 1. 5. The polypeptide according to any one of the paragraphs 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions R28T, K38V, F138L, A157V, E166A, S176P, or a combination thereof compared to SEQ ID NO: 1. 6. The polypeptide according to any one of the paragraphs 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions R28T, K38T, F138L, V165del, E166K, Q175E, or a combination thereof compared to SEQ ID NO: 1. 7. The polypeptide according to any one of the paragraphs 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions K38T, V165del, E166K, or a combination thereof compared to SEQ ID NO: 1. 8. The polypeptide according to any one of the paragraphs 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions R28T and F138L compared to SEQ ID NO: 1. 9. The polypeptide according to any one of the paragraphs 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions K38V or T, A157V, and S176P compared to SEQ ID NO: 1. 10. The polypeptide according to any one of the paragraphs 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions K126T, F138L, E166A or K or P, and A202G compared to SEQ ID NO: 1. 11. The polypeptide according to any one of the preceding paragraphs, wherein the receptor binding domain has an amino acid sequence of any one of SEQ ID NOs: 2- 6. 12. The polypeptide according to paragraph 11, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 2. 13. The polypeptide according to paragraph 11, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 3. 14. The polypeptide according to paragraph 11, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 4. 15. The polypeptide according to paragraph 11, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 5. 16. The polypeptide according to paragraph 11, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 6. 17. The polypeptide according to any one of the preceding paragraphs, wherein the polypeptide comprises one or more signal peptide on the amino-terminus of the polypeptide. 18. The polypeptide according to any one of the preceding paragraphs, wherein the linker peptide is an amino acid linker, a foldon, a scaffold, or a combination thereof. 19. The polypeptide according to paragraph 18, wherein the linker peptide is the amino acid linker. 20. The polypeptide according to paragraph 19, wherein the amino acid linker comprises 2 to 49 amino acids. 21. The polypeptide according to any one of the paragraphs 18-20, wherein the amino acid linker is a glycine serine linker, a glycine proline linker, a glycine threonine linker, an alanine serine linker, any combination of two amino acids, or a combination thereof. 22. The polypeptide according to paragraph 18, wherein the linker peptide is the foldon. 23. The polypeptide according to paragraph 18, wherein the linker peptide is the scaffold. 24. The polypeptide according to any one of the paragraphs 18-21, wherein the linker peptide comprises the amino acid linker and the foldon. 25. The polypeptide according to any one of the paragraphs 18-21, wherein the linker peptide comprises the amino acid linker and the scaffold. 26. The polypeptide according to any one of the paragraphs 18-21, wherein the linker peptide comprises the amino acid linker, the foldon, and the scaffold. 27. The polypeptide according to paragraph 18, wherein the linker peptide comprises the foldon and the scaffold. 28. The polypeptide according to any one of the preceding paragraphs, wherein the linker peptide has an amino acid sequence of any one of SEQ ID NOs: 18-57. 29. The polypeptide according to any one of the preceding paragraphs, wherein the self- assembling peptide is a lumazine synthase, an MS2 coat protein, a hepatitis B surface antigen (HBsAg) from Hepatitis B Virus, a hepatitis B core antigen (HbcAg) from Hepatitis B virus, a human papillomavirus L1 (HPV L1) protein, a ferritin, a riboflavin synthase, a dihydrolipoyl acetyltransferase (E2p), or a combination thereof, including their codon optimized nucleic acid sequences, fragments, mutants, variants, comparable equivalents, or functional analogs thereof. 30. The polypeptide according to paragraph 29, wherein the self-assembling peptide is a ferritin comprising a ferritin subunit or a ferritin peptide, a dihydrolipoyl acetyltransferase (E2p), a lumazine synthase, an MS2 coat protein, or a combination thereof. 31. The polypeptide according to paragraph 30, wherein the ferritin peptide is obtained or derived from Helicobacter pylori ferritin or Listeria innocua ferritin, the lumazine synthase is obtained or derived from Aquifex aeolicus or Bacillus subtilis, the MS2 coat protein is obtained or derived from Emesvirus zinderi, and the dihydrolipoyl acetyltransferase (E2p) is obtained or derived from Bacillus stearothermophilus. 32. The polypeptide according to any one of the preceding paragraphs, wherein the self- assembling peptide has an amino acid sequence of any one of SEQ ID NOs: 7-17 or 99-102. 33. The polypeptide according to any one of the preceding paragraphs, wherein the polypeptide comprises an amino acid sequence of any one of SEQ ID NOs: 94-97 or 103. 34. A composition comprising the polypeptide according to any one of the preceding paragraphs and a pharmaceutically acceptable excipient. 35. The composition according to paragraph 34, wherein the pharmaceutically acceptable excipient is selected from the group comprising buffering agent, stabilizer, tonicity modifier, surfactant, chelating agent, salt, anti-oxidant, diluent, preservative, or a combination thereof. 36. A nucleic acid encoding the polypeptide according to any one of the paragraphs 1- 33. 37. The nucleic acid according to paragraph 36, wherein the nucleic acid is a DNA, an RNA, or an mRNA. 38. A vector comprising the nucleic acid of paragraph 37. 39. A lipid nanoparticle comprising a cationic lipid, a phospholipid, a sterol, a PEG-lipid and the nucleic acid according to paragraph 37. 40. The lipid nanoparticle composition according to paragraph 39, wherein the cationic lipid is present in an amount from 10 mol percent to 70 mol percent. 41. The lipid nanoparticle composition according to paragraph 39, wherein the phospholipid is present in an amount from 2 mol percent to 65 mol percent. 42. The lipid nanoparticle composition according to paragraph 39, wherein the sterol is present in an amount from 20 mol percent to 65 mol percent. 43. The lipid nanoparticle composition according to paragraph 39, wherein the PEG- lipid is present in an amount from 0.2 mol percent to 2.0 mol percent. 44. The lipid nanoparticle composition according to paragraph 39, additionally comprising an ionizable polymer. 45. The lipid nanoparticle composition according to paragraph 44, wherein the ionizable polymer is present in an amount from 1 mol percent to 25 mol percent. 46. The lipid nanoparticle composition according to any one of the paragraphs 39-45, wherein the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315, or a combination thereof. 47. The lipid nanoparticle composition according to paragraph 46, wherein the cationic lipid is represented by formula (I). 48. The lipid nanoparticle composition according to paragraph 46, wherein the cationic lipid is represented by formula (II). 49. The lipid nanoparticle composition according to paragraph 46, wherein the cationic lipid is represented by formula (III). 50. The lipid nanoparticle composition according to paragraph 46, wherein the cationic lipid is represented by formula (IV). 51. The lipid nanoparticle composition according to paragraph 46, wherein the cationic lipid is represented by formula (V). 52. The lipid nanoparticle composition according to paragraph 46, wherein the cationic lipid is represented by formula (VI). 53. The lipid nanoparticle composition according to paragraph 46, wherein the cationic lipid is represented by formula (VII). 54. The lipid nanoparticle composition according to paragraph 46, wherein the cationic lipid is represented by formula (VIII). 55. A polypeptide nanoparticle comprising at least 2 or up to 500 polypeptides according to any one of the paragraphs 1-33. 56. The polypeptide nanoparticle according to paragraphs 55, wherein the polypeptide nanoparticle is icosahedral, helical, spherical, rod-like or a combination thereof. 57. A vaccine comprising the polypeptide according to any one of the paragraphs 1-33. 58. A vaccine comprising the composition according to any one of the paragraphs 34- 35. 59. A vaccine comprising the nucleic acid according to paragraph 37. 60. A vaccine comprising the lipid nanoparticle composition according to any one of the paragraphs 39-54. 61. A vaccine comprising the polypeptide nanoparticle according any one of the paragraphs 55-56. 62. A method of treating or preventing a disease, comprising administering to a subject in need thereof the polypeptide according to any one of the paragraphs 1-33 or the vaccine according to paragraph 57. 63. A method of treating or preventing a disease, comprising administering to a subject in need thereof the composition according to any one of the paragraphs 34-35 or the vaccine according to paragraph 58. 64. A method of treating or preventing a disease, comprising administering to a subject in need thereof the nucleic acid according to paragraph 37 or the vaccine according to paragraph 59. 65. A method of treating or preventing a disease, comprising administering to a subject in need thereof the lipid nanoparticle composition according to any one of the paragraphs 39-54 or the vaccine according to paragraph 60. 66. A method of treating or preventing a disease, comprising administering to a subject need thereof the polypeptide nanoparticle according to any one of the paragraphs 55- 56 or the vaccine according to paragraph 61. 67. The method according to any one of the paragraphs 62-66, wherein the disease is COVID-19. 68. Use of the polypeptide according to any one of the paragraphs 1-33 or the vaccine according to paragraph 57, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. 69. Use of the composition according to any one of the paragraphs 34-35 or the vaccine according to paragraph 58, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. 70. Use of the nucleic acid according to paragraph 37 or the vaccine according to paragraph 59, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. 71. Use of the lipid nanoparticle according to any one of the paragraphs 39-54 or the vaccine according to paragraph 60, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. 72. Use of the polypeptide nanoparticle according to any one of the paragraphs 55-56 or the vaccine according to paragraph 61, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. 73. The use according to any one of the paragraphs 68-72, wherein the disease is COVID-19. Embodiment – Set 3 1. A nucleic acid comprising a plurality of polynucleotide sequences, wherein some or all polynucleotide sequences of the plurality comprises either a receptor binding domain sequence, a linker sequence, and a self-assembling sequence or a linker sequence, a receptor binding domain sequence, a linker sequence and a self- assembling sequence or a combination thereof, wherein each polynucleotide sequence of the plurality is connected to an adjacent polynucleotide sequence of the plurality by a cleavage sequence, wherein the nucleic acid further comprises a signal sequence upstream of one or more of the polynucleotide sequences of the plurality, and wherein the receptor binding domain sequence comprises a mutation at: (a) a codon encoding an amino acid R at the position corresponding to the position 28 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid R with an amino acid T, (b) a codon encoding an amino acid K at the position corresponding to the position 38 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid V or T, (c) a codon encoding an amino acid K at the position corresponding to the position 126 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid T, (d) a codon encoding an amino acid F at the position corresponding to the position 138 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid F with an amino acid L, (e) a codon encoding an amino acid A at the position corresponding to the position 157 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid V, (f) a codon encoding an amino acid V at the position corresponding to the position 165 of the SEQ ID NO: 1, wherein the mutation is a deletion, (g) a codon encoding an amino acid E at the position corresponding to the position 166 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid E with an amino acid A, or K, or P, (h) a codon encoding an amino acid Q at the position corresponding to the position 175 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid Q with an amino acid E, (i) a codon encoding an amino acid S at the position corresponding to the position 176 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid S with an amino acid P, (j) a codon encoding an amino acid A at the position corresponding to the position 202 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid G, or a combination thereof. 2. A nucleic acid comprising a plurality of polynucleotide sequences, wherein each polynucleotide sequence of the plurality comprises a receptor binding domain sequence, a linker sequence, and a self-assembling sequence, wherein each polynucleotide sequence of the plurality is connected to an adjacent polynucleotide sequence of the plurality by a cleavage sequence, wherein the nucleic acid further comprises a signal sequence upstream of one or more of the polynucleotide sequences of the plurality, and wherein the receptor binding domain sequence comprises a mutation at: (a) a codon encoding an amino acid R at the position corresponding to the position 28 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid R with an amino acid T, (b) a codon encoding an amino acid K at the position corresponding to the position 38 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid V or T, (c) a codon encoding an amino acid K at the position corresponding to the position 126 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid T, (d) a codon encoding an amino acid F at the position corresponding to the position 138 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid F with an amino acid L, (e) a codon encoding an amino acid A at the position corresponding to the position 157 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid V, (f) a codon encoding an amino acid V at the position corresponding to the position 165 of the SEQ ID NO: 1, wherein the mutation is a deletion, (g) a codon encoding an amino acid E at the position corresponding to the position 166 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid E with an amino acid A, or K, or P, (h) a codon encoding an amino acid Q at the position corresponding to the position 175 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid Q with an amino acid E, (i) a codon encoding an amino acid S at the position corresponding to the position 176 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid S with an amino acid P, (j) a codon encoding an amino acid A at the position corresponding to the position 202 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid G, or a combination thereof. 3. A nucleic acid comprising a plurality of polynucleotide sequences, wherein each polynucleotide sequence of the plurality comprises a linker sequence, a receptor binding domain sequence, a linker sequence, and a self-assembling sequence, wherein each polynucleotide sequence of the plurality is connected to an adjacent polynucleotide sequence of the plurality by a cleavage sequence, wherein the nucleic acid further comprises a signal sequence upstream of one or more of the polynucleotide sequences of the plurality, and wherein the receptor binding domain sequence comprises a mutation at: (a) a codon encoding an amino acid R at the position corresponding to the position 28 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid R with an amino acid T, (b) a codon encoding an amino acid K at the position corresponding to the position 38 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid V or T, (c) a codon encoding an amino acid K at the position corresponding to the position 126 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid T, (d) a codon encoding an amino acid F at the position corresponding to the position 138 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid F with an amino acid L, (e) a codon encoding an amino acid A at the position corresponding to the position 157 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid V, (f) a codon encoding an amino acid V at the position corresponding to the position 165 of the SEQ ID NO: 1, wherein the mutation is a deletion, (g) a codon encoding an amino acid E at the position corresponding to the position 166 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid E with an amino acid A, or K, or P, (h) a codon encoding an amino acid Q at the position corresponding to the position 175 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid Q with an amino acid E, (i) a codon encoding an amino acid S at the position corresponding to the position 176 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid S with an amino acid P, (j) a codon encoding an amino acid A at the position corresponding to the position 202 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid G, or a combination thereof. 4. The nucleic acid according to any one of the preceding paragraphs, wherein the receptor binding domain sequence, the linker sequence, and the self-assembling sequence or the linker sequence, the receptor binding domain sequence, the linker sequence, and the self-assembling sequence are in 5’ to 3’ order. 5. A nucleic acid encoding a plurality of polypeptides, wherein some or all polypeptides of the plurality comprises either a receptor binding domain, a linker peptide, and a self-assembling peptide or a linker peptide, a receptor binding domain, a linker peptide and a self-assembling peptide or a combination thereof, wherein each polypeptide of the plurality is connected to an adjacent polypeptide of the plurality by a cleavage peptide, and wherein the nucleic acid further encodes a signal peptide on the amino-terminus of one or more of the polypeptides of the plurality, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. A nucleic acid encoding a plurality of polypeptides, wherein each polypeptide of the plurality comprises a receptor binding domain, a linker peptide, and a self- assembling peptide, wherein each polypeptide of the plurality is connected to an adjacent polypeptide of the plurality by a cleavage peptide, and wherein the nucleic acid further encodes a signal peptide on the amino-terminus of one or more of the polypeptides of the plurality, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. A nucleic acid encoding a plurality of polypeptides, wherein each polypeptides of the plurality comprises a linker peptide, a receptor binding domain, a linker peptide and a self-assembling peptide, wherein each polypeptide of the plurality is connected to an adjacent polypeptide of the plurality by a cleavage peptide, and wherein the nucleic acid further encodes a signal peptide on the amino-terminus of one or more of the polypeptides of the plurality, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. The nucleic acid according to any one of the paragraphs 5-7, wherein the receptor binding domain, the linker peptide, and the self-assembling peptide or the linker peptide, the receptor binding domain, the linker peptide and the self-assembling peptide are in N-terminus to C-terminus order. The nucleic acid according to any one of the preceding paragraphs, wherein total number of the polynucleotide sequences is not more than 100. The nucleic acid according to paragraph 9, wherein total number of the polynucleotide sequences is between 2-5, 2-10, 10-20, 20-30, 30-40, 40-50, 50-60, 60-70, 70-80, 80-90, or 90-99. The nucleic acid according to any one of the preceding paragraphs, wherein the nucleic acid is a DNA or an RNA. 12. The nucleic acid according to paragraph 11, wherein the RNA is an mRNA. 13. The nucleic acid according to paragraph 12, wherein the mRNA is 0.5 kb to 1 kb, 1 kb to 2 kb, 2 kb to 3 kb, 3 kb to 4 kb, 4 kb to 5 kb, 5 kb to 6 kb, 6 kb to 7 kb, 7 kb to 8 kb, 8 kb to 9 kb, 9 kb to 10 kb, 10 kb to 11 kb, 11 kb to 12 kb, 12 kb to 13 kb, 13 kb to 14 kb, 14 kb to 15 kb, 15 kb to 16 kb, 16 kb to 17 kb, 17 kb to 18 kb, 18 kb to 19 kb, 19 kb to 20 kb in length, or any range therein. 14. The nucleic acid according to any one of the paragraphs 12-13, wherein the mRNA is obtained through a single IVT process or step. 15. The nucleic acid according to any one of the preceding paragraphs 1-4 and 9-14, wherein the linker sequence encodes a linker peptide. 16. The nucleic acid according to paragraph 15, wherein the linker peptide is an amino acid linker, a foldon, a scaffold, or a combination thereof. 17. The nucleic acid according to paragraph 16, wherein the linker peptide is the amino acid linker. 18. The nucleic acid according to paragraph 17, wherein the amino acid linker comprises 2 to 49 amino acids. 19. The nucleic acid according to any one of the paragraphs 17-18, wherein the amino acid linker is a glycine serine linker, a glycine proline linker, a glycine threonine linker, an alanine serine linker, any combination of two amino acids, or a combination thereof. 20. The nucleic acid according to paragraph 16, wherein the linker peptide is the foldon. 21. The nucleic acid according to paragraph 16, wherein the linker peptide is the scaffold. 22. The nucleic acid according to any one of the paragraphs 16-19, wherein the linker peptide comprises the amino acid linker and the foldon. 23. The nucleic acid according to any one of the paragraphs 16-19, wherein the linker peptide comprises the amino acid linker and the scaffold. 24. The nucleic acid according to any one of the paragraphs 16-19, wherein the linker peptide comprises the amino acid linker, the foldon, and the scaffold. 25. The nucleic acid according to paragraph 16, wherein the linker peptide comprises the foldon and the scaffold. 26. The nucleic acid according to any one of the paragraphs 5-25, wherein the linker peptide has an amino acid sequence of any one of SEQ ID NOs: 18-57. 27. The nucleic acid according to any one of the paragraphs 1-4 and 9-26, wherein the self-assembling sequence encodes a self-assembling peptide. 28. The nucleic acid according to any one of the paragraphs 5-27, wherein the self- assembling peptide is a lumazine synthase, an MS2 coat protein, a hepatitis B surface antigen (HBsAg) from Hepatitis B Virus, a hepatitis B core antigen (HbcAg) from Hepatitis B virus, a human papillomavirus L1 (HPV L1) protein, a matrix protein M1 from influenza A virus, a ferritin, a riboflavin synthase, dihydrolipoyl acetyltransferase (E2p), or a combination thereof, including their codon optimized nucleic acid sequences, fragments, mutants, variants, comparable equivalents, or functional analogs thereof. 29. The nucleic acid according to any one of the paragraphs 27-28, wherein the self- assembling peptide is a ferritin comprising a ferritin subunit or a ferritin peptide, a dihydrolipoyl acetyltransferase (E2p), a lumazine synthase, an MS2 coat protein, or a combination thereof. 30. The nucleic acid according to paragraph 29, wherein the ferritin peptide is obtained or derived from Helicobacter pylori ferritin or Listeria innocua ferritin, the lumazine synthase is obtained or derived from Aquifex aeolicus or Bacillus subtilis, the MS2 coat protein is obtained or derived from Emesvirus zinderi, and the dihydrolipoyl acetyltransferase (E2p) is obtained or derived from Bacillus stearothermophilus. 31. The nucleic acid according to any one of the paragraphs 5-30, wherein the self- assembling peptide has an amino acid sequence of any one of SEQ ID NOs: 7-17 or 99-102. 32. The nucleic acid according to any one of the paragraphs 1-4 and 9-31, wherein the cleavage sequence encodes one or more cleavage peptide. 33. The nucleic acid according to paragraph 32, wherein the one or more cleavage peptides are optionally connected to each other by a linker peptide. 34. The nucleic acid according to paragraph 33, wherein the cleavage peptide is a golgi specific cleavage peptide, a self-cleaving peptide, or a combination thereof. 35. The nucleic acid according to any one of the paragraphs 5-34, wherein the cleavage peptide has an amino acid sequence of any one of SEQ ID NOs: 58-73. 36. The nucleic acid according to any one of the paragraphs 1-4 and 9-35, wherein the signal sequence encodes a signal peptide. 37. The nucleic acid according to any one of the paragraphs 5-36, wherein the signal peptide is present on the amino-terminus of one or more of the polypeptides of the plurality. 38. The nucleic acid according to any one of the paragraphs 5-37, wherein the nucleic acid further encodes a second signal peptide on the amino-terminus of all or some polypeptides of the plurality. 39. The nucleic acid according to any one of the paragraphs 5-38, wherein the signal peptide has an amino acid sequence of any one of SEQ ID NOs: 74-93. 40. The nucleic acid according to any one of the paragraphs 1-4 and 9-39, wherein the receptor binding domain sequence encodes a receptor binding domain. 41. The nucleic acid according to paragraph 5-40, wherein the receptor binding domain has at least 50% identity compared to SEQ ID NO: 1. 42. The nucleic acid according to any one of the paragraphs 40-41, wherein the receptor binding domain comprises a mutation at amino acid position K38T, F138L, V165del, E166P, A202G, or a combination thereof compared to SEQ ID NO: 1. 43. The nucleic acid according to any one of the paragraphs 40-41, wherein the receptor binding domain comprises a mutation at amino acid positions R28T, K38T, F138L, V165del, E166K, or a combination thereof compared to SEQ ID NO: 1. 44. The nucleic acid according to any one of the paragraphs 40-41, wherein the receptor binding domain comprises a mutation at amino acid positions R28T, K38V, F138L, A157V, E166A, S176P, or a combination thereof compared to SEQ ID NO: 1. 45. The nucleic acid according to any one of the paragraphs 40-41, wherein the receptor binding domain comprises a mutation at amino acid positions R28T, K38T, F138L, V165del, E166K, Q175E, or a combination thereof compared to SEQ ID NO: 1. 46. The nucleic acid according to any one of the paragraphs 40-41, wherein the receptor binding domain comprises a mutation at amino acid positions K38T, V165del, E166K, or a combination thereof compared to SEQ ID NO: 1. 47. The nucleic acid according to any one of the paragraphs 40-41, wherein the receptor binding domain comprises a mutation at amino acid position R28T and F138L compared to SEQ ID NO: 1. 48. The nucleic acid according to any one of the paragraphs 40-41, wherein the receptor binding domain comprises a mutation at amino acid positions K38V or T, A157V, and S176P compared to SEQ ID NO: 1. 49. The nucleic acid according to any one of the paragraphs 40-41, wherein the receptor binding domain comprises a mutation at amino acid positions K126T, F138L, E166A or K or P, and A202G compared to SEQ ID NO: 1. 50. The nucleic acid according to any one of the paragraphs 5-49, wherein the receptor binding domain has an amino acid sequence of any one of SEQ ID NOs: 2-6. 51. The nucleic acid according to paragraph 50, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 2. 52. The nucleic acid according to paragraph 50, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 3. 53. The nucleic acid according to paragraph 50, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 4. 54. The nucleic acid according to paragraph 50, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 5. 55. The nucleic acid according to paragraph 50, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 6. 56. The nucleic acid according to any one of the preceding paragraphs, wherein the nucleic acid encoding plurality of polypeptides comprises an amino acid sequence of SEQ ID NO: 98. 57. A lipid nanoparticle composition comprising a cationic lipid, a phospholipid, a sterol, a PEG-lipid, and the nucleic acid according to any one of the preceding paragraphs. 58. The lipid nanoparticle composition according to paragraph 57, wherein the cationic lipid is present in an amount from 10 mol percent to 70 mol percent. 59. The lipid nanoparticle composition according to paragraph 57, wherein the phospholipid is present in an amount from 2 mol percent to 65 mol percent. 60. The lipid nanoparticle composition according to paragraph 57, wherein the sterol is present in an amount from 20 mol percent to 65 mol percent. 61. The lipid nanoparticle composition according to paragraph 57, wherein the PEG- lipid is present in an amount from 0.2 mol percent to 2.0 mol percent. 62. The lipid nanoparticle composition according to paragraph 57, additionally comprising an ionizable polymer. 63. The lipid nanoparticle composition according to paragraph 62, wherein the ionizable polymer is present in an amount from 1 mol percent to 25 mol percent. 64. The lipid nanoparticle composition according to any one of the paragraphs 57-63, wherein the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315, or a combination thereof. 65. The lipid nanoparticle composition according to paragraph 64, wherein the cationic lipid is represented by formula (I). 66. The lipid nanoparticle composition according to paragraph 64, wherein the cationic lipid is represented by formula (II). 67. The lipid nanoparticle composition according to paragraph 64, wherein the cationic lipid is represented by formula (III). 68. The lipid nanoparticle composition according to paragraph 64, wherein the cationic lipid is represented by formula (IV). 69. The lipid nanoparticle composition according to paragraph 64, wherein the cationic lipid is represented by formula (V). 70. The lipid nanoparticle composition according to paragraph 64, wherein the cationic lipid is represented by formula (VI). 71. The lipid nanoparticle composition according to paragraph 64, wherein the cationic lipid is represented by formula (VII). 72. The lipid nanoparticle composition according to paragraph 64, wherein the cationic lipid is represented by formula (VIII). 73. A multisubunit peptide encoded by the nucleic acid according any one of the paragraphs 1-56. 74. A multisubunit peptide comprising a plurality of polypeptides, wherein some or all polypeptides comprises either a receptor binding domain, a linker peptide, and a self- assembling peptide or a linker peptide, a receptor binding domain, a linker peptide, and a self-assembling peptide or a combination thereof, wherein one polypeptide of the plurality is connected to an adjacent polypeptide of the plurality by a cleavage peptide, wherein the multisubunit peptide includes a signal peptide on the amino- terminus of one or more of the polypeptides of the plurality, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1. 75. The multisubunit peptide according to paragraph 74, wherein the receptor binding domain has at least 50% identity compared to SEQ ID NO: 1. 76. The multisubunit peptide according to any one of the paragraphs 74-75, wherein the receptor binding domain comprises a mutation at amino acid positions K38T, F138L, V165del, E166P, A202G, or a combination thereof compared to SEQ ID NO: 1. 77. The multisubunit peptide according to any one of the paragraphs 74-75, wherein the receptor binding domain comprises a mutation at amino acid positions R28T, K38T, F138L, V165del, E166K, or a combination thereof compared to SEQ ID NO: 1. 78. The multisubunit peptide according to any one of the paragraphs 74-75, wherein the receptor binding domain comprises a mutation at amino acid positions R28T, K38V, F138L, A157V, E166A, S176P, or a combination thereof compared to SEQ ID NO: 1. 79. The multisubunit peptide according to any one of the paragraphs 74-75, wherein the receptor binding domain comprises a mutation at amino acid positions R28T, K38T, F138L, V165del, E166K, Q175E, or a combination thereof compared to SEQ ID NO: 1. 80. The multisubunit peptide according to any one of the paragraphs 74-75, wherein the receptor binding domain comprises a mutation at amino acid positions K38T, V165del, E166K, or a combination thereof compared to SEQ ID NO: 1. 81. The multisubunit peptide according to any one of the paragraphs 74-75, wherein the receptor binding domain comprises a mutation at amino acid positions R28T and F138L compared to SEQ ID NO: 1. 82. The multisubunit peptide according to any one of the paragraphs 74-75, wherein the receptor binding domain comprises a mutation at amino acid positions K38V or T, A157V, and S176P compared to SEQ ID NO: 1. 83. The multisubunit peptide according to any one of the paragraphs 74-75, wherein the receptor binding domain comprises a mutation at amino acid positions K126T, F138L, E166A or K or P, and A202G compared to SEQ ID NO: 1. 84. The multisubunit peptide according to any one of the paragraphs 74-83, wherein the receptor binding domain has an amino acid sequence of any one of SEQ ID NOs: 2- 6. 85. The multisubunit peptide according to paragraph 84, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 2. 86. The multisubunit peptide according to paragraph 84, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 3. 87. The multisubunit peptide according to paragraph 84, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 4. 88. The multisubunit peptide according to paragraph 84, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 5. 89. The multisubunit peptide according to paragraph 84, wherein the receptor binding domain has an amino acid sequence of SEQ ID NO: 6. 90. The multisubunit peptide according to any one of the paragraphs 74-89, wherein the linker peptide is an amino acid linker, a foldon, a scaffold, or a combination thereof. 91. The multisubunit peptide according to paragraph 90, wherein the linker peptide is the amino acid linker. 92. The multisubunit peptide according to paragraph 91, wherein the amino acid linker comprises 2-49 amino acids. 93. The multisubunit peptide according to any one of the paragraphs 91-92, wherein the amino acid linker is selected form the group comprising a glycine serine linker, a glycine proline linker, a glycine threonine linker, an alanine serine linker, any combination of two amino acids, or a combination thereof. 94. The multisubunit peptide according to paragraph 90, wherein the linker peptide is the foldon. 95. The multisubunit peptide according to paragraph 90, wherein the linker peptide is the scaffold. 96. The multisubunit peptide according to any one of the paragraphs 90-93, wherein the linker peptide comprises the amino acid linker and the foldon. 97. The multisubunit peptide according to any one of the paragraphs 90-93, wherein the linker peptide comprises the amino acid linker and the scaffold. 98. The multisubunit peptide according to any one of the paragraphs 90-93, wherein the linker peptide comprises the amino acid linker, the foldon, and the scaffold. 99. The multisubunit peptide according to paragraph 90, wherein the linker peptide comprises the foldon and the scaffold. 100. The multisubunit peptide according to any one of the paragraphs 74-99, wherein the self-assembling peptide is selected from the group comprising a lumazine synthase, an MS2 coat protein, a hepatitis B surface antigen (HBsAg) from Hepatitis B Virus, a hepatitis B core antigen (HBcAg) from Hepatitis B virus, a human papillomavirus L1 (HPV L1) protein, a matrix protein M1 from influenza A virus, a ferritin, a riboflavin synthase, dihydrolipoyl acetyltransferase (E2p), or a combination thereof, including their codon optimized nucleic acid sequences, fragments, mutants, or variants thereof. 101. The multisubunit peptide according to paragraph 100, wherein the self-assembling peptide is a ferritin comprising a ferritin subunit or a ferritin peptide, a dihydrolipoyl acetyltransferase (E2p), a lumazine synthase, an MS2 coat protein, or a combination thereof. 102. The multisubunit peptide according to paragraph 101, wherein the ferritin peptide is obtained or derived from Helicobacter pylori ferritin or Listeria innocua ferritin, the lumazine synthase is obtained or derived from Aquifex aeolicus or Bacillus subtilis, the MS2 coat protein is obtained or derived from Emesvirus zinderi, and the dihydrolipoyl acetyltransferase (E2p) is obtained or derived from Bacillus stearothermophilus. 103. The multisubunit peptide according to any one of the paragraphs 74-102, wherein the cleavage peptide is a golgi specific cleavage peptide, a self-cleaving cleavage peptide or a combination thereof. 104. The multisubunit peptide according to any one of the paragraphs 74-103, wherein the signal peptide is present on the amino-terminus of one or more polypeptides. 105. The multisubunit peptide according to any one of the paragraphs 74-104, wherein the multisubunit peptide comprises an amino acid sequence of SEQ ID NO: 98 106. The multisubunit peptide according to any one of the paragraphs 74-105, wherein total number of the polypeptides are not more than 100. 107. The multisubunit peptide according to paragraph 106, wherein total number of the polypeptide are between 2-5, 2-10, 10-20, 20-30, 30-40, 40-50, 50-60, 60-70, 70-80, 80-90, or 90-99. 108. A polypeptide nanoparticle comprising at least 2 or up to 500 polypeptides according to any one of the paragraphs 5-56 or 74-107. 109. The polypeptide nanoparticle according to paragraphs 108, wherein the polypeptide nanoparticle is icosahedral, helical, spherical, rod-like or a combination thereof. 110. A vaccine comprising the nucleic acid according to any one of the paragraphs 1-56. 111. A vaccine comprising the lipid nanoparticle composition according to any one of the paragraphs 57-72. 112. A vaccine comprising the multisubunit peptide according to any one of the paragraphs 74-107. 113. A vaccine comprising the polypeptide nanoparticle according to any one of the paragraphs 108-109. 114. A method of treating or preventing a disease, comprising administering to a subject in need thereof the nucleic acid according to any one of the paragraphs 1-56 or the vaccine according to paragraph 110. 115. A method of treating or preventing a disease, comprising administering to a subject in need thereof the lipid nanoparticle composition according to any one of the paragraphs 57-72 or the vaccine according to paragraph 111. 116. A method of treating or preventing a disease, comprising administering to a subject in need thereof the multisubunit peptide according to any one of the paragraphs 74- 107 or the vaccine according to paragraph 112. 117. A method of treating or preventing a disease, comprising administering to a subject in need thereof the polypeptide nanoparticle according to any one of the paragraphs 108-109 or the vaccine according to paragraph 113. 118. The method according to any one of the paragraphs 114-117, wherein the disease is COVID-19. 119. Use of the nucleic acid according to any one of the paragraphs 1-56 or the vaccine according to paragraph 110, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. 120. Use of the lipid nanoparticle composition according to any one of the paragraphs 57- 72 or the vaccine according to paragraph 111, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. 121. Use of the multisubunit peptide according to any one of the paragraphs 74-107 or the vaccine according to paragraph 112, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. 122. Use of the polypeptide nanoparticle according to any one of the paragraphs 108-109 or the vaccine according to paragraph 113, in the manufacture of a medicament for the treatment or prevention of a disease in a subject. 123. The use according to any one of the paragraphs 119-122, wherein the disease is a COVID-19. The present disclosure is further exemplified by the following non limiting examples. It should be understood that the examples are provided to illustrate the disclosure. From the description and the exemplified embodiments and examples, one skilled in the art can make various modifications or adaptations to the disclosure. Such modifications or adaptations are deemed to be within the scope of the spirit of the disclosure. Examples Example 1: Synthesis of nucleic acid sequence (mRNA) encoding polypeptide of SEQ ID NO: 94 Plasmid DNA construction The nucleic acid sequence of example 1 comprising a signal sequence (encoding a signal peptide), a receptor binding domain sequence (encoding the receptor binding domain (RBD) of SEQ ID NO: 2), a self-assembling sequence (ferritin sequence encoding ferritin), and a linker sequence (glycine serine linker sequence encoding glycine serine linker) connecting the receptor binding domain sequence with the self-assembling sequence was codon optimized for human expression. 5’ UTR, Cap, and 3’ UTR sequences were also included in the nucleic acid sequence. XbaI site was added to the 3’ terminus of the 3’ UTR for vector linearization. The nucleic acid sequence construct was inserted between HindIII and BamHI restriction sites of pTwist Kan High Copy plasmid (Twist BioScience, USA). The nucleic acid sequence was synthesized at Twist BioSciences, USA. Sequence of the polypeptide encoded by the above nucleic acid sequence of example 1, is provided in Table 1. Table 1: shows amino acid sequence of the polypeptide encoded by the nucleic acid sequence of example 1 - polypeptide of SEQ ID NO: 94. Signal Peptide MGVKVLFALICIAVAEA (SEQ ID NO: 93) RVQPTESIVRFPNVTNLCPFHEVFNATR FASVYAWNRTRISNCVADYSVLYNFAP FFAFKCYGVSPTKLNDLCFTNVYADSF RBD of SEQ VIKGNEVSQIAPGQTGNIADYNYKLPD ID NO: 2 DFTGCVIAWNSNKLDSTHSGNYDYWY RSLRKSKLKPFERDISTEIYQAGNKPCK GPGPNCYFPLQSYGFRPTYGVGHQPYR VVVLSFELLHGPATVCGPKKSTNLVKN KCVNF (SEQ ID NO: 2) Polypeptide Linker Peptide (glycine serine GGSGGGGSGG (SEQ ID NO: 21) linker) LSKDIIKLLNEQVNKEMNSSNLYMSMS Self- SWCYTHSLDGAGLFLFDHAAEEYEHA Assembling KKLIIFLNENNVPVQLTSISAPEHKFEGL peptide TQIFQKAYEHEQHISESINNIVDHAIKSK (ferritin DHATFNFLQWYVAEQHEEEVLFKDILD peptide) KIELIGNENHGLYLADQYVKGIRRKR (SEQ ID NO: 8) Cleavage Peptide SVSGSGATNFSLLKQAGDVEENPGP (SEQ ID NO: 73) Note: Cleavage peptide (encoded by cleavage sequence) is not necessary for nucleic acid sequence that do not encode a multisubunit peptide. It was included in the construct of example 1, so that a nucleic acid encoding multisubunit peptide could be easily constructed to include this sequence. Its presence or absence is immaterial in nucleic acid sequences that only encodes polypeptide, and not the multisubunit peptide. Amino acid sequence of different peptides present in the polypeptide encoded by the nucleic acid sequence of example 1 is separately identif...

Claims

What is claimed is:

1. A receptor binding domain comprising one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO:

1.

2. The receptor binding domain according to claim 1, wherein the receptor binding domain has at least 50% identity compared to SEQ ID NO:

1.

3. The receptor binding domain according to any one of the claims 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions K38T, F138L, V165del, E166P, A202G, or a combination thereof compared to SEQ ID NO:

1.

4. The receptor binding domain according to any one of the claims 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions R28T, K38T, F138L, V165del, E166K, or a combination thereof compared to SEQ ID NO:

1.

5. The receptor binding domain according to any one of the claims 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions R28T, K38V, F138L, A157V, E166A, S176P, or a combination thereof compared to SEQ ID NO:

1.

6. The receptor binding domain according to any one of the claims 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions R28T, K38T, F138L, V165del, E166K, Q175E, or a combination thereof compared to SEQ ID NO:

1.

7. The receptor binding domain according to any one of the claims 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions K38T, V165del, E166K, or a combination thereof compared to SEQ ID NO:

1.

8. The receptor binding domain according to any one of the claims 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions R28T and F138L compared to SEQ ID NO:

1.

9. The receptor binding domain according to any one of the claims 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions K38V or T, A157V, and S176P compared to SEQ ID NO: 1.

10. The receptor binding domain according to any one of the claims 1-2, wherein the receptor binding domain comprises a mutation at amino acid positions K126T, F138L, E166A or K or P, and A202G compared to SEQ ID NO:

1.

11. The receptor binding domain according to any one of the preceding claims, wherein the receptor binding domain has an amino acid sequence of any one of SEQ ID NOs: 2-6.

12. The receptor binding domain according to any one of the preceding claims, wherein the receptor binding domain comprises one or more signal peptide on the amino- terminus of the receptor binding domain.

13. A composition comprising the receptor binding domain according to any one of the preceding claims and a pharmaceutically acceptable excipient.

14. The composition according to claim 13, wherein the pharmaceutically acceptable excipient is selected from the group comprising buffering agent, stabilizer, tonicity modifier, surfactant, chelating agent, salt, anti-oxidant, diluent, preservative, or a combination thereof.

15. A nucleic acid encoding the receptor binding domain according to any one of the claims 1-12.

16. The nucleic acid according to claim 15, wherein the nucleic acid is a DNA, an RNA, or an mRNA.

17. A vector comprising the nucleic acid of claim 16.

18. A lipid nanoparticle composition comprising a cationic lipid, a phospholipid, a sterol, a PEG-lipid, and the nucleic acid of claim 16.

19. The lipid nanoparticle composition according to claim 18, wherein the cationic lipid is present in an amount from 10 mol percent to 70 mol percent.

20. The lipid nanoparticle composition according to claim 18, wherein the phospholipid is present in an amount from 2 mol percent to 65 mol percent.

21. The lipid nanoparticle composition according to claim 18, wherein the sterol is present in an amount from 20 mol percent to 65 mol percent.

22. The lipid nanoparticle composition according to claim 18, wherein the PEG-lipid is present in an amount from 0.2 mol percent to 2.0 mol percent.

23. The lipid nanoparticle composition according to claim 18, additionally comprising an ionizable polymer.

24. The lipid nanoparticle composition according to claim 23, wherein the ionizable polymer is present in an amount from 1 mol percent to 25 mol percent.

25. The lipid nanoparticle composition according to any one of the claims 18-24, wherein the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315, or a combination thereof.

26. A vaccine comprising the receptor binding domain according to any one of the claims 1-12.

27. A vaccine comprising the composition according to any one of the claims 13-14.

28. A vaccine comprising the nucleic acid according to claim 16.

29. A vaccine comprising the lipid nanoparticle composition according to any one of the claims 18-25.

30. A method of treating or preventing a disease, comprising administering to a subject in need thereof the receptor binding domain according to any one of the claims 1-12 or the vaccine according to claim 26.

31. A method of treating or preventing a disease, comprising administering to a subject in need thereof the composition according to any one of the claims 13-14 or the vaccine according to claim 27.

32. A method of treating or preventing a disease, comprising administering to a subject in need thereof the nucleic acid according to claim 16 or the vaccine according to claim 28.

33. A method of treating or preventing a disease, comprising administering to a subject in need thereof the lipid nanoparticle composition according to any one of the claims 18-25 or the vaccine according to claim 29.

34. The method according to any one of the claims 30-33, wherein the disease is COVID- 19.

35. A polypeptide comprising a receptor binding domain, a self-assembling peptide, and a linker peptide connecting the receptor binding domain and the self-assembling peptide, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO: 1.

36. The polypeptide according to claim 35, wherein the receptor binding domain has at least 50% identity compared to SEQ ID NO:

1.

37. The polypeptide according to any one of the claims 35-36, wherein the receptor binding domain comprises a mutation at amino acid positions K38T, F138L, V165del, E166P, A202G, or a combination thereof compared to SEQ ID NO:

1.

38. The polypeptide according to any one of the claims 35-36, wherein the receptor binding domain comprises a mutation at amino acid positions R28T, K38T, F138L, V165del, E166K, or a combination thereof compared to SEQ ID NO:

1.

39. The polypeptide according to any one of the claims 35-36, wherein the receptor binding domain comprises a mutation at amino acid positions R28T, K38V, F138L, A157V, E166A, S176P, or a combination thereof compared to SEQ ID NO:

1.

40. The polypeptide according to any one of the claims 35-36, wherein the receptor binding domain comprises a mutation at amino acid positions R28T, K38T, F138L, V165del, E166K, Q175E, or a combination thereof compared to SEQ ID NO:

1.

41. The polypeptide according to any one of the claims 35-36, wherein the receptor binding domain comprises a mutation at amino acid positions K38T, V165del, E166K, or a combination thereof compared to SEQ ID NO:

1.

42. The polypeptide according to any one of the claims 35-36, wherein the receptor binding domain comprises a mutation at amino acid positions R28T and F138L compared to SEQ ID NO:

1.

43. The polypeptide according to any one of the claims 35-36, wherein the receptor binding domain comprises a mutation at amino acid positions K38V or T, A157V, and S176P compared to SEQ ID NO:

1.

44. The polypeptide according to any one of the claims 35-36, wherein the receptor binding domain comprises a mutation at amino acid positions K126T, F138L, E166A or K or P, and A202G compared to SEQ ID NO:

1.

45. The polypeptide according to any one of the claims 35-44, wherein the receptor binding domain has an amino acid sequence of any one of SEQ ID NOs: 2-6.

46. The polypeptide according to any one of the claims 35-45, wherein the polypeptide comprises one or more signal peptide on the amino-terminus of the polypeptide.

47. The polypeptide according to any one of the claims 35-46, wherein the linker peptide is an amino acid linker, a foldon, a scaffold, or a combination thereof.

48. The polypeptide according to claim 47, wherein the linker peptide is the amino acid linker.

49. The polypeptide according to claim 48, wherein the amino acid linker comprises 2 to 49 amino acids.

50. The polypeptide according to any one of the claims 47-49, wherein the amino acid linker is a glycine serine linker, a glycine proline linker, a glycine threonine linker, an alanine serine linker, any combination of two amino acids, or a combination thereof.

51. The polypeptide according to any one of the claims 35-50, wherein the linker peptide has an amino acid sequence of any one of SEQ ID NOs: 18-57.

52. The polypeptide according to any one of the claims 35-51, wherein the self- assembling peptide is a lumazine synthase, an MS2 coat protein, a hepatitis B surface antigen (HBsAg) from Hepatitis B Virus, a hepatitis B core antigen (HbcAg) from Hepatitis B virus, a human papillomavirus L1 (HPV L1) protein, a ferritin, a riboflavin synthase, a dihydrolipoyl acetyltransferase (E2p), or a combination thereof, including their codon optimized nucleic acid sequences, fragments, mutants, variants, comparable equivalents, or functional analogs thereof.

53. The polypeptide according to claim 52, wherein the self-assembling peptide is a ferritin comprising a ferritin subunit or a ferritin peptide, a dihydrolipoyl acetyltransferase (E2p), a lumazine synthase, an MS2 coat protein, or a combination thereof.

54. The polypeptide according to claim 53, wherein the ferritin peptide is obtained or derived from Helicobacter pylori ferritin or Listeria innocua ferritin, the lumazine synthase is obtained or derived from Aquifex aeolicus or Bacillus subtilis, the MS2 coat protein is obtained or derived from Emesvirus zinderi, and the dihydrolipoyl acetyltransferase (E2p) is obtained or derived from Bacillus stearothermophilus.

55. The polypeptide according to any one of the claims 35-54, wherein the self- assembling peptide has an amino acid sequence of any one of SEQ ID NOs: 7-17 or 99-102.

56. The polypeptide according to any one of the claims 35-55, wherein the polypeptide comprises an amino acid sequence of any one of SEQ ID NOs: 94-97 or 103.

57. A composition comprising the polypeptide according to any one of the claims 35-56 and a pharmaceutically acceptable excipient.

58. The composition according to claim 57, wherein the pharmaceutically acceptable excipient is selected from the group comprising buffering agent, stabilizer, tonicity modifier, surfactant, chelating agent, salt, anti-oxidant, diluent, preservative, or a combination thereof.

59. A nucleic acid encoding the polypeptide according to any one of the claims 35-56.

60. The nucleic acid according to claim 59, wherein the nucleic acid is a DNA, an RNA, or an mRNA.

61. A vector comprising the nucleic acid of claim 60.

62. A lipid nanoparticle composition comprising a cationic lipid, a phospholipid, a sterol, a PEG-lipid and the nucleic acid according to claim 60.

63. The lipid nanoparticle composition according to claim 62, wherein the cationic lipid is present in an amount from 10 mol percent to 70 mol percent.

64. The lipid nanoparticle composition according to claim 62, wherein the phospholipid is present in an amount from 2 mol percent to 65 mol percent.

65. The lipid nanoparticle composition according to claim 62, wherein the sterol is present in an amount from 20 mol percent to 65 mol percent.

66. The lipid nanoparticle composition according to claim 62, wherein the PEG-lipid is present in an amount from 0.2 mol percent to 2.0 mol percent.

67. The lipid nanoparticle composition according to claim 62, additionally comprising an ionizable polymer.

68. The lipid nanoparticle composition according to claim 67, wherein the ionizable polymer is present in an amount from 1 mol percent to 25 mol percent.

69. The lipid nanoparticle composition according to any one of the claims 62-68, wherein the cationic lipid is represented by any one of formula (I), formula (II), formula (III), formula (IV), formula (V), formula (VI), formula (VII), formula (VIII), SM-102, ALC-0315, or a combination thereof.

70. A polypeptide nanoparticle comprising at least 2 or up to 500 polypeptides according to any one of the claims 35-56.

71. The polypeptide nanoparticle according to claim 70, wherein the polypeptide nanoparticle is icosahedral, helical, spherical, rod-like or a combination thereof.

72. A vaccine comprising the polypeptide according to any one of the claims 35-56.

73. A vaccine comprising the composition according to any one of the claims 57-58.

74. A vaccine comprising the nucleic acid according to claim 60.

75. A vaccine comprising the lipid nanoparticle composition according to any one of the claims 62-69.

76. A vaccine comprising the polypeptide nanoparticle according any one of the claims 70-71.

77. A method of treating or preventing a disease, comprising administering to a subject in need thereof the polypeptide according to any one of the claims 35-56 or the vaccine according to claim 72.

78. A method of treating or preventing a disease, comprising administering to a subject in need thereof the composition according to any one of the claims 57-58 or the vaccine according to claim 73.

79. A method of treating or preventing a disease, comprising administering to a subject in need thereof the nucleic acid according claim 60 or the vaccine according to claim 74.

80. A method of treating or preventing a disease, comprising administering to a subject in need thereof the lipid nanoparticle composition according to any one of the claims 62-69 or the vaccine according to claim 75.

81. A method of treating or preventing a disease, comprising administering to a subject need thereof the polypeptide nanoparticle according to any one of the claims 70-71 or the vaccine according to claim 76.

82. The method according to any one of the claims 77-81, wherein the disease is COVID- 19.

83. A nucleic acid comprising a plurality of polynucleotide sequences, wherein some or all polynucleotide sequences of the plurality comprises either a receptor binding domain sequence, a linker sequence, and a self-assembling sequence or a linker sequence, a receptor binding domain sequence, a linker sequence and a self- assembling sequence or a combination thereof, wherein each polynucleotide sequence of the plurality is connected to an adjacent polynucleotide sequence of the plurality by a cleavage sequence, wherein the nucleic acid further comprises a signal sequence upstream of one or more of the polynucleotide sequences of the plurality, and wherein the receptor binding domain sequence comprises a mutation at: (a) a codon encoding an amino acid R at the position corresponding to the position 28 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid R with an amino acid T,(b) a codon encoding an amino acid K at the position corresponding to the position 38 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid V or T, (c) a codon encoding an amino acid K at the position corresponding to the position 126 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid K with an amino acid T, (d) a codon encoding an amino acid F at the position corresponding to the position 138 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid F with an amino acid L, (e) a codon encoding an amino acid A at the position corresponding to the position 157 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid V, (f) a codon encoding an amino acid V at the position corresponding to the position 165 of the SEQ ID NO: 1, wherein the mutation is a deletion, (g) a codon encoding an amino acid E at the position corresponding to the position 166 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid E with an amino acid A, or K, or P, (h) a codon encoding an amino acid Q at the position corresponding to the position 175 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid Q with an amino acid E, (i) a codon encoding an amino acid S at the position corresponding to the position 176 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid S with an amino acid P, (j) a codon encoding an amino acid A at the position corresponding to the position 202 of the SEQ ID NO: 1, wherein the mutation is a substitution replacing the amino acid A with an amino acid G, or a combination thereof.

84. The nucleic acid according to claim 83, wherein the receptor binding domain sequence, the linker sequence, and the self-assembling sequence or the linker sequence, the receptor binding domain sequence, the linker sequence, and the self- assembling sequence are in 5’ to 3’ order.

85. A nucleic acid encoding a plurality of polypeptides, wherein some or all polypeptides of the plurality comprises either a receptor binding domain, a linker peptide, and a self-assembling peptide or a linker peptide, a receptor binding domain, a linkerpeptide and a self-assembling peptide or a combination thereof, wherein each polypeptide of the plurality is connected to an adjacent polypeptide of the plurality by a cleavage peptide, and wherein the nucleic acid further encodes a signal peptide on the amino-terminus of one or more of the polypeptides of the plurality, wherein the receptor binding domain comprises one or more mutations at amino acid positions selected from the group comprising R28T, K38V or T, K126T, F138L, A157V, V165del, E166A or K or P, Q175E, S176P, A202G, or a combination thereof compared to SEQ ID NO:

1.

86. The nucleic acid according to claim 85, wherein the receptor binding domain, the linker peptide, and the self-assembling peptide or the linker peptide, the receptor binding domain, the linker peptide, and the self-assembling peptide are in N-terminus to C-terminus order.

87. The nucleic acid according to any one of the claims 83-86, wherein total number of the polynucleotide sequences are not more than 100.

88. The nucleic acid according to claim 87, wherein total number of the polynucleotide sequences are between 2-5, 2-10, 10-20, 20-30, 30-40, 40-50, 50-60, 60-70, 70-80, 80-90, or 90-99.

89. The nucleic acid according to any one of the claims 83-88, wherein the nucleic acid is a DNA or an RNA.

90. The nucleic acid according to claim 89, wherein the RNA is an mRNA.

91. The nucleic acid according to claim 90, wherein the mRNA is 0.3 kb to 1 kb, 1 kb to 2 kb, 2 kb to 3 kb, 3 kb to 4 kb, 4 kb to 5 kb, 5 kb to 6 kb, 6 kb to 7 kb, 7 kb to 8 kb, 8 kb to 9 kb, 9 kb to 10 kb, 10 kb to 11 kb, 11 kb to 12 kb, 12 kb to 13 kb, 13 kb to 14 kb, 14 kb to 15 kb, 15 kb to 16 kb, 16 kb to 17 kb, 17 kb to 18 kb, 18 kb to 19 kb, 19 kb to 20 kb in length, or any range therein.

92. The nucleic acid according to any one of the claims 90-91, wherein the mRNA is obtained through a single IVT process or step.

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