Mutated VSV extracellular domain polypeptides and uses thereof

Abstract

The present invention relates to a mutant polypeptide comprising an amino acid sequence of an extracellular domain of glycoprotein G of a vesicular stomatitis virus (VSV) strain, wherein the extracellular domain comprises an amino acid sequence listed in SEQ ID NO: 2 or a sequence having at least 50% identity with the amino acid sequence listed in SEQ ID NO: 2, and the sequence has a substitution of at least one amino acid residue selected from the following: a) any amino acid residue located at positions 421 to 429 and any amino acid residue located at positions 17 to 25 of SEQ ID NO: 2; or b) any amino acid residue located at a position corresponding to position 421 to a position corresponding to position 429 of SEQ ID NO: 2 and any amino acid residue located at a position corresponding to position 17 to a position corresponding to position 25 of SEQ ID NO: 2 after optimal global alignment with SEQ ID NO: 2.

Description

Technical Field

[0001] The present invention is in the field of viruses with improved properties, more specifically VSV viruses with improved properties, in particular for use in oncolytic cancer therapy, gene therapy, immunotherapy and selective delivery of cargo to selected cell types, and relates to mutant polypeptides comprising the amino acid sequence of the glycoprotein G ectodomain of a vesicular stomatitis virus (VSV) strain, wherein the ectodomain comprises the amino acid sequence as set forth in SEQ ID NO: 2, or a sequence having at least 50% identity to the amino acid sequence set forth in SEQ ID NO: 2, said sequence having at least one substitution of an amino acid residue selected from the group consisting of:

[0002] a) any of the amino acid residues at positions 421 to 429 and any of the amino acid residues at positions 17 to 25 of SEQ ID NO: 2; or

[0003] b) any amino acid residue at a position corresponding to position 421 to a position corresponding to position 429 of SEQ ID NO: 2 and any amino acid residue at a position corresponding to position 17 to a position corresponding to position 25 of SEQ ID NO: 2 after optimal global alignment with SEQ ID NO: 2. Background Art

[0004] Vesicular stomatitis virus (VSV) is an enveloped negative-strand RNA virus belonging to the genus Vesiculovirus of the family Rhabdovirus. It is an arbovirus that can infect insects, cattle, horses, and pigs. In mammals, its ability to infect and kill tumor cells while sparing normal cells makes it a promising oncolytic virus for the treatment of cancer (Barber. Oncogene 24, 7710–7719 (2005); Fernandez et al., J. Virol. 76, 895–904 (2002); Hastie et al., Virus Res. 176, 16–32 (2013)).

[0005] The VSV genome consists of an 11 kb single-stranded negative-sense RNA ( Figure 1 A). It contains five genes encoding five structural proteins; one of which specifically encodes the transmembrane glycoprotein glycoprotein G ( Figure 1 A and Figure 1B). Glycoprotein G plays a key role in the early stages of infection (Albertini et al., Viruses 4, 117–139 (2012)). First, it allows viral attachment by interacting with its cellular receptor (LDL-R or a member of the LDL-R family). Then, after endocytosis of the virion, glycoprotein G undergoes a conformational change induced by acidification within the endosome, changing from a pre-fusion form to a post-fusion form. This structural transition catalyzes the fusion of the viral and endosomal membranes.

[0006] Glycoprotein G is the only protein responsible for VSV tropism. Due to the ubiquitous nature of LDL-R family members, this tropism is broad, allowing VSV to enter many cell types. This is why, for example, VSV glycoprotein G is used in many quasi-retroviral vectors. However, despite this broad tropism, some cell types have only low expression levels or do not carry VSV receptors (such as resting T cells, B cells, and CD341 cells) (Amirache. Blood 123, 1422–4 (2014)).

[0007] Therefore, there is a need for modified VSV viruses with altered tropism.Such modified VSV viruses can infect cell types that do not carry the native VSV receptor.

[0008] To overcome this problem, the inventors attempted to identify sites that allow the insertion of targeting moieties (such as nanobodies) sequences, in particular targeting moieties that recognize a given receptor, into the amino acid sequence of VSV glycoprotein G. In particular, the insertion should not interfere with the membrane fusion properties of glycoprotein G.

[0009] The inventors analyzed several insertion sites and demonstrated that the amino-terminal site tolerated the insertion of nanobodies. The first chimera thus generated ( Figure 2 GNano, described precisely in

[15] , is correctly folded and transported to the cell membrane. It retains its fusogenic properties (albeit impaired). Summary of the Invention

[0010] In the context of the present invention, the inventors subsequently constructed a recombinant VSV in which the gene encoding wild-type glycoprotein G was replaced by the gene encoding GNano (the first chimera). However, amplification of this initial recombinant VSV virus was very difficult; only a very low infectious titer of ∼1.8 × 10 was obtained after 24 h of amplification in BSR cells. 6 Such low titers are incompatible with industrial production of targeted VSV viruses for therapeutic use.

[0011] The inventors then passaged the recombinant virus several times on BSR cells to select mutations that improved its amplification. After 10 passages, genome sequencing of the virus population showed that a variant containing two mutations in the nucleotide sequence of the glycoprotein gradually invaded the population, resulting in the histidine residue at position 22 being converted to asparagine (H22N substitution) and the serine residue at position 422 being converted to isoleucine (S422I substitution). The titer of the recombinant virus obtained after this optimization was approximately 10 8 pfu / ml.

[0012] Surprisingly, the inventors thus found that the combination of two mutations (H22N and S422I) allowed the production of ∼10 8 pfu / ml of recombinant virus (GNano H22N S422I or improved chimera, see Figure 2 )(See Example 1).

[0013] Furthermore, the inventors found that the S422I substitution rescued the G fusion property, while the H407A substitution completely abolished this property. In this context, the inventors demonstrated that S422I promoted G folding and stabilized the G prefusion form by showing that it improved LDL-R CR domain recognition (the structural transition to the postfusion state disrupted the CR domain binding site).

[0014] In the case of GNano H22N, the inventors also demonstrated that substitutions of S422F, S422M, S422L or S422V had similar phenotypes as S422I.

[0015] The inventors also demonstrated that, in the presence of H22N substitutions and / or S422I, S422F, S422M, S422L or S422V substitutions, recombinant VSV expressing a fusion polypeptide was able to form syncytia when exposed to a low pH between 5.5 and 6.3, similar to wild-type VSV Indiana, wherein the fusion polypeptide consists of a VSV Indiana G signal peptide, a dipeptide linker, an anti-GFP nanobody, a GGGGSGGGGS (SEQ ID NO: 81) linker, and a VSV Indiana G extracellular domain having one of the S422I, S422F, S422M, S422L and S422V substitutions. This also suggests that the presence of a hydrophobic residue at position 422 is key to regulating pH-dependent structural transitions and promotes G folding and stabilizing the prefusion form of a G fusion polypeptide having a nanobody inserted into the N-terminus of the extracellular domain (see Example 3). This was also confirmed by the crystal structure of the VSV G extracellular domain resolved by the inventors. In fact, the inventors surprisingly showed that the C-terminal portion (residues 407 to residue 429, more specifically the region located at residues 421 to residue 429, and even more specifically the region at residues 421 to residue 425) interacts to a large extent with the fusion domain and thus helps to stabilize the prefusion complex. The crystal structure further revealed that compensatory substitution of the S422 residue with a hydrophobic residue (such as I, F, M, L or V) stabilizes the β-hairpin structure (and thus stabilizes the prefusion state) through hydrophobic interactions (see Example 4).

[0016] In a first aspect, the present invention therefore relates to a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence of the glycoprotein G extracellular domain of a vesicular stomatitis virus (VSV) strain, wherein the extracellular domain comprises, consists essentially of, or consists of the amino acid sequence set forth in SEQ ID NO: 2, or a sequence having at least 50% identity to the amino acid sequence set forth in SEQ ID NO: 2, said sequence having at least one substitution of an amino acid residue selected from the group consisting of:

[0017] a) any of the amino acid residues at positions 421 to 429 and any of the amino acid residues at positions 17 to 25 of SEQ ID NO: 2, preferably any of the amino acid residues at positions 421 to 425 and any of the amino acid residues at positions 17 to 25 of SEQ ID NO: 2, more preferably any of the amino acid residues at positions 422 and 22 of SEQ ID NO: 2; or

[0018] b) any amino acid residue at a position equivalent to position 421 to a position equivalent to position 429 of SEQ ID NO: 2 and any amino acid residue at a position equivalent to position 17 to a position equivalent to position 25 of SEQ ID NO: 2 after optimal global alignment with SEQ ID NO: 2, preferably any amino acid residue at a position equivalent to position 421 to a position equivalent to position 425 of SEQ ID NO: 2 and any amino acid residue at a position equivalent to position 17 to a position equivalent to position 25 of SEQ ID NO: 2 after optimal global alignment with SEQ ID NO: 2, more preferably any amino acid residue at a position equivalent to position 422 and position 22 of SEQ ID NO: 2 after optimal global alignment with SEQ ID NO: 2.

[0019] The present invention also relates to a fusion polypeptide comprising, consisting essentially of, or consisting of a mutant polypeptide according to the present invention and an additional peptide, polypeptide or protein, wherein the additional peptide, polypeptide or protein is inserted between:

[0020] a) the N-terminus of the mutated polypeptide,

[0021] b) located between any two consecutive amino acids in the region corresponding to positions 192 to 202 of SEQ ID NO: 2 or in the equivalent positions after optimal global alignment with SEQ ID NO: 2,

[0022] c) between any two consecutive amino acids in the region corresponding to positions 240 to 257 of SEQ ID NO: 2 or in the equivalent positions after optimal global alignment with SEQ ID NO: 2,

[0023] d) located between any two consecutive amino acids in the region corresponding to positions 347 to 353 of SEQ ID NO: 2 or in the equivalent positions after optimal global alignment with SEQ ID NO: 2,

[0024] e) located between any two consecutive amino acids in the region corresponding to positions 364 to 366 of SEQ ID NO: 2 or in the equivalent positions after optimal global alignment with SEQ ID NO: 2,

[0025] f) between any two consecutive amino acids in the region corresponding to positions 376 to 379 of SEQ ID NO: 2 or in the equivalent positions after optimal global alignment with SEQ ID NO: 2,

[0026] Preferably, the additional peptide, polypeptide or protein is inserted at: the N-terminus of the mutant polypeptide, or between any two consecutive amino acids at positions 351 and 352 of SEQ ID NO: 2 or equivalent positions after optimal global alignment with SEQ ID NO: 2.

[0027] The present invention also relates to nucleic acid molecules encoding a mutant polypeptide or a fusion polypeptide according to the present invention.

[0028] The present invention further relates to a vector comprising at least one nucleic acid according to the invention or expressing a mutant polypeptide or a fusion polypeptide according to the invention.

[0029] The present invention also relates to a host cell containing or expressing a mutant polypeptide or fusion polypeptide according to the invention, or containing a nucleic acid molecule according to the invention, or containing a vector according to the invention (in particular a VSV vector).

[0030] The present invention also relates to a composition comprising, consisting essentially of, or consisting of a mutant polypeptide or fusion polypeptide according to the invention, a nucleic acid molecule according to the invention, a vector according to the invention, a host cell according to the invention, or any combination thereof.

[0031] The present invention also relates to therapeutic uses of a mutant polypeptide or fusion polypeptide according to the invention, a nucleic acid molecule according to the invention, a vector according to the invention, a host cell according to the invention, a composition according to the invention, or any combination thereof.

[0032] The present invention also relates to a mutant polypeptide according to the present invention or a fusion polypeptide according to the present invention for targeting a lipid membrane to a specific target, such as a cell, in a subject, in particular a cell to be killed (such as a cancer cell), wherein the mutant polypeptide or fusion polypeptide is anchored in the lipid membrane.

[0033] The present invention also relates to the in vitro use of a mutant polypeptide according to the present invention or a fusion polypeptide according to the present invention for targeting a lipid membrane to a specific target, such as a cell, in particular a cell to be killed (such as a cancer cell), wherein the mutant polypeptide or fusion polypeptide is anchored in the lipid membrane. BRIEF DESCRIPTION OF THE DRAWINGS

[0034] Figure 1 A. The VSV genome is a single RNA molecule of negative polarity; it encodes five structural proteins: N (nucleoprotein), P (phosphoprotein), M (matrix protein), G (glycoprotein), and L (large RNA-dependent RNA polymerase). B. VSV is an enveloped virus, with glycoprotein G being the only protein on the viral exterior. This protein is involved in the steps of viral entry (receptor interaction and membrane fusion).

[0035] Figure 2Schematic diagram of the first chimera (GNano) and the improved chimera (GNano H22N S422I). Selected mutations are indicated. (SP: signal peptide of VSV glycoprotein G, Nano: Nanobody, G: glycoprotein G of VSV). Also indicated are the additional inserts (dipeptide QF and linker with the sequence GGGGSGGGGS (SEQ ID NO: 81)).

[0036] Figure 3A Using Emboss Needle software and default parameters, an optimal global alignment of the amino acid sequences of the glycoprotein G ectodomain of VSV Indiana (SEQ ID NO: 2) and Maraba (SEQ ID NO: 4) strains was performed. Positions 17-25 and 421-429 of SEQ ID NO: 2 and the equivalent positions of SEQ ID NO: 4 (also positions 17-25 and 421-429) are boxed. Preferred substitution positions (positions 22 and 422 of SEQ ID NO: 2 and SEQ ID NO: 4) are further boxed. The default parameters used are indicated. The percent identity ("Identity"), percent similarity ("Similarity"), and similarity score ("Score") obtained are indicated.

[0037] Figure 3B Using Emboss Needle software and default parameters, an optimal global alignment of the amino acid sequences of the glycoprotein G ectodomain of VSV Indiana (SEQ ID NO: 2) and Cocal (SEQ ID NO: 6) strains was performed. Positions 17-25 and 421-429 of SEQ ID NO: 2 and the equivalent positions of SEQ ID NO: 6 (also positions 17-25 and 421-429) are boxed. Preferred substitution positions (positions 22 and 422 of SEQ ID NO: 2 and SEQ ID NO: 6) are further boxed. The default parameters used are indicated. The percentage identity ("Identity"), percentage similarity ("Similarity"), and similarity score ("Score") obtained are indicated.

[0038] Figure 3CUsing Emboss Needle software and default parameters, an optimal global alignment of the amino acid sequences of the glycoprotein G ectodomain of VSV Indiana (SEQ ID NO: 2) and Morreton (SEQ ID NO: 8) strains was performed. Positions 17-25 and 421-429 of SEQ ID NO: 2 and the equivalent positions of SEQ ID NO: 8 (also positions 17-25 and 421-429) are boxed. Preferred substitution positions (positions 22 and 422 of SEQ ID NO: 2 and SEQ ID NO: 8) are further boxed. The default parameters used are indicated. The percent identity ("Identity"), percent similarity ("Similarity"), and similarity score ("Score") obtained are indicated.

[0039] Figure 3D Using Emboss Needle software and default parameters, an optimal global alignment of the amino acid sequences of the glycoprotein G ectodomain of VSV Indiana (SEQ ID NO: 2) and Alagoa (SEQ ID NO: 10) strains was performed. Positions 17-25 and 421-429 of SEQ ID NO: 2 and the equivalent positions of SEQ ID NO: 10 (also positions 17-25 and 421-429) are boxed. Preferred substitution positions (positions 22 and 422 of SEQ ID NO: 2 and SEQ ID NO: 10) are further boxed. The default parameters used are indicated. The percent identity ("Identity"), percent similarity ("Similarity"), and similarity score ("Score") obtained are indicated.

[0040] Figure 3E Using Emboss Needle software and default parameters, an optimal global alignment of the amino acid sequences of the glycoprotein G ectodomain of VSV Indiana (SEQ ID NO: 2) and New Jersey (SEQ ID NO: 12) strains was performed. Positions 17-25 and 421-429 of SEQ ID NO: 2 and the equivalent positions (positions 17-25 and 428-436) of SEQ ID NO: 12 are boxed. The preferred substitution position 429 (positions 22 and 422 of SEQ ID NO: 2 and positions 22 and 429 of SEQ ID NO: 12) is further boxed. The default parameters used are indicated. The percent identity ("Identity"), percent similarity ("Similarity"), and similarity score ("Score") obtained are indicated.

[0041] Figure 3FUsing Emboss Needle software and default parameters, an optimal global alignment of the amino acid sequences of the glycoprotein G ectodomain of VSV Indiana (SEQ ID NO: 2) and Carajas (SEQ ID NO: 14) strains was performed. Positions 17-25 and 421-429 of SEQ ID NO: 2 and the equivalent positions (positions 17-25 and 425-433) of SEQ ID NO: 14 are boxed. Preferred substitution positions (positions 22 and 422 of SEQ ID NO: 2 and positions 22 and 426 of SEQ ID NO: 14) are further boxed. The default parameters used are indicated. The percent identity ("Identity"), percent similarity ("Similarity"), and similarity score ("Score") obtained are indicated.

[0042] Figure 4 . Using clustal omega (https: / / www.ebi.ac.uk / Tools / msa) / clustalo / ) and espript (http: / / espript.ibcp.fr / ESPript / ESPript / esp_userguide.php), a multiple sequence alignment of the amino acid sequences of the glycoprotein G extracellular domain of the following VSV strains was generated: Indiana (SEQ ID NO:2), Maraba (SEQ ID NO:4), Cocal (SEQ ID NO:6), Morreton (SEQ ID NO:8), Alagoa (SEQ ID NO:10), New Jersey (SEQ ID NO:12), and Carajas (SEQ ID NO:14). Strictly conserved amino acids (same for all strains) are written in white on a gray background. The boxed areas correspond to highly similar residues. The consensus sequence shown below was generated using the criteria from MultAlin (similarity score>0.7): uppercase is identical, lowercase is an identity level>0.5,! is any one of IV, $ is any one of LM, % is any one of FY, and # is any one of NDQEBZ.

[0043] Figure 5 The histidine cluster in the VSV Indiana G fusion preprotomer. Mutation of histidine 407 to alanine abolishes the G fusion property.

[0044] Figure 6Upper panel: Flow cytometric analysis of WT and mutant glycoprotein expression and binding of fluorescent GST-CR2 (CR2 fused to GST at the amino terminus) on HEK293T cells. 24 hours after transfection, cell surface expression of WT and mutant G was assessed directly on living cells using the monoclonal anti-G antibody 8G5F11 at 4°C for 1 hour. Cells were then incubated with anti-mouse AlexaFluor 488 and the indicated GST-CR2. ATTO550 Incubate simultaneously. Cells transfected with the G construct, which is still able to bind to the GST-CR protein, exhibit red fluorescence due to the ATTO550 dye. Mutant R354A is a mutant that is unable to bind to the CR domain.

[0045] Bottom: Flow cytometric analysis of surface expression of mutant glycoproteins G-H407A and G.H407A / S422I. Surface G protein expression was detected using monoclonal antibody 8G5F11 (KeraFAST) and a goat anti-mouse IgG secondary antibody conjugated to Alexa Fluor 488. A total of 10,000 cells were counted by flow cytometry. In each box, the black curve corresponds to the fluorescence of untransfected cells, the blue curve corresponds to the fluorescence of cells transfected with a pCAGGS plasmid encoding WT G, and the red curve corresponds to the fluorescence of cells transfected with a pCAGGS plasmid encoding the indicated mutants. In each box, surface expression of mutant G is expressed as a percentage of WT G surface expression.

[0046] Figure 7 Cell-cell fusion assay. Fusion activity of optimized VSV G Indiana WT and VSV GNano (i.e., H22 residue mutated to N, S422 residue mutated to I, F, M, L, or V).

[0047] Figure 8 Crystal structure of VSV G1-440 (residues 1 to 440 of VSV G Indiana WT) and the environment of residue S422.

[0048] (A) Crystal structure of the G1-440 trimer before fusion. The chain is traced to residue 432. Residues 410 to 432 are dark gray.

[0049] (B) Structure of the 410-432 segment. Two close-ups detail the organization of the 410-432 segment and its interaction with the fusion domain.

[0050] (C) Close-up view of the S422 residue in the G prefusion state. DETAILED DESCRIPTION

[0051] In the context of the present invention, the inventors unexpectedly found that although the recombinant VSV virus containing a nanobody inserted between the signal peptide and the VSV Indiana glycoprotein G extracellular domain retained its fusion properties and infectivity, it was difficult to amplify and could not allow its industrial use. The inventors further unexpectedly found that inserting at least one substitution at position 22 or position 422 of the VSV Indiana glycoprotein G extracellular domain allowed a significant increase in the amplification of the recombinant virus while retaining fusion properties and infectivity, thereby allowing its industrial use (see Example 1). The results obtained by the inventors also show that the presence of a hydrophobic residue at position 422 is key to regulating the pH-dependent structural transition and promotes G folding and stabilizing the pre-fusion form of the G fusion polypeptide having a nanobody inserted into the N-terminus of the extracellular domain (see Examples 2, 3 and 4).

[0052] Mutant polypeptides with improved yield

[0053] The present invention therefore first relates to a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence of the glycoprotein G extracellular domain of a vesicular stomatitis virus (VSV) strain, wherein the extracellular domain comprises, consists essentially of, or consists of the amino acid sequence set forth in SEQ ID NO: 2, or an amino acid sequence having at least 50% identity to the amino acid sequence set forth in SEQ ID NO: 2, said sequence having at least one substitution of an amino acid residue selected from the group consisting of:

[0054] a) any of the amino acid residues at positions 421 to 429 and any of the amino acid residues at positions 17 to 25 of SEQ ID NO: 2, preferably any of the amino acid residues at positions 421 to 425 and any of the amino acid residues at positions 17 to 25 of SEQ ID NO: 2, more preferably any of the amino acid residues at positions 422 and 22 of SEQ ID NO: 2; or

[0055] b) any amino acid residue at a position equivalent to position 421 to a position equivalent to position 429 of SEQ ID NO: 2 and any amino acid residue at a position equivalent to position 17 to a position equivalent to position 25 of SEQ ID NO: 2 after optimal global alignment with SEQ ID NO: 2, preferably any amino acid residue at a position equivalent to position 421 to a position equivalent to position 425 of SEQ ID NO: 2 and any amino acid residue at a position equivalent to position 17 to a position equivalent to position 25 of SEQ ID NO: 2 after optimal global alignment with SEQ ID NO: 2, more preferably any amino acid residue at a position equivalent to position 422 and position 22 of SEQ ID NO: 2 after optimal global alignment with SEQ ID NO: 2.

[0056] In a preferred embodiment, the mutant polypeptide of the present invention is an isolated and / or non-naturally occurring polypeptide.

[0057] Reference sequence and position of substitution

[0058] The mutant polypeptide is based on the amino acid sequence of the glycoprotein G extracellular domain of a vesicular stomatitis virus (VSV) strain, which corresponds to the amino acid sequence of glycoprotein G without the signal peptide. In this specification, the reference VSV strain is the Indiana strain. The amino acid sequence of glycoprotein G of the VSV Indiana strain is set forth in SEQ ID NO: 1. The amino acid sequence of the glycoprotein G extracellular domain of the VSV Indiana strain is set forth in SEQ ID NO: 2 and corresponds to amino acids 17-511 of SEQ ID NO: 1, and amino acids 1-16 of SEQ ID NO: 1 correspond to the signal peptide. In a preferred embodiment, the mutant polypeptide according to the present invention is derived from the extracellular domain of glycoprotein G of VSV Indiana strain, and thus comprises the amino acid sequence set forth in SEQ ID NO: 2, or consists essentially of this sequence, or consists of this sequence, said sequence having at least one substitution of an amino acid residue selected from the group consisting of: any amino acid residue at positions 421 to 429 and any amino acid residue at positions 17 to 25 of SEQ ID NO: 2, preferably any amino acid residue at positions 421 to 425 and any amino acid residue at positions 17 to 25 of SEQ ID NO: 2, more preferably any amino acid residue at positions 422 and 22 of SEQ ID NO: 2.

[0059] However, the mutant polypeptide according to the present invention may also be derived from the glycoprotein G extracellular domain of a VSV strain other than Indiana, or may comprise further mutations, provided that it comprises, consists essentially of, or consists of an amino acid sequence having the following identity to the amino acid sequence set forth in SEQ ID NO: 2: at least 50% identity, preferably at least 55% identity, at least 60% identity, at least 65% identity, more preferably at least 70% identity, at least 75% identity, at least 78% identity, at least 79% identity, at least 80% identity, at least 81% identity, at least 82% identity, at least 83% identity, at least 84% identity, at least 85% identity, at least 86% identity, at least 87% identity, at least 88% identity, at least 89% identity, at least 90% identity, at least 91% identity, at least 92% identity, at least 93% identity, at least 94% identity, at least 95% identity, at least 96% identity, at least 97% identity, at least 98% identity, at least 99% identity, at least 100% identity, at least 101% identity, at least 102% identity, at least 103% identity, at least 104% identity, at least 105% identity, at least 106% identity, at least 107% identity at least 85% identity, at least 86% identity, at least 87% identity, at least 88% identity, at least 89% identity, at least 90% identity, at least 91% identity, at least 92% identity, at least 93% identity, at least 94% identity, at least 95% identity, at least 96% identity, at least 97% identity, at least 98% identity, or even at least 99% identity, said sequence having at least one substitution of an amino acid residue selected from the group consisting of: ID NO: 2, any amino acid residue at a position equivalent to position 421 to a position equivalent to position 429 of SEQ ID NO: 2 and any amino acid residue at a position equivalent to position 17 to a position equivalent to position 25 of SEQ ID NO: 2 after the best global alignment with SEQ ID NO: 2, preferably any amino acid residue at a position equivalent to position 421 to a position equivalent to position 425 of SEQ ID NO: 2 and any amino acid residue at a position equivalent to position 17 to a position equivalent to position 25 of SEQ ID NO: 2 after the best global alignment with SEQ ID NO: 2, more preferably any amino acid residue at a position equivalent to position 422 and position 22 of SEQ ID NO: 2 after the best global alignment with SEQ ID NO: 2.

[0060] In this case, SEQ ID NO: 2 and an initial amino acid sequence (e.g., an amino acid sequence of the glycoprotein G extracellular domain of a VSV strain other than Indiana, provided that the sequence, after optimal global alignment, has at least 50% identity with SEQ ID NO: 2 or any other preferred minimum identity percentage defined above) are optimally globally aligned, and the initial amino acid sequence has at least one substitution of an amino acid residue selected from the group consisting of: after optimal global alignment with SEQ ID NO: 2, any amino acid residue at a position corresponding to position 421 to a position corresponding to position 429 of SEQ ID NO: 2 and any amino acid residue at a position corresponding to position 17 to a position corresponding to position 25 of SEQ ID NO: 2, preferably after optimal global alignment with SEQ ID NO: 2, any amino acid residue at a position corresponding to position 421 to a position corresponding to position 425 of SEQ ID NO: 2 and any amino acid residue at a position corresponding to position 17 to a position corresponding to position 25 of SEQ ID NO: 2, more preferably after optimal global alignment with SEQ ID NO: 2, any amino acid residue at a position corresponding to position 421 to a position corresponding to position 425 of SEQ ID NO: 2, Any amino acid residue at positions 422 and 22 of NO:2.

[0061] The percentage identity mentioned in the context of the present disclosure is determined based on the best global alignment of the sequences to be compared, i.e., using any algorithm well known to those skilled in the art (such as the algorithm of Needleman and Wunsch (1970)), based on the best alignment of the sequences obtained completely over their entire length. The sequence comparison can be performed using any software well known to those skilled in the art, such as Emboss Needle software. For example, Emboss Needle software can be obtained from https: / / www.ebi.ac.uk / Tools / psa / emboss_needle / . The software reads two input sequences and writes their best global sequence alignment to a file. It uses the Needleman-Wunsch alignment algorithm to find the best alignment of the two sequences along their entire length (including gaps). The algorithm uses a dynamic programming approach to ensure the best alignment by exploring all possible alignments and selecting the best one. A scoring matrix containing each possible residue or nucleotide matching value is read. Needle finds the alignment with the maximum possible score, where the score of the alignment is equal to the sum of the matches obtained from the scoring matrix, minus the penalties for opening and extending gaps in the aligned sequences. The substitution matrix and the penalties for opening and extending gaps are user-specified. In the context of the present invention, to obtain the best global alignment, the Emboss Needle software and default parameters can be used, i.e., using the "Gap open" parameter equal to 10.0, the "Gap extend" parameter equal to 0.5, the "End gap penalty" parameter as "false," the "End gap open" parameter as 10.0, and the "Blosum 62" matrix. When two amino acid sequences are input, the Emboss Needle software returns the best global alignment, as well as several values ​​that characterize the alignment:

[0062] "Identity" is the percentage of identity, i.e., the percentage of identical matches between the two sequences over the reported aligned region (including any gaps in that length),

[0063] "Similarity" is the percentage of similarity between the two sequences over the reported aligned region (including any gaps in that length), and

[0064] • "Score" is the overall score for the alignment, corresponding to the best score obtained by the software for all tested global alignments (ie, over the entire length of the two sequences).

[0065] This score can be referred to as a "similarity score" because the higher the score value between SEQ ID NO: 2 and another initial sequence, the higher the similarity between the initial sequence and SEQ ID NO: 2, taking into account not only the aligned identical amino acids, but also conservative substitutions that are not expected to significantly change the function of the protein.

[0066] When an optimal global alignment is obtained between SEQ ID NO: 2 and another initial sequence, the percent identity and the position corresponding to a specific position of SEQ ID NO: 2 are defined. In particular, the position corresponding to position N of SEQ ID NO: 2 is the position of the other initial sequence aligned with position N of SEQ ID NO: 2.

[0067] Examples of VSV strains other than Indiana include seven serotypes, such as Maraba, Cocal, Morreton, Alagoa, New Jersey, and Carajas strains. The full-length glycoprotein G and non-mutated (wild-type) amino acid sequences of the glycoprotein G extracellular domain of these strains and the Indiana strain are shown in Table 1 below:

[0068] Table 1. Full-length glycoprotein G and non-mutated (wild-type) amino acid sequences of the glycoprotein G ectodomain of Indiana, Maraba, Cocal, Morreton, Alagoa, New Jersey, and Carajas VSV strains. In the full-length amino acid sequences, the signal peptide is underlined. The position of the signal peptide in the full-length amino acid sequence is further indicated.

[0069]

[0070]

[0071]

[0072]

[0073] The best global alignment of the non-mutated amino acid sequences of the glycoprotein G extracellular domain of VSV Indiana strain relative to Maraba, Cocal, Morreton, Alagoa, New Jersey, and Carajas strains is shown in Figures 3A to 3FBased on these optimal global alignments, the percent identities and similarity scores (obtained using Emboss Needle software and the default parameters defined above) were determined, as well as the positions in the amino acid sequences of the glycoprotein G ectodomain of VSV Maraba, Cocal, Morreton, Alagoa, New Jersey, and Carajas strains corresponding to positions 17-25 and 421-429 of SEQ ID NO: 2 (VSV Indiana glycoprotein G ectodomain). These are listed in Table 2 below:

[0074] Table 2. Positions in the amino acid sequence of the glycoprotein G ectodomain of VSV Maraba, Cocal, Morreton, Alagoa, New Jersey, and Carajas strains corresponding to positions 17-25 and 421-429 of SEQ ID NO: 2 (VSV Indiana glycoprotein G ectodomain), percent identity with SEQ ID NO: 2 after optimal global alignment, and similarity scores (calculated by Emboss Needle using default parameters: Gap Open = 10.0, Gap Extension = 0.5, End Gap Penalty = False, End Gap Open = 10.0, Blosum 62 matrix).

[0075]

[0076]

[0077] Figures 3A to 3F The alignment also shows that, in addition to the identical amino acids between the two amino acid sequences, some substitutions are conservative, which ensure the function of the extracellular domain. After optimal global alignment, in particular when calculating the similarity score of the two sequences using Emboss Needle software and default parameters, the presence of such conservative substitutions is taken into account. Thus, when using an initial sequence different from SEQ ID NO: 2, in addition to having at least 50% identity with SEQ ID NO: 2 (or any other minimum identity percentage defined above), after optimal global alignment (preferably using Emboss Needle software and default parameters as defined above), the initial sequence preferably has the following similarity score: at least 1400, more preferably at least 1500, at least 1600, at least 1700, at least 1800, even more preferably at least 1900, at least 2000, at least 2100, at least 2200, or even at least 2300, given that SEQ ID NO: 2 has a similarity score of 2693 to itself.

[0078] Multiple amino acid sequence alignments of the glycoprotein G extracellular domain of VSV Indiana, Maraba, Cocal, Morreton, Alagoa, New Jersey, and Carajas strains are shown in Figure 4 .like Figure 4 As shown, all amino acid sequences of the glycoprotein G extracellular domain of VSV, regardless of the specific strain, contain conserved amino acids and structural domains (ie, amino acids or structural domains that are identical between SEQ ID NO: 2 and another aligned amino acid sequence).

[0079] In particular, positions 17-25 of SEQ ID NO: 2 contain conserved amino acids at positions 17-18, 21, and 23-25. The consensus sequence of amino acid sequences at positions 17-25 of the glycoprotein G extracellular domain of VSV Indiana, Maraba, Cocal, Morreton, Alagoa, New Jersey, and Carajas strains can be defined as VPX1X2YX3YCP (SEQ ID NO: 15), wherein:

[0080] X1 is selected from the group consisting of serine (S), histidine (H), lysine (K), proline (P) and alanine (A),

[0081] X2 is selected from the group consisting of asparagine (N), glutamic acid (E), threonine (T), glycine (G) and serine (S), and

[0082] • X3 is selected from the group consisting of histidine (H), asparagine (N), arginine (R) and glutamine (Q).

[0083] Similarly, positions 421-429 of SEQ ID NO: 2 contain conserved amino acids at positions 421 and 426-429. The consensus sequence of amino acid sequences at positions 421-429 of the glycoprotein G extracellular domain of VSV Indiana, Maraba, Cocal, Morreton, Alagoa, New Jersey, and Carajas strains can be defined as EX4X5X6X7GDTG (SEQ ID NO: 16), wherein:

[0084] X4 is selected from serine (S), valine (V) and threonine (T),

[0085] X5 is selected from leucine (L) and isoleucine (I),

[0086] X6 is selected from phenylalanine (F) and tyrosine (Y), and

[0087] X7 is selected from phenylalanine (F) and tyrosine (Y).

[0088] Therefore, in a preferred embodiment, the mutant polypeptide according to the present invention comprises, consists essentially of, or consists of the following sequence:

[0089] a) the amino acid sequence set forth in SEQ ID NO: 2, or a sequence having at least 50% identity to the amino acid sequence set forth in SEQ ID NO: 2 after optimal global alignment with SEQ ID NO: 2, and

[0090] b) two domains with sequences VPX1X2YX3YCP (SEQ ID NO: 15) and EX4X5X6X7GDTG (SEQ ID NO: 16),

[0091] in:

[0092] i) one of X4 to X7 (corresponding to positions 422-425 of SEQ ID NO: 2), preferably X4 (corresponding to position 422 of SEQ ID NO: 2);

[0093] ii) one of X1 to X3 (corresponding to positions 19-20 and 22 of SEQ ID NO: 2), preferably X3 (corresponding to position 22 of SEQ ID NO: 2); or

[0094] iii) one of X1 to X3 (corresponding to positions 19-20 and 22 of SEQ ID NO: 2) and one of X4 to X7 (corresponding to positions 422-425 of SEQ ID NO: 2), preferably X3 and X4 (corresponding to positions 22 and 422 of SEQ ID NO: 2),

[0095] was replaced.

[0096] In addition, the conserved amino acids in all amino acid sequences of the glycoprotein G extracellular domain of VSV Indiana, Maraba, Cocal, Morreton, Alagoa, New Jersey and Carajas strains correspond to amino acids 1, 4, 6-7, 12, 14, 17-18, 21, 23-25, 27, 29, 31, 33, 46-4755-56, 58-60, 64, 66-69, 71-75, 77, 79, 81-82, 87, 91-92, 96, 102, 107-111, 114-116, 119, 121, 1 27, 130, 132, 134, 137-139, 141, 143, 145, 151, 153, 158, 160, 162-165, 167, 177, 199, 204, 206-208, 210, 212, 219, 221, 224, 228, 231, 236-237, 241, 253, 259, 2 62, 268, 271-272, 274-277, 279-281, 283-285, 287-290, 299, 301, 304, 307-311, 313-314, 316-318, 320-321, 323, 325-326, 330, 332, 338, 345, 349, 354, 356-3 57, 360, 362, 368-372, 374, 376, 379, 381, 383-384, 388, 390, 393, 395, 407-408, 413, 421, 426-429, 431-434, 436, 439-443, 445, 447, 456, 467, 487 and 489-490. Hereinafter, these positions are referred to as "conserved positions".

[0097] Therefore, in some embodiments of the mutant polypeptides according to the present invention, the amino acid sequence having at least 50% identity with the amino acid sequence set forth in SEQ ID NO: 2, after optimal global alignment with SEQ ID NO: 2, has the same amino acids as SEQ ID NO: 2 at the conserved positions defined above.

[0098] When it is desired to alter the ability of the extracellular domain to bind to the low-density lipoprotein receptor (LDL-R), conserved positions 47 and 354 may be exceptions (see the section below entitled "Further Optional Mutations"). In this case, an amino acid sequence having at least 50% identity (or any other minimum % identity disclosed above) to the amino acid sequence set forth in SEQ ID NO: 2, after optimal global alignment with SEQ ID NO: 2, has the same amino acids as SEQ ID NO: 2 at the conserved positions defined above, except for possible additional substitutions at positions 47 and / or 354 of SEQ ID NO: 2.

[0099] Substituted amino acid type

[0100] Although the substituted amino acids in the mutant polypeptides according to the present invention can be selected from any amino acids different from the original amino acids, certain specific types of amino acids are preferred depending on the position of the substitution.

[0101] In particular, when the mutant polypeptide according to the present invention comprises a substitution in any of the amino acid residues located at positions 421 to 429 of SEQ ID NO: 2 or at equivalent positions after optimal global alignment with SEQ ID NO: 2, the original amino acid is preferably substituted by a hydrophobic amino acid, preferably selected from the group consisting of glycine (G), alanine (A), valine (V), leucine (L), isoleucine (I), methionine (M), proline (P), phenylalanine (F) and tryptophan (W), more preferably isoleucine (I), leucine (L), methionine (M), valine (V) and phenylalanine (F), even more preferably isoleucine (I). In fact, the present inventors have shown that the presence of a hydrophobic amino acid in any of the amino acid residues located at positions 421 to 429 of SEQ ID NO: 2 or at equivalent positions after optimal global alignment with SEQ ID NO: 2 leads to a stabilization of the prefusion conformation of glycoprotein G.

[0102] When the mutant polypeptide according to the present invention comprises a substitution in any of the amino acid residues located at positions 17 to 25 of SEQ ID NO: 2, or at equivalent positions after optimal global alignment with SEQ ID NO: 2, the original amino acid is preferably substituted with a polar amino acid, preferably selected from the group consisting of asparagine (N), glutamine (Q), cysteine ​​(C), tyrosine (Y), threonine (T) and serine (S), more preferably asparagine (N). In fact, it is believed that the presence of a polar amino acid in any of the amino acid residues located at positions 17 to 25 of SEQ ID NO: 2, or at equivalent positions after optimal global alignment with SEQ ID NO: 2, leads to a stabilization of the prefusion conformation of glycoprotein G.

[0103] When the mutant polypeptide according to the present invention comprises a substitution in any of the amino acid residues located at positions 17 to 25 of SEQ ID NO: 2 or at equivalent positions after optimal global alignment with SEQ ID NO: 2, and comprises a substitution in any of the amino acid residues located at positions 421 to 429 of SEQ ID NO: 2 or at equivalent positions after optimal global alignment with SEQ ID NO: 2,

[0104] a) the original amino acids at positions 17 to 25 of SEQ ID NO: 2 or at equivalent positions after optimal global alignment with SEQ ID NO: 2 are preferably substituted with polar amino acids, preferably selected from the group consisting of asparagine (N), glutamine (Q), cysteine ​​(C), tyrosine (Y), threonine (T) and serine (S), more preferably asparagine (N); and

[0105] b) the original amino acids at positions 421 to 429 of SEQ ID NO: 2 or at equivalent positions after optimal global alignment with SEQ ID NO: 2 are preferably substituted with a hydrophobic amino acid, preferably selected from the group consisting of glycine (G), alanine (A), valine (V), leucine (L), isoleucine (I), methionine (M), proline (P), phenylalanine (F) and tryptophan (W), more preferably isoleucine (I), leucine (L), methionine (M), valine (V) and phenylalanine (F), even more preferably isoleucine (I) ( Figure 7 ).

[0106] Preferred mutant polypeptides

[0107] Some preferred mutant polypeptides according to the present invention are based on the amino acid sequence of the glycoprotein G extracellular domain of VSV Indiana strain and can be selected from:

[0108] a) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 17, which corresponds to SEQ ID NO: 2 in which the histidine (H) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue;

[0109] b) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 18, which corresponds to SEQ ID NO: 2 in which the serine (S) amino acid residue at position 422 is substituted with an isoleucine (I) amino acid residue;

[0110] c) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 19, which corresponds to SEQ ID NO: 2 in which the serine (S) amino acid residue at position 422 is substituted with a leucine (L) amino acid residue;

[0111] d) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 20, which corresponds to SEQ ID NO: 2 in which the serine (S) amino acid residue at position 422 is substituted with a phenylalanine (F) amino acid residue;

[0112] e) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 21, which corresponds to SEQ ID NO: 2 in which the serine (S) amino acid residue at position 422 is substituted with a methionine (M) amino acid residue;

[0113] f) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 22, which corresponds to SEQ ID NO: 2 in which the serine (S) amino acid residue at position 422 is substituted with a valine (V) amino acid residue;

[0114] g) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO:23, which corresponds to SEQ ID NO:2 in which the histidine (H) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the serine (S) amino acid residue at position 422 is substituted with an isoleucine (I) amino acid residue;

[0115] h) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 24, which corresponds to SEQ ID NO: 2 in which the histidine (H) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the serine (S) amino acid residue at position 422 is substituted with a leucine (L) amino acid residue;

[0116] i) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 25, which corresponds to SEQ ID NO: 2 in which the histidine (H) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the serine (S) amino acid residue at position 422 is substituted with a phenylalanine (F) amino acid residue;

[0117] j) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 26, which corresponds to SEQ ID NO: 2 in which the histidine (H) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the serine (S) amino acid residue at position 422 is substituted with a methionine (M) amino acid residue;

[0118] k) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 27, which corresponds to SEQ ID NO: 2 in which the histidine (H) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the serine (S) amino acid residue at position 422 is substituted with a valine (V) amino acid residue; and

[0119] l) A mutant polypeptide comprising, or consisting essentially of, or consisting of an amino acid sequence as defined in any one of a) to k) above, and further comprising a signal peptide at the N-terminus, preferably the signal peptide corresponding to positions 1-16 of SEQ ID NO: 1.

[0120] The most preferred mutant polypeptides based on the amino acid sequence of the glycoprotein G extracellular domain of VSV Indiana strain are those comprising at least one substitution at position 422 (SEQ ID NOs: 18 to 27, or a mutant polypeptide comprising one of these amino acid sequences and further comprising a signal peptide at the N-terminus, preferably the signal peptide corresponding to positions 1-16 of SEQ ID NO: 1).

[0121] The amino acid sequences of preferred mutant polypeptides derived from the VSV Indiana glycoprotein G extracellular domain, SEQ ID NOs: 17 to 27, are shown in Table 3 below.

[0122] Table 3. Amino acid sequences based on the VSV Indiana strain glycoprotein G extracellular domain (SEQ ID NO: 2) SEQ ID NO: 17 to 27, and related substitutions compared to SEQ ID NO: 2. For each substitution, the starting amino acid in SEQ ID NO: 2 is indicated by a single-letter code, followed by its position in SEQ ID NO: 2 and the substituted amino acid indicated by a single-letter code.

[0123]

[0124]

[0125]

[0126]

[0127] Other preferred mutant polypeptides according to the present invention are based on the amino acid sequence of the glycoprotein G extracellular domain of the VSV Maraba strain and can be selected from:

[0128] a) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 28, which corresponds to SEQ ID NO: 4 in which the histidine (H) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue;

[0129] b) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 29, which corresponds to SEQ ID NO: 4 in which the threonine (T) amino acid residue at position 422 is substituted with an isoleucine (I) amino acid residue;

[0130] c) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO:30, which corresponds to SEQ ID NO:4 in which the threonine (T) amino acid residue at position 422 is substituted with a leucine (L) amino acid residue;

[0131] d) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO:31, which corresponds to SEQ ID NO:4 in which the threonine (T) amino acid residue at position 422 is substituted with a phenylalanine (F) amino acid residue;

[0132] e) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 32, which corresponds to SEQ ID NO: 4 in which the threonine (T) amino acid residue at position 422 is substituted with a methionine (M) amino acid residue;

[0133] f) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 33, which corresponds to SEQ ID NO: 4 in which the threonine (T) amino acid residue at position 422 is substituted with a valine (V) amino acid residue;

[0134] g) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO:34, which corresponds to SEQ ID NO:4 in which the histidine (H) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with an isoleucine (I) amino acid residue;

[0135] h) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 35, which corresponds to SEQ ID NO: 4 in which the histidine (H) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with a leucine (L) amino acid residue;

[0136] i) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 36, which corresponds to SEQ ID NO: 4 in which the histidine (H) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with a phenylalanine (F) amino acid residue;

[0137] j) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 37, which corresponds to SEQ ID NO: 4 in which the histidine (H) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with a methionine (M) amino acid residue;

[0138] k) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO:38, which corresponds to SEQ ID NO:4 in which the histidine (H) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with a valine (V) amino acid residue; and

[0139] l) A mutant polypeptide comprising, or essentially consisting of, or consisting of an amino acid sequence as defined in any one of a) to k) above, and further comprising a signal peptide at the N-terminus, preferably the signal peptide corresponds to positions 1-16 of SEQ ID NO: 3.

[0140] The most preferred mutant polypeptides based on the amino acid sequence of the extracellular domain of glycoprotein G of VSV Maraba strain are those comprising at least one substitution at position 422 (SEQ ID NOs: 29 to 38, or a mutant polypeptide comprising one of these amino acid sequences and further comprising a signal peptide at the N-terminus, preferably the signal peptide corresponding to positions 1 to 16 of SEQ ID NO: 3).

[0141] The amino acid sequences of preferred mutant polypeptides derived from the VSV Maraba glycoprotein G extracellular domain, SEQ ID NOs: 28 to 38, are shown in Table 4 below.

[0142] Table 4. Amino acid sequences based on the VSV Maraba strain glycoprotein G extracellular domain (SEQ ID NO: 4) SEQ ID NO: 28 to 38, and related substitutions compared to SEQ ID NO: 4. For each substitution, the starting amino acid in SEQ ID NO: 4 is indicated by a single-letter code, followed by its position in SEQ ID NO: 4 and the substituted amino acid indicated by a single-letter code.

[0143]

[0144]

[0145]

[0146]

[0147] Other preferred mutant polypeptides according to the present invention are based on the amino acid sequence of the extracellular domain of glycoprotein G of VSV Cocal strain and can be selected from:

[0148] a) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 39, which corresponds to SEQ ID NO: 6 in which the histidine (H) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue;

[0149] b) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO:40, which corresponds to SEQ ID NO:6 in which the threonine (T) amino acid residue at position 422 is substituted with an isoleucine (I) amino acid residue;

[0150] c) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO:41, which corresponds to SEQ ID NO:6 in which the threonine (T) amino acid residue at position 422 is substituted with a leucine (L) amino acid residue;

[0151] d) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO:42, which corresponds to SEQ ID NO:6 in which the threonine (T) amino acid residue at position 422 is substituted with a phenylalanine (F) amino acid residue;

[0152] e) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 43, which corresponds to SEQ ID NO: 6 in which the threonine (T) amino acid residue at position 422 is substituted with a methionine (M) amino acid residue;

[0153] f) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 44, which corresponds to SEQ ID NO: 6 in which the threonine (T) amino acid residue at position 422 is substituted with a valine (V) amino acid residue;

[0154] g) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO:45, which corresponds to SEQ ID NO:6 in which the histidine (H) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with an isoleucine (I) amino acid residue;

[0155] h) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 46, which corresponds to SEQ ID NO: 6 in which the histidine (H) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with a leucine (L) amino acid residue;

[0156] i) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 47, which corresponds to SEQ ID NO: 6 in which the histidine (H) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with a phenylalanine (F) amino acid residue;

[0157] j) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 48, which corresponds to SEQ ID NO: 6 in which the histidine (H) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with a methionine (M) amino acid residue;

[0158] k) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO:49, which corresponds to SEQ ID NO:6 in which the histidine (H) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with a valine (V) amino acid residue; and

[0159] l) A mutant polypeptide comprising, or essentially consisting of, or consisting of an amino acid sequence as defined in any one of a) to k) above, and further comprising a signal peptide at the N-terminus, preferably the signal peptide corresponds to positions 1-17 of SEQ ID NO: 5.

[0160] The most preferred mutant polypeptides based on the amino acid sequence of the extracellular domain of glycoprotein G of VSV Cocal strain are those comprising at least one substitution at position 422 (SEQ ID NOs: 40 to 49, or a mutant polypeptide comprising one of these amino acid sequences and further comprising a signal peptide at the N-terminus, preferably the signal peptide corresponding to positions 1-17 of SEQ ID NO: 5).

[0161] The amino acid sequences of preferred mutant polypeptides derived from the VSV Cocal glycoprotein G extracellular domain, SEQ ID NOs: 39 to 49, are shown in Table 5 below.

[0162] Table 5. Amino acid sequences of SEQ ID NOs: 39 to 49 based on the glycoprotein G extracellular domain of VSV Cocal strain (SEQ ID NO: 6), and relevant substitutions compared to SEQ ID NO: 6. For each substitution, the starting amino acid in SEQ ID NO: 6 is indicated by a single-letter code, followed by its position in SEQ ID NO: 6 and the substituted amino acid indicated by a single-letter code.

[0163]

[0164]

[0165]

[0166]

[0167] Other preferred mutant polypeptides according to the present invention are based on the amino acid sequence of the glycoprotein G extracellular domain of VSV Morreton strain and can be selected from:

[0168] a) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 50, which corresponds to SEQ ID NO: 8 in which the glutamine (Q) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue;

[0169] b) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 51, which corresponds to SEQ ID NO: 8 in which the threonine (T) amino acid residue at position 422 is substituted with an isoleucine (I) amino acid residue;

[0170] c) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 52, which corresponds to SEQ ID NO: 8 in which the threonine (T) amino acid residue at position 422 is substituted with a leucine (L) amino acid residue;

[0171] d) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 53, which corresponds to SEQ ID NO: 8 in which the threonine (T) amino acid residue at position 422 is substituted with a phenylalanine (F) amino acid residue;

[0172] e) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 54, which corresponds to SEQ ID NO: 8 in which the threonine (T) amino acid residue at position 422 is substituted with a methionine (M) amino acid residue;

[0173] f) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 55, which corresponds to SEQ ID NO: 8 in which the threonine (T) amino acid residue at position 422 is substituted with a valine (V) amino acid residue;

[0174] g) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 56, which corresponds to SEQ ID NO: 8 in which the glutamine (Q) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with an isoleucine (I) amino acid residue;

[0175] h) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 57, which corresponds to SEQ ID NO: 8 in which the glutamine (Q) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with a leucine (L) amino acid residue;

[0176] i) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 58, which corresponds to SEQ ID NO: 8 in which the glutamine (Q) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with a phenylalanine (F) amino acid residue;

[0177] j) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 59, which corresponds to SEQ ID NO: 8 in which the glutamine (Q) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with a methionine (M) amino acid residue;

[0178] k) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO:60, which corresponds to SEQ ID NO:8 in which the glutamine (Q) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with a valine (V) amino acid residue; and

[0179] l) A mutant polypeptide comprising, or essentially consisting of, or consisting of an amino acid sequence as defined in any one of a) to k) above, and further comprising a signal peptide at the N-terminus, preferably the signal peptide corresponds to positions 1-17 of SEQ ID NO: 7.

[0180] The most preferred mutant polypeptides based on the amino acid sequence of the glycoprotein G extracellular domain of VSV Morreton strain are those comprising at least one substitution at position 422 (SEQ ID NOs: 51 to 60, or a mutant polypeptide comprising one of these amino acid sequences and further comprising a signal peptide at the N-terminus, preferably the signal peptide corresponding to positions 1-17 of SEQ ID NO: 7).

[0181] The amino acid sequences of preferred mutant polypeptides derived from the VSV Morreton glycoprotein G extracellular domain, SEQ ID NOs: 50 to 60, are shown in Table 6 below.

[0182] Table 6. Amino acid sequences of SEQ ID NOs: 50 to 60 based on the extracellular domain of glycoprotein G of VSV Morreton strain (SEQ ID NO: 8), and relevant substitutions compared to SEQ ID NO: 8. For each substitution, the starting amino acid in SEQ ID NO: 8 is indicated by a single letter code, followed by its position in SEQ ID NO: 8 and the substituted amino acid indicated by a single letter code.

[0183]

[0184]

[0185]

[0186] Other preferred mutant polypeptides according to the present invention are based on the amino acid sequence of the glycoprotein G extracellular domain of the VSV Alagoa strain and can be selected from:

[0187] a) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 61, which corresponds to SEQ ID NO: 10 in which the arginine (R) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue;

[0188] b) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 62, which corresponds to SEQ ID NO: 10 in which the threonine (T) amino acid residue at position 422 is substituted with an isoleucine (I) amino acid residue;

[0189] c) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 63, which corresponds to SEQ ID NO: 10 in which the threonine (T) amino acid residue at position 422 is substituted with a leucine (L) amino acid residue;

[0190] d) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 64, which corresponds to SEQ ID NO: 10 in which the threonine (T) amino acid residue at position 422 is substituted with a phenylalanine (F) amino acid residue;

[0191] e) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 65, which corresponds to SEQ ID NO: 10 in which the threonine (T) amino acid residue at position 422 is substituted with a methionine (M) amino acid residue;

[0192] f) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 66, which corresponds to SEQ ID NO: 10 in which the threonine (T) amino acid residue at position 422 is substituted with a valine (V) amino acid residue;

[0193] g) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 67, which corresponds to SEQ ID NO: 10 in which the arginine (R) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with an isoleucine (I) amino acid residue;

[0194] h) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 68, which corresponds to SEQ ID NO: 10 in which the arginine (R) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with a leucine (L) amino acid residue;

[0195] i) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 69, which corresponds to SEQ ID NO: 10 in which the arginine (R) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with a phenylalanine (F) amino acid residue;

[0196] j) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 70, which corresponds to SEQ ID NO: 10 in which the arginine (R) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with a methionine (M) amino acid residue; and

[0197] k) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO:71, which corresponds to SEQ ID NO:10 in which the arginine (R) amino acid residue at position 22 is substituted with an asparagine (N) amino acid residue and the threonine (T) amino acid residue at position 422 is substituted with a valine (V) amino acid residue; and

[0198] l) A mutant polypeptide comprising, or essentially consisting of, or consisting of an amino acid sequence as defined in any one of a) to k) above, and further comprising a signal peptide at the N-terminus, preferably the signal peptide corresponds to positions 1-17 of SEQ ID NO: 9.

[0199] The most preferred mutant polypeptides based on the amino acid sequence of the glycoprotein G extracellular domain of VSV Alagoa strain are those comprising at least one substitution at position 422 (SEQ ID NOs: 62 to 71, or a mutant polypeptide comprising one of these amino acid sequences and further comprising a signal peptide at the N-terminus, preferably the signal peptide corresponding to positions 1 to 17 of SEQ ID NO: 9).

[0200] The amino acid sequences of preferred mutant polypeptides derived from the extracellular domain of VSV Alagoa glycoprotein G, SEQ ID NOs: 61 to 71, are shown in Table 7 below.

[0201] Table 7. Amino acid sequences of SEQ ID NOs: 61 to 71 based on the glycoprotein G extracellular domain of VSV Alagoa strain (SEQ ID NO: 10), and relevant substitutions compared to SEQ ID NO: 10. For each substitution, the starting amino acid in SEQ ID NO: 10 is indicated by a single letter code, followed by its position in SEQ ID NO: 10 and the substituted amino acid indicated by a single letter code.

[0202]

[0203]

[0204]

[0205] Other preferred mutant polypeptides according to the present invention are based on the amino acid sequence of the glycoprotein G extracellular domain of the VSV New Jersey strain and can be selected from:

[0206] a) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 72, which corresponds to SEQ ID NO: 12 in which the valine (V) amino acid residue at position 429 is substituted with an isoleucine (I) amino acid residue;

[0207] b) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 73, which corresponds to SEQ ID NO: 12 in which the valine (V) amino acid residue at position 429 is substituted with a leucine (L) amino acid residue;

[0208] c) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 74, which corresponds to SEQ ID NO: 12 in which the valine (V) amino acid residue at position 429 is substituted with a phenylalanine (F) amino acid residue;

[0209] d) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 75, which corresponds to SEQ ID NO: 12 in which the valine (V) amino acid residue at position 429 is substituted with a methionine (M) amino acid residue;

[0210] e) A mutant polypeptide comprising, or consisting essentially of, or consisting of an amino acid sequence as defined in any one of a) to d) above, and further comprising a signal peptide at the N-terminus, preferably the signal peptide corresponding to positions 1-16 of SEQ ID NO: 11.

[0211] The amino acid sequences of preferred mutant polypeptides derived from the extracellular domain of VSV New Jersey glycoprotein G are shown in Table 8 below, SEQ ID NOs: 72 to 75.

[0212] Table 8. Amino acid sequences SEQ ID NOs: 72 to 75 based on the extracellular domain of glycoprotein G of VSV New Jersey strain (SEQ ID NO: 12), and relevant substitutions compared to SEQ ID NO: 12. For each substitution, the starting amino acid in SEQ ID NO: 12 is indicated by a single letter code, followed by its position in SEQ ID NO: 12 and the substituted amino acid indicated by a single letter code.

[0213]

[0214]

[0215] Other preferred mutant polypeptides according to the present invention are based on the amino acid sequence of the glycoprotein G extracellular domain of the VSV Carajas strain and can be selected from:

[0216] a) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 76, which corresponds to SEQ ID NO: 14 in which the valine (V) amino acid residue at position 426 is substituted with an isoleucine (I) amino acid residue;

[0217] b) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 77, which corresponds to SEQ ID NO: 14 in which the valine (V) amino acid residue at position 426 is substituted with a leucine (L) amino acid residue;

[0218] c) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 78, which corresponds to SEQ ID NO: 14 in which the valine (V) amino acid residue at position 426 is substituted with a phenylalanine (F) amino acid residue;

[0219] d) a mutant polypeptide comprising, consisting essentially of, or consisting of the amino acid sequence set forth in SEQ ID NO: 79, which corresponds to SEQ ID NO: 14 in which the valine (V) amino acid residue at position 426 is substituted with a methionine (M) amino acid residue;

[0220] e) A mutant polypeptide comprising, or consisting essentially of, or consisting of an amino acid sequence as defined in any one of a) to d) above, and further comprising a signal peptide at the N-terminus, preferably the signal peptide corresponding to positions 1-21 of SEQ ID NO: 13.

[0221] The amino acid sequences of preferred mutant polypeptides derived from the VSV Carajas glycoprotein G extracellular domain, SEQ ID NOs: 76 to 79, are shown in Table 9 below.

[0222] Table 9. Amino acid sequences based on the VSV Carajas strain glycoprotein G extracellular domain (SEQ ID NO: 14) SEQ ID NO: 76 to 79, and related substitutions compared to SEQ ID NO: 14. For each substitution, the starting amino acid in SEQ ID NO: 14 is indicated by the single-letter code, followed by its position in SEQ ID NO: 14 and the substituted amino acid indicated by the single-letter code.

[0223]

[0224]

[0225] Therefore, the mutant polypeptide of the present invention advantageously comprises, essentially consists of, or consists of an amino acid sequence selected from SEQ ID NOs: 17-79, preferably an amino acid sequence selected from SEQ ID NOs: 17-72 or SEQ ID NOs: 74-79.

[0226] Further optional mutations

[0227] The mutant polypeptide according to the present invention is derived from the amino acid sequence of the extracellular domain of glycoprotein G of a VSV strain and therefore comprises, or essentially consists of, or consists of the following sequence: the amino acid sequence set forth in SEQ ID NO: 2 or an amino acid sequence having at least 50% identity (or any other minimum % identity disclosed above) to the amino acid sequence set forth in SEQ ID NO: 2, said sequence having at least one substitution of an amino acid residue as defined above.

[0228] The mutant polypeptide according to the present invention may further contain one or more (eg 1, 2 or more) additional substitutions at additional positions in SEQ ID NO: 2 or at equivalent positions after optimal global alignment with SEQ ID NO: 2.

[0229] When it is desired not to alter the function of the extracellular domain, the possible additional substitution(s) will preferably be conservative, meaning that the substituted amino acid has a similar structure to the original amino acid and is therefore less likely to alter the biological activity of the polypeptide. Examples of such conservative substitutions are shown in Table 10 below:

[0230] Table 10. Examples of conservative substitutions.

[0231]

[0232]

[0233] In addition, as explained above, Figure 4The alignment shown shows that the 1st, 4th, 6-7th, 12th, 14th, 17-18th, 21st, 23rd, 25th, 27th, 29th, 31st, 33rd, 46th, 47th, 55th, 56th, 58th, 60th, 64th, 66th, 69th, 71st, 75th, 77th, 79th, 81st, 82nd, 87th, 91st, 92nd, 96th, 102nd, 107th, 111st, 114th, 116th, 119th, 121st, 122nd, 123rd, 124th, 125th, 126th, 127th, 128th, 129th, 130th, 131st, 132nd, 133rd, 134th, 135th 27, 130, 132, 134, 137-139, 141, 143, 145, 151, 153, 158, 160, 162-165, 167, 177, 199, 204, 206-208, 210, 212, 219, 221, 224, 228, 231, 236-237, 241, 253, 259, 26 2, 268, 271-272, 274-277, 279-281, 283-285, 287-290, 299, 301, 304, 307-311, 313-314, 316-318, 320-321, 323, 325-326, 330, 332, 338, 345, 349, 354, 356-357 , 360, 362, 368-372, 374, 376, 379, 381, 383-384, 388, 390, 393, 395, 407-408, 413, 421, 426-429, 431-434, 436, 439-443, 445, 447, 456, 467, 487 and 489-490 are conserved in the amino acid sequence of the glycoprotein G extracellular domain of VSV Indiana, Maraba, Cocal, Morreton, Alagoa, New Jersey and Carajas strains. Conserved amino acid positions are generally associated with conserved functions, and according to the present invention, a mutant polypeptide comprising an amino acid sequence having at least 50% identity (or any other minimum % identity disclosed above) with the amino acid sequence set forth in SEQ ID NO: 2, when it is desired not to alter the function of the extracellular domain, preferably has the same amino acid as SEQ ID NO: 2 at one or more of the conserved positions defined above (such as at all the conserved positions defined above) after optimal global alignment with SEQ ID NO: 2.

[0234] However, in some cases, it may be necessary to alter the function of the extracellular domain, for example to alter the ability of the extracellular domain to bind to the low-density lipoprotein receptor (LDL-R), as described in the application filed under number PCT / EP2018 / 075824 and in Nikolic et al., Nat Commun. 2018 Mar 12; 9(1): 1029. This allows altering the tropism of VSV expressing an extracellular domain that is unable to interact with the LDL membrane receptor.

[0235] Therefore, in one embodiment of the present invention, the mutant polypeptide according to the present invention further comprises a substitution of at least one amino acid residue selected from the group consisting of amino acid residues at positions 8, 47, 209 and 354 of SEQ ID NO: 2, or amino acid residues at positions 8, 47, 209 and 354 of SEQ ID NO: 2 after optimal global alignment with SEQ ID NO: 2.

[0236] For substitution at position 8 or an equivalent position after optimal global alignment with SEQ ID NO: 2, the original amino acid is preferably substituted by any amino acid except histidine (H), glutamine (Q) or tyrosine (Y), more preferably the original amino acid is substituted by alanine (A).

[0237] For substitution at position 47 of SEQ ID NO: 2 or an equivalent position after optimal global alignment with SEQ ID NO: 2, the original amino acid is preferably substituted by any amino acid except lysine (K) or arginine (R), more preferably the original amino acid is substituted by alanine (A) or glutamine (Q).

[0238] For substitution at position 209 or an equivalent position after optimal global alignment with SEQ ID NO: 2, the original amino acid is preferably substituted with any amino acid except tyrosine (Y) or histidine (H), more preferably the original amino acid is substituted with alanine (A).

[0239] For substitution at position 354 or an equivalent position after optimal global alignment with SEQ ID NO: 2, the original amino acid is preferably substituted by any amino acid except lysine (K) or arginine (R), more preferably the original amino acid is substituted by alanine (A) or glutamine (Q).

[0240] Preferably, positions 47 and 354 of SEQ ID NO: 2 or equivalent positions after the best global alignment with SEQ ID NO: 2 are used to obtain an extracellular domain that is unable to interact with the LDL membrane receptor. When it is required that the mutant polypeptide according to the present invention is unable to interact with the LDL membrane receptor, the mutant polypeptide is therefore further preferably included in SEQ ID NO: 2 at position 47 or an equivalent position after the best global alignment with SEQ ID NO: 2, at position 354 of SEQ ID NO: 2 or an equivalent position after the best global alignment with SEQ ID NO: 2, or at two substitutions at positions 47 and 354 of SEQ ID NO: 2 or an equivalent position after the best global alignment with SEQ ID NO: 2. More preferably, the substitutions at positions 47 and / or 354 are those defined as preferred above.

[0241] Fusion peptide

[0242] The present invention also relates to a fusion polypeptide comprising, consisting essentially of, or consisting of a mutant polypeptide of the present invention and an additional peptide, polypeptide, or protein, wherein the additional peptide, polypeptide, or protein is inserted between:

[0243] a) the N-terminus of the mutated polypeptide,

[0244] b) located between any two consecutive amino acids in the region corresponding to positions 192 to 202 of SEQ ID NO: 2 or in the equivalent positions after optimal global alignment with SEQ ID NO: 2,

[0245] c) between any two consecutive amino acids in the region corresponding to positions 240 to 257 of SEQ ID NO: 2 or in the equivalent positions after optimal global alignment with SEQ ID NO: 2,

[0246] d) located between any two consecutive amino acids in the region corresponding to positions 347 to 353 of SEQ ID NO: 2 or in the equivalent positions after optimal global alignment with SEQ ID NO: 2,

[0247] e) located between any two consecutive amino acids in the region corresponding to positions 364 to 366 of SEQ ID NO: 2 or in the equivalent positions after optimal global alignment with SEQ ID NO: 2,

[0248] f) between any two consecutive amino acids in the region corresponding to positions 376 to 379 of SEQ ID NO: 2 or in the equivalent positions after optimal global alignment with SEQ ID NO: 2,

[0249] Preferably, the additional peptide, polypeptide or protein is inserted at: the N-terminus of the mutant polypeptide, or between amino acids 351 and 352 of SEQ ID NO: 2 or equivalent positions after optimal global alignment with SEQ ID NO: 2.

[0250] The additional peptide, polypeptide, or protein can have a variety of functions, but can be particularly useful for targeting the recombinant VSV virus to specific target cells. In this context, any additional peptide, polypeptide, or protein that is capable of specifically binding to an antigen expressed on the extracellular surface of the target cell can be used. In particular, the additional peptide, polypeptide, or protein can comprise at least a portion of a ligand for a cellular receptor.

[0251] When the target cell expresses one component of a (receptor-ligand) pair (e.g., EGF-EGFR, TNFa-TNFaR, PD1-PDL1 or PDL2, etc.) on its surface (this often happens because molecules expressed on the cell surface often have cognate receptors or ligands), then at least a portion of the second component of the (receptor-ligand) pair (i.e., the natural receptor or ligand of the targeted cell surface antigen) can be used (provided that it is still able to bind to its cognate receptor or ligand).

[0252] Alternatively, antibodies, functional antibody fragments.

[0253] An "antibody" or "immunoglobulin" refers to a molecule that contains at least one binding domain for a given antigen and constant domains, wherein the constant domains include an Fc fragment that can bind to an Fc receptor (FcR). In most mammals (such as humans and mice), antibodies are composed of four polypeptide chains: two heavy chains and two light chains, which are held together by a variable number of disulfide bonds, providing flexibility to the molecule. Each light chain consists of a constant domain (CL) and a variable domain (VL); depending on the antibody's isotype, the heavy chain consists of a variable domain (VH) and three or four constant domains (CH1 to CH3 or CH1 to CH4). In a few rare mammals (such as camels and alpacas), antibodies are composed of only two heavy chains, each of which contains a variable domain (VH) and a constant region.

[0254] The variable domains are involved in antigen recognition, whereas the constant domains are involved in the biological, pharmacokinetic, and effector properties of the antibody.

[0255] "Functional antibody fragments" refer to antibody fragments that retain the antigen-binding domain and therefore have the same antigen specificity as the original antibody. In most mammals, such functional antibody fragments include Fv, ScFv, Fab, F(ab')2, Fab', and scFv-Fc fragments. In the case of camels and alpacas, where antibodies consist only of two heavy chains, each containing a variable domain (called VHH) and a constant region, such functional antibodies correspond to VHH fragments (also called nanobodies).

[0256] In the context of the present invention, the additional peptide, polypeptide or protein will preferably be a peptide or relatively short polypeptide (preferably less than 200 amino acids), so as not to alter the function of the mutant polypeptide according to the invention. Thus, when an antibody or functional antibody fragment is an additional peptide, polypeptide or protein of the selected type, a functional antibody fragment will preferably be used. Although any suitable functional antibody fragment can be used in the context of the present invention, nanobodies (or VHH fragments) will be preferably used due to their small size, globular shape and robustness.

[0257] The antigens targeted to the cell surface will be different, depending on the target cell. For example, when the recombinant VSV virus expressing the mutant polypeptide according to the present invention is used as an oncolytic virus, the mutant polypeptide according to the present invention can be fused with an antibody or functional antibody fragment (particularly nano antibody) that targets the G extracellular domain to a cancer cell antigen as described above. For example, anti-HER2 or anti-MUC18 or anti-EGFR or anti-CD20 or anti-CD52 antibodies or functional antibody fragments (particularly nano antibodies) can be used. In another case, when it is necessary to target immune cells expressing inhibitory immune checkpoints (such as PD1 or its ligands PD-L1 and PD-L2, or CTLA4), antibodies or functional antibody fragments (particularly nano antibodies) that target such inhibitory immune checkpoints can be used. In addition, when it is necessary to target immune cells expressing inhibitory immune checkpoints (such as PD1 or its ligands PD-L1 and PD-L2, or CTLA4), antibodies or functional antibody fragments (particularly nano antibodies) that target such inhibitory immune checkpoints can be used. Similarly, when it is necessary to target B cells, antibodies or functional antibody fragments (particularly nano antibodies) that target B lymphocyte antigen CD19 can be used. An exemplary Nanobody against GFP has the amino acid sequence SEQ ID NO: 80 (VQLVESGGALVQPGGSLRLSCAASGFPVNRYSMRWYRQAPGKEREWVAGMSSAGDRSSYEDSVKGRFTISRDDARNTVYLQMNSLKPEDTAVYYCNVNVGFEYWGQGTQVTVSS).

[0258] When an additional peptide, polypeptide or protein (preferably a functional antibody fragment, such as a Nanobody) is inserted at the N-terminus of a mutant polypeptide according to the present invention, it can be directly fused to the N-terminus of the mutant polypeptide or separated from the N-terminus of the mutant polypeptide by a linker peptide, preferably separated from the N-terminus of the mutant polypeptide by a first linker peptide.

[0259] Typically, a linker is a peptide consisting of amino acid residues of 1 to 30 amino acids in length, such as glycine (G), serine (S), threonine (T), asparagine (N), glutamine (Q), alanine (A), proline (P) and / or phenylalanine (F). Preferred linkers in the context of the present invention comprise 2 to 15 amino acids, preferably 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 or 12 amino acids.

[0260] The first linker peptide between the additional peptide, polypeptide or protein (preferably a functional antibody fragment, such as a Nanobody) and the mutant polypeptide according to the invention is 2 to 15 amino acids long, preferably 4 to 12 or 6 to 10 amino acids long, and in particular 8 amino acids long. Alternatively or in combination, its amino acid sequence preferably consists of amino acids selected from the group consisting of glycine (G), serine (S), threonine (T), asparagine (N), glutamine (Q), alanine (A), proline (P) and phenylalanine (F), more preferably selected from the group consisting of glycine (G), serine (S), threonine (T) and alanine (A), or selected from the group consisting of glycine (G), serine (S), threonine (T), or selected from the group consisting of glycine (G), serine (S) and alanine (A), even more preferably selected from the group consisting of glycine (G) and serine (S). In a preferred embodiment, the first linker peptide consists of 6 to 10 amino acids selected from glycine (G) and serine (S), and in particular may consist of the amino acid sequence GGGGSGGGGS (SEQ ID NO: 81).

[0261] When an additional peptide, polypeptide or protein (preferably a functional antibody fragment, such as a Nanobody) is inserted into the N-terminus of the mutant polypeptide according to the invention, the fusion polypeptide may further comprise a signal peptide at the N-terminus of the additional peptide, polypeptide or protein (preferably a functional antibody fragment, such as a Nanobody) to localize the fusion polypeptide to the viral envelope (when the fusion polypeptide is expressed by a virus) or the cell membrane (when the fusion polypeptide is expressed by a host cell).

[0262] In this case, the fusion polypeptide according to the invention comprises, or essentially consists of, or consists of, from N-terminus to C-terminus: a signal peptide, an optional second linker peptide, an additional peptide, polypeptide or protein (preferably a functional antibody fragment, such as a Nanobody), an optional first linker peptide and a mutant polypeptide according to the invention. In this fusion polypeptide, when the first linker peptide is present, the first linker peptide is as described above. When the second linker peptide is present (between the signal peptide and the additional peptide, polypeptide or protein (preferably a functional antibody fragment, such as a Nanobody)), the second linker peptide is 2 to 15 amino acids long, preferably 2 to 6 amino acids long, 2 to 4 amino acids long, and in particular 2 or 3 amino acids long. Alternatively or in combination, its amino acid sequence is preferably composed of amino acids selected from the group consisting of glycine (G), serine (S), threonine (T), asparagine (N), glutamine (Q), alanine (A), proline (P) and phenylalanine (F), more preferably selected from the group consisting of serine (S), threonine (T), asparagine (N), glutamine (Q) and phenylalanine (F), in particular selected from the group consisting of serine (S), threonine (T), asparagine (N) and glutamine (Q), or selected from the group consisting of glutamine (Q) and serine (S), or glutamine (Q) and phenylalanine (F). In a preferred embodiment, the second linker peptide consists of 2 to 4 amino acids, and the amino acids are selected from serine (S), threonine (T), asparagine (N), glutamine (Q) and phenylalanine (F), in particular selected from serine (S), threonine (T), asparagine (N) and glutamine (Q), or selected from glutamine (Q) and serine (S), or glutamine (Q) and phenylalanine (F), and the second linker peptide can especially be the amino acid sequence QF or QS.

[0263] In a preferred embodiment, the fusion polypeptide according to the present invention comprises the first linker peptide or the second linker peptide, more preferably comprises both the first linker peptide and the second linker peptide.

[0264] When the fusion polypeptide according to the present invention comprises both a first linker peptide and a second linker peptide:

[0265] The first linker peptide (between the additional peptide, polypeptide or protein (preferably a functional antibody fragment, such as a Nanobody) and the mutant polypeptide according to the invention) preferably consists of 6 to 10 amino acids, said amino acids being chosen from glycine (G) and serine (S), and may in particular be the amino acid sequence GGGGSGGGGS (SEQ ID NO: 81); and

[0266] The second linker peptide (between the signal peptide and the additional peptide, polypeptide or protein (preferably a functional antibody fragment, such as a Nanobody)) preferably consists of 2 to 4 amino acids, said amino acids being chosen from serine (S), threonine (T), asparagine (N), glutamine (Q) and phenylalanine (F), in particular from serine (S), threonine (T), asparagine (N) and glutamine (Q), or from glutamine (Q) and serine (S), or glutamine (Q) and phenylalanine (F), and said second linker peptide may in particular be the amino acid sequence QF or QS.

[0267] In a preferred embodiment, when the fusion polypeptide according to the invention comprises both a first linker peptide and a second linker peptide, the first linker peptide (between the additional peptide, polypeptide or protein (preferably a functional antibody fragment, such as a Nanobody) and the mutant polypeptide according to the invention) has the amino acid sequence GGGGSGGGGS (SEQ ID NO: 81), and the second linker peptide (between the signal peptide and the additional peptide, polypeptide or protein (preferably a functional antibody fragment, such as a Nanobody)) has the amino acid sequence QF or QS.

[0268] An exemplary preferred fusion polypeptide has the sequence SEQ ID NO: 82

[0269]

[0270] Nucleic acid molecules

[0271] The present invention also relates to nucleic acid molecules encoding a mutant polypeptide or a fusion polypeptide according to the present invention.

[0272] Due to the degeneracy of the genetic code, all different nucleic acid sequences encoding a particular amino acid sequence are within the scope of the present invention.

[0273] In some embodiments, the present invention provides a nucleic acid sequence that is optimized to promote its expression in host cell or any other production host. In fact, there are usually several trinucleotide combinations encoding identical amino acids (except methionine and tryptophan), and these combinations are called synonymous codons. However, cells or given organisms usually preferably use some codons in these combinations (this is called genetic code usage deviation). This preference especially depends on the production organism from which the cell is derived. Therefore, when the protein derived from one or more organisms is produced in the cell of a heterologous organism or this heterologous organism, it may be useful to modify the nucleic acid sequence encoding the protein with the preferred codons mainly using this heterologous organism. The data on the use of the preferred codons of different species can be obtained in the literature, and those skilled in the art know how to optimize the expression of a given protein in the cell of a heterologous organism or this heterologous organism.

[0274] Preferred nucleic acid molecules include those based on the native nucleotide sequence encoding the glycoprotein G ectodomain of VSV Indiana strain (SEQ ID NO: 83) that is mutated at one or more nucleotides to generate substitutions as defined above. Preferred nucleic acid molecules include those having a nucleotide sequence selected from the group consisting of SEQ ID NO: 83 to SEQ ID NO: 86, which are more precisely defined in Table 11 below.

[0275] Table 11. Preferred nucleotide sequences encoding wild-type (SEQ ID NO:83) or mutant (SEQ ID NO:84: c112a nucleotide substitution, encoding the H22N mutant of the amino acid sequence SEQ ID NO:17; SEQ ID NO:85: g1313t nucleotide substitution, encoding the S422I mutant of the amino acid sequence SEQ ID NO:18; and SEQ ID NO:86: c112a g1313t nucleotide substitution, encoding the H22N S422I mutant of the amino acid sequence SEQ ID NO:23) VSV Indiana glycoprotein G extracellular domain.

[0276]

[0277]

[0278]

[0279]

[0280] The nucleic acid molecules according to the present invention may further contain any modifications aimed at improving the cloning and / or expression of the encoded mutant polypeptide or fusion polypeptide according to the present invention as well as its folding and stability.

[0281] carrier

[0282] The present invention further relates to a vector comprising at least one nucleic acid according to the invention or expressing a mutant polypeptide or a fusion polypeptide according to the invention.

[0283] This vector comprises the necessary elements of expressing the described nucleotide sequence, especially promotor, transcription initiation codon, terminator sequence and suitable transcriptional control sequence.These elements change according to the host that is used for expression, and those skilled in the art are easy to select these elements based on their common sense.

[0284] In the context of the present invention, the term "vector" must be understood broadly to include plasmids and viral vectors. In the context of the present invention, suitable vectors include, but are not limited to, phage, plasmid, or cosmid vectors for expression in prokaryotic host cells such as bacteria (e.g., E. coli, BCG, or Listeria); vectors for expression in yeast (e.g., Saccharomyces cerevisiae, Schizosaccharomyces pombe, Pichia pastoris); baculovirus vectors for expression in insect cell systems (e.g., Sf9 cells); and plasmid and viral vectors for expression in higher eukaryotic cells or subjects. Typically, such vectors are commercially available (e.g., at Invitrogen, Stratagene, Amersham Biosciences, Promega, etc.), or are available from depositories such as the American Type Culture Collection (ATCC, Rockville, MD), or have been the subject of numerous publications describing the sequence, organization, and production methods of such vectors, allowing the skilled artisan to apply such vectors.

[0285] As used herein, "plasmid vector" refers to a replicable DNA construct. Typically, a plasmid vector contains a selectable marker gene that allows selection or non-selection of host cells carrying the plasmid vector in the presence of a corresponding selective drug. Many positively selectable and negatively selectable marker genes are known in the art. For example, antibiotic resistance genes can be used as positive selection marker genes that allow selection of host cells in the presence of a corresponding antibiotic. Suitable plasmid vectors are commercially available.

[0286] As used herein, the term "viral vector" refers to a nucleic acid vector that comprises at least one element of a viral genome and can be packaged into or into viral particles. The terms "virus," "virion," "viral particle," and "viral vector particle" are used interchangeably to refer to viral particles formed when a nucleic acid vector is transduced into a suitable cell or cell line under suitable conditions that allow the production of viral particles. In the context of the present invention, the term "viral vector" must be broadly understood to include nucleic acid vectors (e.g., DNA viral vectors) and viral particles generated therefrom. The term "infectious" refers to the ability of a viral vector to infect and enter a host cell or subject.

[0287] The viral vector may preferably be a vesicular stomatitis virus (VSV) vector comprising at least one nucleic acid according to the present invention or expressing a mutant polypeptide or a fusion polypeptide according to the present invention.

[0288] VSV is an enveloped negative-strand RNA virus belonging to the genus Vesiculovirus of the family Rhabdoviridae. The VSV negative-strand RNA genome encodes five structural proteins and includes, from 3' to 5', genes for the leader region, nucleoprotein (N), phosphoprotein (P), matrix protein (M), glycoprotein (G), and polymerase protein (L), and a trailer region. Therefore, by replacing the natural wild-type sequence (encoding the natural wild-type glycoprotein G) with a nucleic acid sequence according to the present invention (encoding the mutant polypeptide or fusion polypeptide according to the present invention), a mutant VSV vector according to the present invention can be obtained. Standard techniques for generating mutant VSV vectors can be used for this purpose. In particular, reverse genetics can be used to recover the recombinant virus.

[0289] With respect to other regions of the VSV genome (leader, genes encoding nucleoprotein (N), phosphoprotein (P), matrix protein (M), glycoprotein (G), and polymerase protein (L), and the tail region), the mutant VSV vector may contain any suitable natural or artificial sequence. In particular, the complete genome sequences of various Indiana strain isolates (Rodriguez et al., J Gen Virol. 2002 Oct; 83(Pt 10): 2475-83) and New Jersey strain isolates (Velazquez-Salinas et al., Genome Announc. 2017 Sep 14; 5(37)) are known in the art. In addition, various VSV strains are available from the American Type Culture Collection (ATCC) under the reference numbers VR-1238, VR-1239, VR-159, and VR-1415 to VR-1421.

[0290] In one embodiment, the vector according to the present invention (preferably a VSV vector) is preferably oncolytic, meaning that the vector preferentially infects and kills cancer cells. All of the VSV strains listed previously (Indiana, Maraba, Cocal, Morreton, Alagoa, New Jersey, and Carajas) are potentially oncolytic and can therefore be used.

[0291] Alternatively or in combination, the vectors according to the present invention (preferably VSV vectors) may also be used in gene therapy, immunotherapy and the selective delivery of cargo to selected cell types.

[0292] When used in gene therapy, the vector according to the present invention (preferably a VSV vector) further encodes a gene of therapeutic interest in order to restore the activity of the gene in cells lacking the activity.

[0293] When used for immunotherapy, the vector according to the present invention (preferably a VSV vector) further encodes at least one antigen of interest and / or molecules involved in the regulation of immune responses, such as cytokines, adjuvants, immune checkpoint regulators, antibodies targeting cytokines, etc.

[0294] When aiming to deliver cargo to selected cell types (such as unstimulated T cells, B cells, and hematopoietic cells), recombinant mutant glycoproteins can be inserted into the surface of VLPs containing therapeutic molecules, markers, or any drug.

[0295] According to a preferred embodiment, the viral vector according to the present invention (particularly a VSV vector) is in the form of infectious viral particles. Typically, such viral particles are produced by a method comprising the following steps: (i) introducing the viral vector of the present invention into suitable producer cells, (ii) culturing the producer cells under suitable conditions allowing the production of the infectious viral particles, (iii) recovering the produced viral particles from the culture of the producer cells, and (iv) optionally purifying the recovered viral particles.

[0296] host cells

[0297] The present invention also relates to a host cell containing or expressing a mutant polypeptide or fusion polypeptide according to the invention, or containing a nucleic acid molecule according to the invention, or containing a vector according to the invention (in particular a VSV vector).

[0298] When the host cell contains a vector according to the present invention (particularly a VSV vector), the host cell is preferably a eukaryotic cell suitable for VSV replication, such as BSR cells (BHK-21: Baby Hamster Kidney cells, a clone of ATCC CCL-10), BHK-21 cells (ATCC CCL-10) or Vero cells (ATCC CCL-81).

[0299] Composition

[0300] The present invention also relates to a composition comprising, consisting essentially of, or consisting of a mutant polypeptide or fusion polypeptide according to the invention, a nucleic acid molecule according to the invention, a vector according to the invention, a host cell according to the invention, or any combination thereof.

[0301] Preferably, the composition is a pharmaceutical composition comprising a therapeutically effective amount of an active agent (a mutant polypeptide or fusion polypeptide according to the present invention, a nucleic acid molecule according to the present invention, a vector according to the present invention, a host cell according to the present invention, or any combination thereof) and one or more pharmaceutically acceptable carriers.

[0302] As used herein, "pharmaceutically acceptable carrier" is intended to include any and all carriers, solvents, diluents, excipients, adjuvants, dispersion media, coatings, antibacterial and antifungal agents and absorption delaying agents, etc., that are compatible with administration in a subject, particularly a human.

[0303] As used herein, a "therapeutically effective amount" is a dosage sufficient for the intended use.

[0304] The composition preferably comprises a vector according to the invention, and more particularly a VSV vector according to the invention.

[0305] Therapeutic / in vivo uses

[0306] The present invention also relates to the use of a vector according to the invention (in particular a VSV vector according to the invention, preferably an oncolytic VSV vector according to the invention) or a (pharmaceutical) composition according to the invention (in particular a composition comprising a vector according to the invention, more particularly a composition comprising a VSV vector according to the invention, preferably a composition comprising an oncolytic VSV vector according to the invention) as a medicament.

[0307] The present invention also relates to the use of a vector according to the invention (in particular a VSV vector according to the invention, preferably an oncolytic VSV vector according to the invention) or a (pharmaceutical) composition according to the invention (in particular a composition comprising a vector according to the invention, more particularly a composition comprising a VSV vector according to the invention, preferably a composition comprising an oncolytic VSV vector according to the invention) for treating cancer.

[0308] The present invention also relates to the use of a vector according to the present invention (in particular a VSV vector according to the present invention, preferably an oncolytic VSV vector according to the present invention) or a (pharmaceutical) composition according to the present invention (in particular a composition comprising a vector according to the present invention, more particularly a composition comprising a VSV vector according to the present invention, preferably a composition comprising an oncolytic VSV vector according to the present invention) for the manufacture of a medicament for the treatment of cancer.

[0309] The present invention also relates to the use of a vector according to the present invention (in particular a VSV vector according to the present invention, preferably an oncolytic VSV vector according to the present invention) or a (pharmaceutical) composition according to the present invention (in particular a composition comprising a vector according to the present invention, more particularly a composition comprising a VSV vector according to the present invention, preferably a composition comprising an oncolytic VSV vector according to the present invention) for treating cancer.

[0310] The present invention also relates to a method for treating cancer in a subject in need thereof, which method comprises administering to the subject a therapeutically effective amount of a vector according to the invention (in particular a VSV vector according to the invention, preferably an oncolytic VSV vector according to the invention) or a (pharmaceutical) composition according to the invention (in particular a composition comprising a vector according to the invention, more particularly a composition comprising a VSV vector according to the invention, preferably a composition comprising an oncolytic VSV vector according to the invention).

[0311] Since the VSV virus is an oncolytic virus, it can be used to treat various types of cancer, including prostate cancer, breast cancer, pancreatic cancer, and melanoma (Bishnoi. Viruses 10, (2018)).

[0312] The present invention also relates to the use of a vector according to the invention (in particular a VSV vector according to the invention) or a (pharmaceutical) composition according to the invention (in particular a composition comprising a vector according to the invention, more particularly a composition comprising a VSV vector according to the invention) for gene therapy or immunotherapy (in particular as a vaccine).

[0313] The present invention also relates to the use of a vector according to the invention (in particular a VSV vector according to the invention) or a (pharmaceutical) composition according to the invention (in particular a composition comprising a vector according to the invention, more particularly a composition comprising a VSV vector according to the invention) for the manufacture of a medicament for gene therapy or immunotherapy (in particular as a vaccine).

[0314] The present invention also relates to the use of a vector according to the invention (in particular a VSV vector according to the invention) or a (pharmaceutical) composition according to the invention (in particular a composition comprising a vector according to the invention, more particularly a composition comprising a VSV vector according to the invention) for gene therapy or immunotherapy (in particular as a vaccine).

[0315] The present invention also relates to a method for gene therapy or immunotherapy in a subject in need thereof, which method comprises administering to the subject a therapeutically effective amount of a vector according to the invention (in particular a VSV vector according to the invention) or a (pharmaceutical) composition according to the invention (in particular a composition comprising a vector according to the invention, more particularly a composition comprising a VSV vector according to the invention).

[0316] The vectors according to the invention (and in particular the VSV vectors according to the invention) used for gene therapy or immunotherapy are preferably as disclosed above in the section "Vectors".

[0317] Gene therapy can be used every time there is a need to correct defective gene activity in defective cells.

[0318] Immunotherapy can be used to treat a variety of diseases, including cancer, infectious diseases, and inflammatory diseases (particularly autoimmune diseases).

[0319] The present invention also relates to the use of a vector according to the invention (in particular a VSV vector according to the invention) or a (pharmaceutical) composition according to the invention (in particular a composition comprising a vector according to the invention, more particularly a composition comprising a VSV vector according to the invention) for the selective delivery of a cargo to a selected cell type in vivo.

[0320] The present invention also relates to the use of a vector according to the invention (in particular a VSV vector according to the invention) or a (pharmaceutical) composition according to the invention (in particular a composition comprising a vector according to the invention, more particularly a composition comprising a VSV vector according to the invention) for the manufacture of a medicament for the selective delivery of a cargo to a selected cell type in vivo.

[0321] The present invention also relates to the use of a vector according to the invention (in particular a VSV vector according to the invention) or a (pharmaceutical) composition according to the invention (in particular a composition comprising a vector according to the invention, more particularly a composition comprising a VSV vector according to the invention) for the selective delivery of a cargo to a selected cell type in vivo.

[0322] The present invention also relates to a method for selectively delivering a cargo to a selected cell type in vivo in a subject in need thereof, said method comprising administering to said subject a therapeutically effective amount of a vector according to the invention (in particular a VSV vector according to the invention) or a (pharmaceutical) composition according to the invention (in particular a composition comprising a vector according to the invention, more particularly a composition comprising a VSV vector according to the invention).

[0323] The vectors according to the invention (and in particular the VSV vectors according to the invention) for selectively delivering a cargo to a selected cell type in vivo are preferably as disclosed above in the section "Vectors".

[0324] The present invention also relates to a mutant polypeptide according to the invention, or a fusion polypeptide according to the invention, or a vector according to the invention, or a host cell according to the invention, or a composition according to the invention (in particular a composition comprising a vector according to the invention, more particularly a composition comprising a VSV vector according to the invention) or a combination thereof, for targeting a lipid membrane to a specific target in a subject, such as a cell, in particular a cell to be killed (such as a cancer cell) or an unstimulated T cell, B cell and hematopoietic cell, wherein the mutant polypeptide or fusion polypeptide is anchored in the lipid membrane.

[0325] In vitro use

[0326] The present invention also relates to the in vitro use of a mutant polypeptide according to the invention, or a fusion polypeptide according to the invention, or a vector according to the invention (in particular a VSV vector according to the invention), or a host cell according to the invention, or a composition according to the invention (in particular a composition comprising a vector according to the invention, more particularly a composition comprising a VSV vector according to the invention), or a combination thereof, for selectively delivering a cargo to selected cell types (such as unstimulated T cells, B cells and hematopoietic cells).

[0327] The vectors according to the invention (and in particular the VSV vectors according to the invention) for selectively delivering a cargo to a selected cell type in vitro are preferably as disclosed above in the section "Vectors".

[0328] The present invention also relates to the in vitro use of a mutant polypeptide according to the invention, or a fusion polypeptide according to the invention, or a vector according to the invention, or a host cell according to the invention, or a composition according to the invention (in particular a composition comprising a vector according to the invention, more particularly a composition comprising a VSV vector according to the invention) or a combination thereof for targeting a lipid membrane to a specific target, such as a cell, in particular a cell to be killed (such as a cancer cell) or an unstimulated T cell, B cell and hematopoietic cell, wherein the mutant polypeptide or fusion polypeptide is anchored in the lipid membrane.

[0329] The following examples are intended only to illustrate the present invention.

[0330] Example

[0331] Example 1: Selection of H22N and S422I mutations in Indiana VSV G to produce recombinant VSV virus expressing anti-GFP targeted G protein.

[0332] Materials and methods

[0333] Construction of GNano (first chimera)

[0334] The GNano construct was created starting from the VSV G gene (Indiana strain) cloned in the pCAGGS plasmid. The pCAGGS plasmid containing the desired coding GNano sequence was generated using the Gibson assembly method, in which the nanobody was inserted at different positions. The empty vector pCAGGS was linearized using the EcoRI restriction enzyme. Three PCR products with overlapping parts were then generated. Product I is the G fragment before the nanobody insertion site. Product II is the nanobody gene. Product III is the G fragment after the insertion site. The PCR products and the linearized vector were combined and ligated by incubation with NEB Master Mix.

[0335] Obtaining and amplifying recombinant VSV virus in BSR cells

[0336] Recombinant VSV was obtained as described in Schnell et al., J. virol. 1996. The plasmid pVSVFL(+)-GNano, which expresses the 11,161 nucleotide (nt) positive-strand full-length VSV RNA sequence with mutant GNano replacing wt VSV G, was generated using two unique restriction sites present on pVSVFL(+). The two restriction sites, MluI, are in the 5' noncoding sequence of the G gene, while NheI is present in the sequence introduced between the G and L genes. BSR cells were infected with vaccinia virus at an MOI of 10. One hour later, pBS-N, pBS-P, pBS-L, and pcDNA3.1-G plasmids (encoding N, P, L, and G proteins, respectively) plus the pVSVFL(+)-GNano plasmid were transfected into the cells using lipofectamine 2000 (Invitrogen) in the presence of 10 μg / ml AraC (Sigma). The plasmids and amounts used were as follows: 5 μg pVSVFL(+)_GNano, 2.5 μg pBS-N, 2 μg pBS-P, 1 μg pCDNA3.1-G, and 0.5 μg pBS-L. After incubation at 37°C, 5% CO₂ for 48 h, the supernatant of the transfected cells was collected and the debris from the cell lysate was pelleted by centrifugation. The supernatant was filtered through 0.2 μm to remove the vaccinia virus, and 2.5 ml of this filtrate was added to approximately 10 liters of vaccinia virus in a 3.5 cm diameter plate. 6 After 24 h, the supernatant containing recombinant VSV was clarified by centrifugation and stored at -80°C for further use.

[0337] The titers (pfu / ml) of the obtained recombinant VSV supernatants were determined by plaque assay on BSR cells in 6-well plates and counting the plaques in each wheel 24 h after infection using crystal violet staining.

[0338] Then, 3 10 cells were infected at an MOI of 0.1 on a 6 cm diameter cell plate. 6 The harvested recombinant virus was amplified using 100 BSR cells. The new supernatant was titered by plaque assay and stored at -80°C for further use.

[0339] To obtain higher titers, 3 10 cells were infected with 10 000 pfu in a 6 cm diameter plate. 6 BSR cells were added to promote the emergence of mutations that tend to increase the growth rate of the recombinant virus. The viral supernatant was serially passaged 10 times on BSR cells. The titer was again estimated using a plaque assay.

[0340] Titration by plaque assay

[0341] One day in advance 6 BSR cells were seeded in six round plates to ensure a monolayer of approximately 90% confluency the following day. The cells were then infected with 200 μL of a ten-fold serial dilution for 1 hour at room temperature. Following infection, mounting medium was added directly to the inoculum containing 0.8% agarose in the round plates, allowing the mounting medium to cover the cells.

[0342] After adding the overlay, the plates were incubated at 37°C, 5% CO2 for 24 hours. To determine the viral titer, plaques were counted in wells containing 5 to 100 plaques. The viral titer was determined as follows: pfu / ml = (average number of plaques) / (dilution x volume of diluent added to the plate).

[0343] Sequencing of the G gene in viral populations

[0344] 3 10 cells were infected at an MOI of 3 on a 6 cm diameter plate. 6 BSR cells were isolated and total RNA was extracted using TRIzol (Invitrogen). RT-PCR was then performed on the total RNA extract using the primer TTTTTTTTTTTTCAT (SEQ ID NO: 87), which is specific for all viral mRNAs. The VSVG gene was then amplified by PCR, and the resulting PCR product was sequenced to identify compensatory mutations.

[0345] result

[0346] A recombinant VSV virus was constructed in which the gene encoding wild-type glycoprotein G was replaced by the gene encoding GNano (the first chimera, consisting of the signal peptide of VSV Indiana G protein, a diamino acid QF linker, an anti-GFP nanobody with the sequence of SEQ ID NO: 80, a 10-amino acid linker GGGGSGGGGS (SEQ ID NO: 81) and the wild-type VSV Indiana G protein extracellular domain (SEQ ID NO: 2, see Figure 2 However, amplification of this initial recombinant VSV virus was very difficult; only a very low infectious titer of 8.10 was obtained after 24 hours of amplification in BSR cells. 4 Such low titers are incompatible with industrial production of targeted VSV viruses for therapeutic use.

[0347] The recombinant virus was then passaged several times on BSR cells to select mutations that improved its amplification. After 10 passages, genome sequencing of the viral population showed that a variant containing two mutations in the glycoprotein nucleotide sequence gradually invaded the population. The two mutations resulted in:

[0348] The histidine residue at position 22 is changed to asparagine (H22N substitution), and

[0349] The serine residue at position 422 was changed to isoleucine (S422I substitution).

[0350] The titer of the recombinant virus obtained after optimization is about 10 8 pfu / ml.

[0351] The resulting improved chimera (mutated GNano, see Figure 2 Bottom) Shows high amplification in BSR cells after 24 h, compatible with industrial production of targeted VSV virus for therapeutic use.

[0352] 24 hours after infection, the titers obtained in BSR cells are shown in Table 12 below:

[0353] Table 12. Recombinant VSV titers in BSR cells 24 hours after infection.

[0354] Recombinant VSV virus Titer in BSR cells 24 hours after infection (pfu / ml) The first chimera (see Figure 2 upper part) <![CDATA[1.8 10 6 ]]> Mutation chimera (H22N and S422I) <![CDATA[9.10 7 ]]>

[0355] Notably, a third mutation subsequently appeared in approximately 50% of cases in the sequence encoding a dipeptide linker consisting of glutamine and phenylalanine (QF), located between the signal peptide of VSV glycoprotein G and the inserted nanobody. This mutation resulted in a phenylalanine to serine substitution (QF->QS; data not shown).

[0356] Importantly, this third mutation had no effect on kinetics and viral titers (data not shown). In fact, the titer of the recombinant virus with 3 mutations was still ∼10 8 Therefore, the third mutation did not affect the improved amplification of the recombinant virus in BSR cells.

[0357] in conclusion

[0358] Insertion of H22N and S422I mutations in the VSV Indiana glycoprotein G ectodomain surprisingly resulted in a significant increase in the amplification capacity of recombinant VSV viruses containing GFP-targeted glycoprotein G (by insertion of anti-GFP nanobodies).

[0359] Example 2: The S422I mutation in Indiana VSV G was also selected in another context to explain its role.

[0360] In an attempt to identify the histidine that functions as a pH-sensitive molecular switch, we replaced the histidine in the G ectodomain with alanine.

[0361] Specifically, in VSV Indiana G, in the prefusion form of the protomer, there is a cluster of four histidines (H60, H162, H407) ( Figure 5 We hypothesize that protonation of these histidines generates positively charged clusters that induce local repulsive forces and initiate structural transitions.

[0362] Materials and methods

[0363] Plasmids and cloning.

[0364] Point mutations were generated starting from the VSV G gene (Indiana Mudd-Summer strain) cloned from the pCAGGS plasmid. Briefly, the forward and reverse primers containing the desired mutation were each combined with one of the primers flanking the G gene to generate two PCR products. The two G gene fragments overlapped in the region containing the mutation and were assembled into the pCAGGS linearized vector (via EcoRI) using the Gibson Assembly Reaction Kit (New England Biolabs).

[0365] cells and antibodies.

[0366] Clones of BSR and BHK-21 (baby hamster kidney; ATCC CCL-10), and HEK-293T (human embryonic kidney expressing simian virus 40T antigen [SV40T]; ATCC CRL-3216) cells were grown in Dulbecco's modified Eagle's medium (DMEM) supplemented with 8% fetal calf serum (FCS). Mouse monoclonal antibodies against the G extracellular domain were provided by KeraFAST (8G5F11);

[0367] Transfection.

[0368] For fusion assays and indirect immunofluorescence, 70% confluent BSR cells grown in six-well plates were transfected by the calcium phosphate method (5 μg of the appropriate plasmid per well). For pseudovirus production, HEK-293 cells were grown in 10 cm dishes; these cells were transfected with 6 μg of the appropriate plasmid and polyethyleneimine (PEI; Sigma-Aldrich).

[0369] Cell surface expression.

[0370] To quantify cell surface G protein expression, HEK-293 cells plated on six-well culture dishes at 70% confluence were transfected as described above. 24 h after transfection, cells were harvested by scraping into 1 mM EDTA-PBS and then centrifuged at 600 g for 5 min. Cells were incubated with a 1:2000 dilution of a mouse monoclonal anti-G extracellular domain antibody (8G5F11; KeraFAST) in PBS on ice for 1 h. Cells were washed twice in PBS, fixed in paraformaldehyde at 4°C, incubated with a 1:100 dilution of goat anti-mouse AlexaFluor 488 (Invitrogen) on ice for 1 h, and then rinsed in PBS. After resuspending the cells in 500 ml of 0.5 mM EDTA-PBS, the fluorescence of 10,000 cells from each population was determined by flow cytometry using a BD Accuri C6 fluorescence-activated cell sorter (FACS). The mean fluorescence intensity (MFI) of transfected cells expressing G was quantified by flow cytometry. The relative cell surface expression of transfected cells was determined as follows: (MFI of mutant) / (MFI of WT). Figure 6 The percentages given at the bottom are the means of three independent experiments.

[0371] result

[0372] Mutation H407A completely abolishes the G fusion property. This mutation is lethal to the virus. Therefore, the recombinant virus (VSVG H407A) cannot be generated spontaneously. We used a complementation strategy to support its growth.

[0373] Briefly, functional WT VSV G protein was expressed in trans from a transfected plasmid to support the recovery of recombinant VSV. To generate viral particles containing only fusion-defective VSV G expressed from the viral genome, virus present in the supernatant was amplified in cells lacking the transcomplementing VSV G plasmid. Sequence analysis of independent clones revealed two different compensatory mutations: one of which resulted in the substitution of serine 422 with isoleucine (resulting in the double mutant VSV G H407A S422I).

[0374] in conclusion

[0375] Comparison of the characteristics of VSV G H407A and VSV G H407A / S422I revealed that, in the context of the H407A mutation, S422I enhanced the efficiency of VSV G transport and G recognition by the soluble form of the LDL-R CR2 domain ( Figure 6This strongly suggests that, in the context of the H407A mutation, the S422I mutation (or similar substitutions such as S422F, S422M, S422L, or S422V, or equivalent substitutions at equivalent positions in the G ectodomain of other VSV strains) promotes G folding and stabilizes the prefusion form (because the structural shift disrupts the CR domain binding site).

[0376] Example 3: Cell-Cell Fusion Assay Comparison of the Fusion Properties of VSV Indiana WT G Glycoprotein and VSV Indiana GNano Optimized Glycoprotein.

[0377] Materials and methods

[0378] Cell-cell fusion assay.

[0379] BSR cells at 70% confluence plated on glass coverslips were co-transfected with pCAGGS plasmids encoding wild-type (WT) G or mutant G and P-GFP plasmids encoding rabies virus phosphoprotein fused to GFP (cytoplasmic marker). 24 hours after transfection, cells were incubated with fusion buffer (DMEM + 10mM MES) at different pH values ​​(5.0 to 6.5) at 37°C for 10 minutes. The cells were then washed once and incubated with DMEM + 10mM HEPES-NaOH buffered with pH 7.4 and 1% BSA at 37°C for 1 hour. The cells were fixed with 4% paraformaldehyde in 1× PBS for 15 minutes. The nuclei were stained with DAPI, and the formation of syncytia was analyzed using a Zeiss Axiovert 200 fluorescence microscope and a 20x microscope.

[0380] result

[0381] The fusion properties of optimized VSV G Indiana WT and VSV GNano (i.e., H22 residue mutated to N, S422 residue mutated to I, F, M, L, or V) were analyzed in a cell-cell fusion assay. To this end, BSR cells were transfected with pCAGGS plasmids expressing VSV G (WT or mutant) and P-GFP (a protein present only in the cytoplasm, allowing easy observation of syncytia). 24 h after transfection, cells were exposed to DMEM adjusted to the specified pH for 10 min, and then the DMEM was replaced with DMEM at pH 7.4. The cells were fixed after being maintained at 37°C for 1 h.

[0382] When exposed to low pH between 5.5 and 6.3, cells expressing wild-type G protein formed numerous syncytia ( Figure 7 When exposed to low pH, cells expressing the optimized GNano were able to form syncytia ( Figure 7 ).

[0383] in conclusion

[0384] The results are consistent with the fact that the presence of the hydrophobic residue at position 422 is key to mediating the pH-dependent structural transition. This strongly suggests that the S422I mutation (or S422F, S422M, S422L or S422V, or equivalent substitutions at equivalent positions in the G ectodomain of other VSV strains) promotes the G fold and stabilizes the prefusion form of GNano.

[0385] Example 4: The VSV G C-terminal portion helps lock the ectodomain in its pre-fusion state.

[0386] result

[0387] by The WT Indiana VSV G extracellular domain (G 1-440 , containing residues 1 to 440). The extracellular domain was crystallized in its pre-trimeric conformation. The structure was determined at a resolution of Figure 8 ). The polypeptide chain was traced to residue 432. G 1-440 The C-terminal portion of the VSV G fusion domain consists of an α-helix (residues 409 to 416), followed by a kinked region ending in a β-turn between Pro 418 and Glu 421, and a short β-hairpin (residues 422 to 432). This hairpin interacts with strands 79-84 of the VSV G fusion domain β-sheet through hydrogen bonds between the main chains of the two segments and between the side chains of residues H80 and E421.

[0388] in conclusion

[0389] This X-ray structure of the VSV G ectodomain reveals that the C-terminal portion (residues 407 to 425) interacts significantly with the fusion domain, thereby contributing to the stabilization of the prefusion complex. Of particular relevance to the present invention is the fact that, in this prefusion structure, residue S422 points toward residues F424 and L430. Therefore, the compensatory mutation S422I stabilizes the β-hairpin structure (and thus the prefusion state) through hydrophobic interactions between residues I422 and residues F424 and L430. This also explains why replacing S422 with other hydrophobic residues (L, M, V, or F) has the same effect (i.e., stabilizing the prefusion conformation).

[0390] bibliography

[0391] Albertini et al., Viruses 4, 117–139 (2012).

[0392] Amirache. Blood 123,1422–4(2014).

[0393] Barber. Oncogene 24,7710–7719(2005).

[0394] Bishnoi et al., Viruses 10, 90 (2018).

[0395] Fernandez et al., J. Virol. 76, 895–904 (2002).

[0396] Hastie et al., Virus Res. 176, 16–32 (2013).

[0397] Needleman and Wunsch. J. Mol. Biol. 48, 443–453, 1970.

[0398] Nikolic et al., Nat Commun. 2018 Mar 12;9(1):1029.

[0399] Rodriguez et al., J Gen Virol. 2002 Oct;83(Pt 10):2475-83.

[0400] Schnell et al., J. virol. 1996 70:2318–2323.

[0401] Velazquez-Salinas et al., Genome Announc. 2017 Sep 14; 5(37). 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Val Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 145 150 155 160 Asp Ser Gln Phe Ile Asn Gly Lys Cys Ser Asn Tyr Ile Cys Pro Thr 165 170 175 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Lys Gly Leu 180 185 190 Cys Asp Ser Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 195 200 205 Gly Glu Leu Ser Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 210 215 220 Tyr Phe Ala Tyr Glu Thr Gly Gly Lys Ala Cys Lys Met Gln Tyr Cys 225 230 235 240 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 245 250 255 Asp Lys Asp Leu Phe Ala Ala Ala Arg Phe Pro Glu Cys Pro Glu Gly 260 265 270 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 275 280 285 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 290 295 300 Ser Lys Ile Arg Ala Gly Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 305 310 315 320 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 325 330 335 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 340 345 350 Ala Pro Ile Leu Ser Arg Met Val Gly Met Ile Ser Gly Thr Thr Thr 355 360 365 Glu Arg Glu Leu Trp Asp Asp Trp Ala Pro Tyr Glu Asp Val Glu Ile 370 375 380 Gly Pro Asn Gly Val Leu Arg Thr Ser Ser Gly Tyr Lys Phe Pro Leu 385 390 395 400 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Leu Ser Ser 405 410 415 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 420 425 430 Leu Pro Asp Asp Glu Ser Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 435 440 445 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Ser 450 455 460 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Ile Ile Gly Leu Phe Leu 465 470 475 480 Val Leu Arg Val Gly Ile His Leu Cys Ile Lys Leu Lys His Thr Lys 485 490 495 Lys Arg Gln Ile Tyr Thr Asp Ile Glu Met Asn Arg Leu Gly Lys 500 505 510 <210> 2 <211> 495 <212> PRT <213> Vesicular stomatitis Indiana virus <400> 2 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Asn Tyr His Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Asp Leu Ile Gly Thr Ala Ile Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ser Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr Gln 65 70 75 80 Ser Ile Arg Ser Phe Thr Pro Ser Val Glu Gln Cys Lys Glu Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Ala Val Ile Val Gln 115 120 125 Val Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Ile Asn Gly Lys Cys Ser Asn Tyr Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Lys Gly Leu 165 170 175 Cys Asp Ser Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Glu Leu Ser Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Thr Gly Gly Lys Ala Cys Lys Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Leu Phe Ala Ala Ala Arg Phe Pro Glu Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Gly Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Ala Pro Ile Leu Ser Arg Met Val Gly Met Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asp Asp Trp Ala Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Arg Thr Ser Ser Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Leu Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Ser Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Ser 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Ile Ile Gly Leu Phe Leu 450 455 460 Val Leu Arg Val Gly Ile His Leu Cys Ile Lys Leu Lys His Thr Lys 465 470 475 480 Lys Arg Gln Ile Tyr Thr Asp Ile Glu Met Asn Arg Leu Gly Lys 485 490 495 <210> 3 <211> 512 <212> PRT <213> Maraba virus <400> 3 Met Leu Arg Leu Phe Leu Phe Cys Phe Leu Ala Leu Gly Ala His Ser 1 5 10 15 Lys Phe Thr Ile Val Phe Pro His His Gln Lys Gly Asn Trp Lys Asn 20 25 30 Val Pro Ser Thr Tyr His Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 35 40 45 His Asn Asp Leu Thr Gly Val Ser Leu His Val Lys Ile Pro Lys Ser 50 55 60 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 65 70 75 80 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 85 90 95 Ser Ile His Ser Met Ser Pro Thr Leu Glu Gln Cys Lys Thr Ser Ile 100 105 110 Glu Gln Thr Lys Gln Gly Val Trp Ile Asn Pro Gly Phe Pro Pro Gln 115 120 125 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Val Val Val Val Gln 130 135 140 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 145 150 155 160 Asp Ser Gln Leu Val Gly Gly Lys Cys Ser Lys Glu Val Cys Gln Thr 165 170 175 Val His Asn Ser Thr Val Trp His Ala Asp Tyr Lys Ile Thr Gly Leu 180 185 190 Cys Glu Ser Asn Leu Ala Ser Val Asp Ile Thr Phe Phe Ser Glu Asp 195 200 205 Gly Gln Lys Thr Ser Leu Gly Lys Pro Asn Thr Gly Phe Arg Ser Asn 210 215 220 His Phe Ala Tyr Glu Ser Gly Glu Lys Ala Cys Arg Met Gln Tyr Cys 225 230 235 240 Thr Gln Trp Gly Ile Arg Leu Pro Ser Gly Val Trp Phe Glu Leu Val 245 250 255 Asp Lys Asp Leu Phe Gln Ala Ala Lys Leu Pro Glu Cys Pro Arg Gly 260 265 270 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 275 280 285 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 290 295 300 Ser Lys Ile Arg Ala Lys Leu Pro Val Ser Pro Val Asp Leu Ser Tyr 305 310 315 320 Leu Ala Pro Lys Asn Pro Gly Ser Gly Pro Ala Phe Thr Ile Ile Asn 325 330 335 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ser 340 345 350 Asn Pro Ile Ile Pro His Met Val Gly Thr Met Ser Gly Thr Thr Thr 355 360 365 Glu Arg Glu Leu Trp Asn Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 370 375 380 Gly Pro Asn Gly Val Leu Lys Thr Pro Thr Gly Phe Lys Phe Pro Leu 385 390 395 400 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Ser Ser 405 410 415 Gln Ala Gln Val Phe Glu His Pro His Ala Lys Asp Ala Ala Ser Gln 420 425 430 Leu Pro Asp Asp Glu Thr Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 435 440 445 Asn Pro Val Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 450 455 460 Leu Ala Ser Phe Phe Leu Ile Ile Gly Leu Gly Val Ala Leu Ile Phe 465 470 475 480 Ile Ile Arg Ile Ile Val Ala Ile Arg Tyr Lys Tyr Lys Gly Arg Lys 485 490 495 Thr Gln Lys Ile Tyr Asn Asp Val Glu Met Ser Arg Leu Gly Asn Lys 500 505 510 <210> 4 <211> 496 <212> PRT <213> Maraba virus of vesicular stomatitis <400> 4 Lys Phe Thr Ile Val Phe Pro His His Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Thr Tyr His Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Thr Gly Val Ser Leu His Val Lys Ile Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Met Ser Pro Thr Leu Glu Gln Cys Lys Thr Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Val Trp Ile Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Val Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Leu Val Gly Gly Lys Cys Ser Lys Glu Val Cys Gln Thr 145 150 155 160 Val His Asn Ser Thr Val Trp His Ala Asp Tyr Lys Ile Thr Gly Leu 165 170 175 Cys Glu Ser Asn Leu Ala Ser Val Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Gln Lys Thr Ser Leu Gly Lys Pro Asn Thr Gly Phe Arg Ser Asn 195 200 205 His Phe Ala Tyr Glu Ser Gly Glu Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Thr Gln Trp Gly Ile Arg Leu Pro Ser Gly Val Trp Phe Glu Leu Val 225 230 235 240 Asp Lys Asp Leu Phe Gln Ala Ala Lys Leu Pro Glu Cys Pro Arg Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Lys Leu Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Ser Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ser 325 330 335 Asn Pro Ile Ile Pro His Met Val Gly Thr Met Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asn Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Pro Thr Gly Phe Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Ser Ser 385 390 395 400 Gln Ala Gln Val Phe Glu His Pro His Ala Lys Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Thr Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Val Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Leu Ala Ser Phe Phe Leu Ile Ile Gly Leu Gly Val Ala Leu Ile Phe 450 455 460 Ile Ile Arg Ile Ile Val Ala Ile Arg Tyr Lys Tyr Lys Gly Arg Lys 465 470 475 480 Thr Gln Lys Ile Tyr Asn Asp Val Glu Met Ser Arg Leu Gly Asn Lys 485 490 495 <210> 5 <211> 512 <212> PRT <213> Vesicular stomatitis Cocal virus <400> 5 Met Asn Phe Leu Leu Leu Thr Phe Ile Val Leu Pro Leu Cys Ser His 1 5 10 15 Ala Lys Phe Ser Ile Val Phe Pro Gln Ser Gln Lys Gly Asn Trp Lys 20 25 30 Asn Val Pro Ser Ser Tyr His Tyr Cys Pro Ser Ser Ser Asp Gln Asn 35 40 45 Trp His Asn Asp Leu Leu Gly Ile Thr Met Lys Val Lys Met Pro Lys 50 55 60 Thr His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys 65 70 75 80 Trp Ile Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr 85 90 95 His Ser Ile His Ser Ile Gln Pro Thr Ser Glu Gln Cys Lys Glu Ser 100 105 110 Ile Lys Gln Thr Lys Gln Gly Thr Trp Met Ser Pro Gly Phe Pro Pro 115 120 125 Gln Asn Cys Gly Tyr Ala Thr Val Thr Asp Ser Val Ala Val Val Val 130 135 140 Gln Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp 145 150 155 160 Ile Asp Ser Gln Phe Pro Asn Gly Lys Cys Glu Thr Glu Glu Cys Glu 165 170 175 Thr Val His Asn Ser Thr Val Trp Tyr Ser Asp Tyr Lys Val Thr Gly 180 185 190 Leu Cys Asp Ala Thr Leu Val Asp Thr Glu Ile Thr Phe Phe Ser Glu 195 200 205 Asp Gly Lys Lys Glu Ser Ile Gly Lys Pro Asn Thr Gly Tyr Arg Ser 210 215 220 Asn Tyr Phe Ala Tyr Glu Lys Gly Asp Lys Val Cys Lys Met Asn Tyr 225 230 235 240 Cys Lys His Ala Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Phe 245 250 255 Val Asp Gln Asp Val Tyr Ala Ala Ala Lys Leu Pro Glu Cys Pro Val 260 265 270 Gly Ala Thr Ile Ser Ala Pro Thr Gln Thr Ser Val Asp Val Ser Leu 275 280 285 Ile Leu Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr 290 295 300 Trp Ser Lys Ile Arg Ser Lys Gln Pro Val Ser Pro Val Asp Leu Ser 305 310 315 320 Tyr Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile 325 330 335 Asn Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Ile Asp Ile 340 345 350 Asp Asn Pro Ile Ile Ser Lys Met Val Gly Lys Ile Ser Gly Ser Gln 355 360 365 Thr Glu Arg Glu Leu Trp Thr Glu Trp Phe Pro Tyr Glu Gly Val Glu 370 375 380 Ile Gly Pro Asn Gly Ile Leu Lys Thr Pro Thr Gly Tyr Lys Phe Pro 385 390 395 400 Leu Phe Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Thr 405 410 415 Ser Gln Ala Glu Val Phe Glu His Pro His Leu Ala Glu Ala Pro Lys 420 425 430 Gln Leu Pro Glu Glu Glu Thr Leu Phe Phe Gly Asp Thr Gly Ile Ser 435 440 445 Lys Asn Pro Val Glu Leu Ile Glu Gly Trp Phe Ser Ser Trp Lys Ser 450 455 460 Thr Val Val Thr Phe Phe Phe Ala Ile Gly Val Phe Ile Leu Leu Tyr 465 470 475 480 Val Val Ala Arg Ile Val Ile Ala Val Arg Tyr Arg Tyr Gln Gly Ser 485 490 495 Asn Asn Lys Arg Ile Tyr Asn Asp Ile Glu Met Ser Arg Phe Arg Lys 500 505 510 <210> 6 <211> 495 <212> PRT <213> Cocal virus <400> 6 Light Phe Ser Ile Val Phe Pro Gln Ser Gln Light Gly Asn Trp Light Asn 1 5 10 15 Val Pro Ser Ser Tyr His Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Leu Gly Ile Thr Met Lys Val Lys Met Pro Lys Thr 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Ile Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Ile Gln Pro Thr Ser Glu Gln Cys Lys Glu Ser Ile 85 90 95 Lys Gln Thr Lys Gln Gly Thr Trp Met Ser Pro Gly Phe Pro Pro Gln 100 105 110 Asn Cys Gly Tyr Ala Thr Val Thr Asp Ser Val Ala Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Phe Pro Asn Gly Lys Cys Glu Thr Glu Glu Cys Glu Thr 145 150 155 160 Val His Asn Ser Thr Val Trp Tyr Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Thr Leu Val Asp Thr Glu Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Lys Glu Ser Ile Gly Lys Pro Asn Thr Gly Tyr Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Lys Gly Asp Lys Val Cys Lys Met Asn Tyr Cys 210 215 220 Lys His Ala Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Phe Val 225 230 235 240 Asp Gln Asp Val Tyr Ala Ala Ala Lys Leu Pro Glu Cys Pro Val Gly 245 250 255 Ala Thr Ile Ser Ala Pro Thr Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Leu Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ser Lys Gln Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Ile Asp Ile Asp 325 330 335 Asn Pro Ile Ile Ser Lys Met Val Gly Lys Ile Ser Gly Ser Gln Thr 340 345 350 Glu Arg Glu Leu Trp Thr Glu Trp Phe Pro Tyr Glu Gly Val Glu Ile 355 360 365 Gly Pro Asn Gly Ile Leu Lys Thr Pro Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Phe Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Thr Ser 385 390 395 400 Gln Ala Glu Val Phe Glu His Pro His Leu Ala Glu Ala Pro Lys Gln 405 410 415 Leu Pro Glu Glu Glu Thr Leu Phe Phe Gly Asp Thr Gly Ile Ser Lys 420 425 430 Asn Pro Val Glu Leu Ile Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Val Val Thr Phe Phe Phe Ala Ile Gly Val Phe Ile Leu Leu Tyr Val 450 455 460 Val Ala Arg Ile Val Ile Ala Val Arg Tyr Arg Tyr Gln Gly Ser Asn 465 470 475 480 Asn Lys Arg Ile Tyr Asn Asp Ile Glu Met Ser Arg Phe Arg Lys 485 490 495 <210> 7 <211> 513 <212> PRT <213> Morreton virus <400> 7 Met Leu Val Leu Tyr Leu Leu Leu Ser Leu Leu Leu Ala Leu Gly Ala Gln 1 5 10 15 Cys Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys 20 25 30 Asn Val Pro Ala Asn Tyr Gln Tyr Cys Pro Ser Ser Ser Asp Leu Asn 35 40 45 Trp His Asn Gly Leu Ile Gly Thr Ser Leu Gln Val Lys Met Pro Lys 50 55 60 Ser His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys 65 70 75 80 Trp Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Val Thr 85 90 95 His Ser Ile Lys Ser Met Ile Pro Thr Val Asp Gln Cys Lys Glu Ser 100 105 110 Ile Ala Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro 115 120 125 Gln Ser Cys Gly Tyr Ala Ser Val Thr Asp Ala Glu Ala Val Ile Val 130 135 140 Lys Ala Thr Pro His Gln Val Leu Val Asp Glu Tyr Thr Gly Glu Trp 145 150 155 160 Val Asp Ser Gln Phe Pro Thr Gly Lys Cys Asn Lys Asp Ile Cys Pro 165 170 175 Thr Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Thr Gly 180 185 190 Leu Cys Asp Ala Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu 195 200 205 Asp Gly Lys Leu Thr Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser 210 215 220 Asn Tyr Phe Ala Tyr Glu Asn Gly Asp Lys Ala Cys Arg Met Gln Tyr 225 230 235 240 Cys Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met 245 250 255 Ala Asp Lys Asp Ile Tyr Asn Asp Ala Lys Phe Pro Asp Cys Pro Glu 260 265 270 Gly Ser Ser Ile Ala Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu 275 280 285 Ile Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr 290 295 300 Trp Ser Lys Ile Arg Ala His Leu Pro Ile Ser Pro Val Asp Leu Ser 305 310 315 320 Tyr Leu Ser Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile 325 330 335 Asn Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile 340 345 350 Ala Gly Pro Ile Ile Pro Gln Met Arg Gly Val Ile Ser Gly Thr Thr 355 360 365 Thr Glu Arg Glu Leu Trp Thr Asp Trp Tyr Pro Tyr Glu Asp Val Glu 370 375 380 Ile Gly Pro Asn Gly Val Leu Lys Thr Ala Thr Gly Tyr Lys Phe Pro 385 390 395 400 Leu Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Ile Ser 405 410 415 Ser Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser 420 425 430 Gln Leu Pro Asp Asp Glu Thr Leu Phe Phe Gly Asp Thr Gly Leu Ser 435 440 445 Lys Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Gly Trp Lys Ser 450 455 460 Thr Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Val Ile Gly Leu Tyr 465 470 475 480 Leu Val Leu Arg Ile Gly Ile Ala Leu Cys Ile Lys Cys Arg Val Gln 485 490 495 Glu Lys Arg Pro Lys Ile Tyr Thr Asp Val Glu Met Asn Arg Leu Asp 500 505 510 Arg <210> 8 <211> 496 <212> PRT <213> Vesicular stomatitis Morreton virus <400> 8 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ala Asn Tyr Gln Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Gly Leu Ile Gly Thr Ser Leu Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Val Thr His 65 70 75 80 Ser Ile Lys Ser Met Ile Pro Thr Val Asp Gln Cys Lys Glu Ser Ile 85 90 95 Ala Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Ser Val Thr Asp Ala Glu Ala Val Ile Val Lys 115 120 125 Ala Thr Pro His Gln Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Pro Thr Gly Lys Cys Asn Lys Asp Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Leu Thr Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Asn Gly Asp Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Ile Tyr Asn Asp Ala Lys Phe Pro Asp Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ala Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala His Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ser Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Gly Pro Ile Ile Pro Gln Met Arg Gly Val Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Thr Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Ala Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Ile Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Thr Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Gly Trp Lys Ser Thr 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Val Ile Gly Leu Tyr Leu 450 455 460 Val Leu Arg Ile Gly Ile Ala Leu Cys Ile Lys Cys Arg Val Gln Glu 465 470 475 480 Lys Arg Pro Lys Ile Tyr Thr Asp Val Glu Met Asn Arg Leu Asp Arg 485 490 495 <210> 9 <211> 511 <212> PRT <213> Vesicular stomatitis Alagoa virus <400> 9 Met Thr Pro Ala Phe Ile Leu Cys Met Leu Leu Ala Gly Ser Ser Trp 1 5 10 15 Ala Lys Phe Thr Ile Val Phe Pro Gln Ser Gln Lys Gly Asp Trp Lys 20 25 30 Asp Val Pro Pro Asn Tyr Arg Tyr Cys Pro Ser Ser Ala Asp Gln Asn 35 40 45 Trp His Gly Asp Leu Leu Gly Val Asn Ile Arg Ala Lys Met Pro Lys 50 55 60 Val His Lys Ala Ile Lys Ala Asp Gly Trp Met Cys His Ala Ala Lys 65 70 75 80 Trp Val Thr Thr Cys Asp Tyr Arg Trp Tyr Gly Pro Gln Tyr Ile Thr 85 90 95 His Ser Ile His Ser Phe Ile Pro Thr Lys Ala Gln Cys Glu Glu Ser 100 105 110 Ile Lys Gln Thr Lys Glu Gly Val Trp Ile Asn Pro Gly Phe Pro Pro 115 120 125 Lys Asn Cys Gly Tyr Ala Ser Val Ser Asp Ala Glu Ser Ile Ile Val 130 135 140 Gln Ala Thr Ala His Ser Val Met Ile Asp Glu Tyr Ser Gly Asp Trp 145 150 155 160 Leu Asp Ser Gln Phe Pro Thr Gly Arg Cys Thr Gly Ser Thr Cys Glu 165 170 175 Thr Ile His Asn Ser Thr Leu Trp Tyr Ala Asp Tyr Gln Val Thr Gly 180 185 190 Leu Cys Asp Ser Ala Leu Val Ser Thr Glu Val Thr Phe Tyr Ser Glu 195 200 205 Asp Gly Leu Met Thr Ser Ile Gly Arg Gln Asn Thr Gly Tyr Arg Ser 210 215 220 Asn Tyr Phe Pro Tyr Glu Lys Gly Ala Ala Ala Cys Arg Met Lys Tyr 225 230 235 240 Cys Thr His Glu Gly Ile Arg Leu Pro Ser Gly Val Trp Phe Glu Met 245 250 255 Val Asp Lys Glu Leu Leu Glu Ser Val Gln Met Pro Glu Cys Pro Ala 260 265 270 Gly Leu Thr Ile Ser Ala Pro Thr Gln Thr Ser Val Asp Val Ser Leu 275 280 285 Ile Leu Asp Val Glu Arg Met Leu Asp Tyr Ser Leu Cys Gln Glu Thr 290 295 300 Trp Ser Lys Val His Ser Gly Leu Pro Ile Ser Pro Val Asp Leu Gly 305 310 315 320 Tyr Ile Ala Pro Lys Asn Pro Gly Ala Gly Pro Ala Phe Thr Ile Val 325 330 335 Asn Gly Thr Leu Lys Tyr Phe Asp Thr Arg Tyr Leu Arg Ile Asp Ile 340 345 350 Glu Gly Pro Val Leu Lys Lys Met Thr Gly Lys Val Ser Gly Thr Pro 355 360 365 Thr Lys Arg Glu Leu Trp Thr Glu Trp Phe Pro Tyr Asp Asp Val Glu 370 375 380 Ile Gly Pro Asn Gly Val Leu Lys Thr Pro Glu Gly Tyr Lys Phe Pro 385 390 395 400 Leu Tyr Met Ile Gly His Gly Leu Leu Asp Ser Asp Leu Gln Lys Thr 405 410 415 Ser Gln Ala Glu Val Phe His His Pro Gln Ile Ala Glu Ala Val Gln 420 425 430 Lys Leu Pro Asp Asp Glu Thr Leu Phe Phe Gly Asp Thr Gly Ile Ser 435 440 445 Lys Asn Pro Val Glu Val Ile Glu Gly Trp Phe Ser Asn Trp Arg Ser 450 455 460 Ser Val Met Ala Ile Val Phe Ala Ile Leu Leu Leu Val Ile Thr Val 465 470 475 480 Leu Met Val Arg Leu Cys Val Ala Phe Arg His Phe Cys Cys Gln Lys 485 490 495 Arg His Lys Ile Tyr Asn Asp Leu Glu Met Asn Gln Leu Arg Arg 500 505 510 <210> 10 <211> 494 <212> PRT <213> Vesicular stomatitis Alagoa virus <400> 10 Lys Phe Thr Ile Val Phe Pro Gln Ser Gln Lys Gly Asp Trp Lys Asp 1 5 10 15 Val Pro Pro Asn Tyr Arg Tyr Cys Pro Ser Ser Ala Asp Gln Asn Trp 20 25 30 His Gly Asp Leu Leu Gly Val Asn Ile Arg Ala Lys Met Pro Lys Val 35 40 45 His Lys Ala Ile Lys Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Tyr Arg Trp Tyr Gly Pro Gln Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Phe Ile Pro Thr Lys Ala Gln Cys Glu Glu Ser Ile 85 90 95 Lys Gln Thr Lys Glu Gly Val Trp Ile Asn Pro Gly Phe Pro Pro Lys 100 105 110 Asn Cys Gly Tyr Ala Ser Val Ser Asp Ala Glu Ser Ile Ile Val Gln 115 120 125 Ala Thr Ala His Ser Val Met Ile Asp Glu Tyr Ser Gly Asp Trp Leu 130 135 140 Asp Ser Gln Phe Pro Thr Gly Arg Cys Thr Gly Ser Thr Cys Glu Thr 145 150 155 160 Ile His Asn Ser Thr Leu Trp Tyr Ala Asp Tyr Gln Val Thr Gly Leu 165 170 175 Cys Asp Ser Ala Leu Val Ser Thr Glu Val Thr Phe Tyr Ser Glu Asp 180 185 190 Gly Leu Met Thr Ser Ile Gly Arg Gln Asn Thr Gly Tyr Arg Ser Asn 195 200 205 Tyr Phe Pro Tyr Glu Lys Gly Ala Ala Ala Cys Arg Met Lys Tyr Cys 210 215 220 Thr His Glu Gly Ile Arg Leu Pro Ser Gly Val Trp Phe Glu Met Val 225 230 235 240 Asp Lys Glu Leu Leu Glu Ser Val Gln Met Pro Glu Cys Pro Ala Gly 245 250 255 Leu Thr Ile Ser Ala Pro Thr Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Leu Asp Val Glu Arg Met Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Val His Ser Gly Leu Pro Ile Ser Pro Val Asp Leu Gly Tyr 290 295 300 Ile Ala Pro Lys Asn Pro Gly Ala Gly Pro Ala Phe Thr Ile Val Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Asp Thr Arg Tyr Leu Arg Ile Asp Ile Glu 325 330 335 Gly Pro Val Leu Lys Lys Met Thr Gly Lys Val Ser Gly Thr Pro Thr 340 345 350 Lys Arg Glu Leu Trp Thr Glu Trp Phe Pro Tyr Asp Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Pro Glu Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Leu Leu Asp Ser Asp Leu Gln Lys Thr Ser 385 390 395 400 Gln Ala Glu Val Phe His His Pro Gln Ile Ala Glu Ala Val Gln Lys 405 410 415 Leu Pro Asp Asp Glu Thr Leu Phe Phe Gly Asp Thr Gly Ile Ser Lys 420 425 430 Asn Pro Val Glu Val Ile Glu Gly Trp Phe Ser Asn Trp Arg Ser Ser 435 440 445 Val Met Ala Ile Val Phe Ala Ile Leu Leu Leu Val Ile Thr Val Leu 450 455 460 Met Val Arg Leu Cys Val Ala Phe Arg His Phe Cys Cys Gln Lys Arg 465 470 475 480 His Lys Ile Tyr Asn Asp Leu Glu Met Asn Gln Leu Arg Arg 485 490 <210> 11 <211> 517 <212> PRT <213> Vesicular stomatitis New Jersey virus <400> 11 Met Leu Ser Tyr Leu Ile Phe Ala Leu Val Val Ser Pro Ile Leu Gly 1 5 10 15 Lys Ile Glu Ile Val Phe Pro Gln His Thr Thr Gly Asp Trp Lys Arg 20 25 30 Val Pro His Glu Tyr Asn Tyr Cys Pro Thr Ser Ala Asp Lys Asn Ser 35 40 45 His Gly Thr Gln Thr Gly Ile Pro Val Glu Leu Thr Met Pro Lys Gly 50 55 60 Leu Thr Thr His Gln Val Asp Gly Phe Met Cys His Ser Ala Leu Trp 65 70 75 80 Met Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 85 90 95 Ser Ile His Asn Glu Glu Pro Thr Asp Tyr Gln Cys Leu Glu Ala Ile 100 105 110 Lys Ala Tyr Lys Asp Gly Val Ser Phe Asn Pro Gly Phe Pro Pro Gln 115 120 125 Ser Cys Gly Tyr Gly Thr Val Thr Asp Ala Glu Ala His Ile Val Thr 130 135 140 Val Thr Pro His Ser Val Lys Val Asp Glu Tyr Thr Gly Glu Trp Ile 145 150 155 160 Asp Pro His Phe Ile Gly Gly Arg Cys Lys Gly Gln Ile Cys Glu Thr 165 170 175 Val His Asn Ser Thr Lys Trp Phe Thr Ser Ser Asp Gly Glu Ser Val 180 185 190 Cys Ser Gln Leu Phe Thr Leu Val Gly Gly Thr Phe Phe Ser Asp Ser 195 200 205 Glu Glu Ile Thr Ser Met Gly Leu Pro Glu Thr Gly Ile Arg Ser Asn 210 215 220 Tyr Phe Pro Tyr Val Ser Thr Glu Gly Ile Cys Lys Met Pro Phe Cys 225 230 235 240 Arg Lys Pro Gly Tyr Lys Leu Lys Asn Asp Leu Trp Phe Gln Ile Thr 245 250 255 Asp Pro Asp Leu Asp Lys Thr Val Arg Asp Leu Pro His Ile Lys Asp 260 265 270 Cys Asp Leu Ser Ser Ser Ile Val Thr Pro Gly Glu His Ala Thr Asp 275 280 285 Ile Ser Leu Ile Ser Asp Val Glu Arg Ile Leu Asp Tyr Ala Leu Cys 290 295 300 Gln Asn Thr Trp Ser Lys Ile Glu Ala Gly Glu Pro Ile Thr Pro Val 305 310 315 320 Asp Leu Ser Tyr Leu Gly Pro Lys Asn Pro Gly Ala Gly Pro Val Phe 325 330 335 Thr Ile Ile Asn Gly Ser Leu His Tyr Phe Met Ser Lys Tyr Leu Arg 340 345 350 Val Glu Leu Glu Ser Pro Val Ile Pro Arg Met Glu Gly Lys Val Ala 355 360 365 Gly Thr Arg Ile Val Arg Gln Leu Trp Asp Gln Trp Phe Pro Phe Gly 370 375 380 Glu Val Glu Ile Gly Pro Asn Gly Val Leu Lys Thr Lys Gln Gly Tyr 385 390 395 400 Lys Phe Pro Leu His Ile Ile Gly Thr Gly Glu Val Asp Asn Asp Ile 405 410 415 Lys Met Glu Arg Ile Val Lys His Trp Glu His Pro His Ile Glu Ala 420 425 430 Ala Gln Thr Phe Leu Lys Lys Asp Asp Thr Glu Glu Val Leu Tyr Tyr 435 440 445 Gly Asp Thr Gly Val Ser Lys Asn Pro Val Glu Leu Val Glu Gly Trp 450 455 460 Phe Ser Gly Trp Arg Ser Ser Ile Met Gly Val Leu Ala Val Ile Ile 465 470 475 480 Gly Phe Val Ile Leu Ile Phe Leu Ile Arg Leu Ile Gly Val Leu Ser 485 490 495 Ser Leu Phe Arg Gln Lys Arg Arg Pro Ile Tyr Lys Ser Asp Val Glu 500 505 510 Met Ala His Phe Arg 515 <210> 12 <211> 501 <212> PRT <213> Vesicular stomatitis New Jersey virus <400> 12 Lys Ile Glu Ile Val Phe Pro Gln His Thr Thr Gly Asp Trp Lys Arg 1 5 10 15 Val Pro His Glu Tyr Asn Tyr Cys Pro Thr Ser Ala Asp Lys Asn Ser 20 25 30 His Gly Thr Gln Thr Gly Ile Pro Val Glu Leu Thr Met Pro Lys Gly 35 40 45 Leu Thr Thr His Gln Val Asp Gly Phe Met Cys His Ser Ala Leu Trp 50 55 60 Met Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Asn Glu Glu Pro Thr Asp Tyr Gln Cys Leu Glu Ala Ile 85 90 95 Lys Ala Tyr Lys Asp Gly Val Ser Phe Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Gly Thr Val Thr Asp Ala Glu Ala His Ile Val Thr 115 120 125 Val Thr Pro His Ser Val Lys Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Pro His Phe Ile Gly Gly Arg Cys Lys Gly Gln Ile Cys Glu Thr 145 150 155 160 Val His Asn Ser Thr Lys Trp Phe Thr Ser Ser Asp Gly Glu Ser Val 165 170 175 Cys Ser Gln Leu Phe Thr Leu Val Gly Gly Thr Phe Phe Ser Asp Ser 180 185 190 Glu Glu Ile Thr Ser Met Gly Leu Pro Glu Thr Gly Ile Arg Ser Asn 195 200 205 Tyr Phe Pro Tyr Val Ser Thr Glu Gly Ile Cys Lys Met Pro Phe Cys 210 215 220 Arg Lys Pro Gly Tyr Lys Leu Lys Asn Asp Leu Trp Phe Gln Ile Thr 225 230 235 240 Asp Pro Asp Leu Asp Lys Thr Val Arg Asp Leu Pro His Ile Lys Asp 245 250 255 Cys Asp Leu Ser Ser Ser Ile Val Thr Pro Gly Glu His Ala Thr Asp 260 265 270 Ile Ser Leu Ile Ser Asp Val Glu Arg Ile Leu Asp Tyr Ala Leu Cys 275 280 285 Gln Asn Thr Trp Ser Lys Ile Glu Ala Gly Glu Pro Ile Thr Pro Val 290 295 300 Asp Leu Ser Tyr Leu Gly Pro Lys Asn Pro Gly Ala Gly Pro Val Phe 305 310 315 320 Thr Ile Ile Asn Gly Ser Leu His Tyr Phe Met Ser Lys Tyr Leu Arg 325 330 335 Val Glu Leu Glu Ser Pro Val Ile Pro Arg Met Glu Gly Lys Val Ala 340 345 350 Gly Thr Arg Ile Val Arg Gln Leu Trp Asp Gln Trp Phe Pro Phe Gly 355 360 365 Glu Val Glu Ile Gly Pro Asn Gly Val Leu Lys Thr Lys Gln Gly Tyr 370 375 380 Lys Phe Pro Leu His Ile Ile Gly Thr Gly Glu Val Asp Asn Asp Ile 385 390 395 400 Lys Met Glu Arg Ile Val Lys His Trp Glu His Pro His Ile Glu Ala 405 410 415 Ala Gln Thr Phe Leu Lys Lys Asp Asp Thr Glu Glu Val Leu Tyr Tyr 420 425 430 Gly Asp Thr Gly Val Ser Lys Asn Pro Val Glu Leu Val Glu Gly Trp 435 440 445 Phe Ser Gly Trp Arg Ser Ser Ile Met Gly Val Leu Ala Val Ile Ile 450 455 460 Gly Phe Val Ile Leu Ile Phe Leu Ile Arg Leu Ile Gly Val Leu Ser 465 470 475 480 Ser Leu Phe Arg Gln Lys Arg Arg Pro Ile Tyr Lys Ser Asp Val Glu 485 490 495 Met Ala His Phe Arg 500 <210> 13 <211> 523 <212> PRT <213> Vesicular stomatitis Carajas virus <400> 13 Met Lys Met Lys Met Val Ile Ala Gly Leu Ile Leu Cys Ile Gly Ile 1 5 10 15 Leu Pro Ala Ile Gly Lys Ile Thr Ile Ser Phe Pro Gln Ser Leu Lys 20 25 30 Gly Asp Trp Arg Pro Val Pro Lys Gly Tyr Asn Tyr Cys Pro Thr Ser 35 40 45 Ala Asp Lys Asn Leu His Gly Asp Leu Ile Asp Ile Gly Leu Arg Leu 50 55 60 Arg Ala Pro Lys Ser Phe Lys Gly Ile Ser Ala Asp Gly Trp Met Cys 65 70 75 80 His Ala Ala Arg Trp Ile Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro 85 90 95 Lys Tyr Ile Thr His Ser Ile His Ser Phe Arg Pro Ser Asn Asp Gln 100 105 110 Cys Lys Glu Ala Ile Arg Leu Thr Asn Glu Gly Asn Trp Ile Asn Pro 115 120 125 Gly Phe Pro Pro Gln Ser Cys Gly Tyr Ala Ser Val Thr Asp Ser Glu 130 135 140 Ser Val Val Val Thr Val Thr Lys His Gln Val Leu Val Asp Glu Tyr 145 150 155 160 Ser Gly Ser Trp Ile Asp Ser Gln Phe Pro Gly Gly Ser Cys Thr Ser 165 170 175 Pro Ile Cys Asp Thr Val His Asn Ser Thr Leu Trp His Ala Asp His 180 185 190 Thr Leu Asp Ser Ile Cys Asp Gln Glu Phe Val Ala Met Asp Ala Val 195 200 205 Leu Phe Thr Glu Ser Gly Lys Phe Glu Glu Phe Gly Lys Pro Asn Ser 210 215 220 Gly Ile Arg Ser Asn Tyr Phe Pro Tyr Glu Ser Leu Lys Asp Val Cys 225 230 235 240 Gln Met Asp Phe Cys Lys Arg Lys Gly Phe Lys Leu Pro Ser Gly Val 245 250 255 Trp Phe Glu Ile Glu Asp Ala Glu Lys Ser His Lys Ala Gln Val Glu 260 265 270 Leu Lys Ile Lys Arg Cys Pro His Gly Ala Val Ile Ser Ala Pro Asn 275 280 285 Gln Asn Ala Ala Asp Ile Asn Leu Ile Met Asp Val Glu Arg Ile Leu 290 295 300 Asp Tyr Ser Leu Cys Gln Ala Thr Trp Ser Lys Ile Gln Asn Lys Glu 305 310 315 320 Ala Leu Thr Pro Ile Asp Ile Ser Tyr Leu Gly Pro Lys Asn Pro Gly 325 330 335 Pro Gly Pro Ala Phe Thr Ile Ile Asn Gly Thr Leu His Tyr Phe Asn 340 345 350 Thr Arg Tyr Ile Arg Val Asp Ile Ala Gly Pro Val Thr Lys Glu Ile 355 360 365 Thr Gly Phe Val Ser Gly Thr Ser Thr Ser Arg Val Leu Trp Asp Gln 370 375 380 Trp Phe Pro Tyr Gly Glu Asn Ser Ile Gly Pro Asn Gly Leu Leu Lys 385 390 395 400 Thr Ala Ser Gly Tyr Lys Tyr Pro Leu Phe Met Val Gly Thr Gly Val 405 410 415 Leu Asp Ala Asp Ile His Lys Leu Gly Glu Ala Thr Val Ile Glu His 420 425 430 Pro His Ala Lys Glu Ala Gln Lys Val Val Asp Asp Ser Glu Val Ile 435 440 445 Phe Phe Gly Asp Thr Gly Val Ser Lys Asn Pro Val Glu Val Val Glu 450 455 460 Gly Trp Phe Ser Gly Trp Arg Ser Ser Leu Met Ser Ile Phe Gly Ile 465 470 475 480 Ile Leu Leu Ile Val Cys Leu Val Leu Ile Val Arg Ile Leu Ile Ala 485 490 495 Leu Lys Tyr Cys Cys Val Arg His Lys Lys Arg Thr Ile Tyr Lys Glu 500 505 510 Asp Leu Glu Met Gly Arg Ile Pro Arg Arg Ala 515 520 <210> 14 <211> 502 <212> PRT <213> Vesicular stomatitis Carajas virus <400> 14 Lys Ile Thr Ile Ser Phe Pro Gln Ser Leu Lys Gly Asp Trp Arg Pro 1 5 10 15 Val Pro Lys Gly Tyr Asn Tyr Cys Pro Thr Ser Ala Asp Lys Asn Leu 20 25 30 His Gly Asp Leu Ile Asp Ile Gly Leu Arg Leu Arg Ala Pro Lys Ser 35 40 45 Phe Lys Gly Ile Ser Ala Asp Gly Trp Met Cys His Ala Ala Arg Trp 50 55 60 Ile Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Phe Arg Pro Ser Asn Asp Gln Cys Lys Glu Ala Ile 85 90 95 Arg Leu Thr Asn Glu Gly Asn Trp Ile Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Ser Val Thr Asp Ser Glu Ser Val Val Val Thr 115 120 125 Val Thr Lys His Gln Val Leu Val Asp Glu Tyr Ser Gly Ser Trp Ile 130 135 140 Asp Ser Gln Phe Pro Gly Gly Ser Cys Thr Ser Pro Ile Cys Asp Thr 145 150 155 160 Val His Asn Ser Thr Leu Trp His Ala Asp His Thr Leu Asp Ser Ile 165 170 175 Cys Asp Gln Glu Phe Val Ala Met Asp Ala Val Leu Phe Thr Glu Ser 180 185 190 Gly Lys Phe Glu Glu Phe Gly Lys Pro Asn Ser Gly Ile Arg Ser Asn 195 200 205 Tyr Phe Pro Tyr Glu Ser Leu Lys Asp Val Cys Gln Met Asp Phe Cys 210 215 220 Lys Arg Lys Gly Phe Lys Leu Pro Ser Gly Val Trp Phe Glu Ile Glu 225 230 235 240 Asp Ala Glu Lys Ser His Lys Ala Gln Val Glu Leu Lys Ile Lys Arg 245 250 255 Cys Pro His Gly Ala Val Ile Ser Ala Pro Asn Gln Asn Ala Ala Asp 260 265 270 Ile Asn Leu Ile Met Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys 275 280 285 Gln Ala Thr Trp Ser Lys Ile Gln Asn Lys Glu Ala Leu Thr Pro Ile 290 295 300 Asp Ile Ser Tyr Leu Gly Pro Lys Asn Pro Gly Pro Gly Pro Ala Phe 305 310 315 320 Thr Ile Ile Asn Gly Thr Leu His Tyr Phe Asn Thr Arg Tyr Ile Arg 325 330 335 Val Asp Ile Ala Gly Pro Val Thr Lys Glu Ile Thr Gly Phe Val Ser 340 345 350 Gly Thr Ser Thr Ser Arg Val Leu Trp Asp Gln Trp Phe Pro Tyr Gly 355 360 365 Glu Asn Ser Ile Gly Pro Asn Gly Leu Leu Lys Thr Ala Ser Gly Tyr 370 375 380 Lys Tyr Pro Leu Phe Met Val Gly Thr Gly Val Leu Asp Ala Asp Ile 385 390 395 400 His Lys Leu Gly Glu Ala Thr Val Ile Glu His Pro His Ala Lys Glu 405 410 415 Ala Gln Lys Val Val Asp Asp Ser Glu Val Ile Phe Phe Gly Asp Thr 420 425 430 Gly Val Ser Lys Asn Pro Val Glu Val Val Glu Gly Trp Phe Ser Gly 435 440 445 Trp Arg Ser Ser Leu Met Ser Ile Phe Gly Ile Ile Leu Leu Ile Val 450 455 460 Cys Leu Val Leu Ile Val Arg Ile Leu Ile Ala Leu Lys Tyr Cys Cys 465 470 475 480 Val Arg His Lys Lys Arg Thr Ile Tyr Lys Glu Asp Leu Glu Met Gly 485 490 495 Arg Ile Pro Arg Arg Ala 500 <210> 15 <211> 9 <212> PRT <213> Artificial sequence <220> <223> Consistent positions 17-25 <220> <221> MISC_FEATURE <222> (3) <223> Xaa can be serine (S), histidine (H), lysine (K), proline (P), or alanine (A) <220> <221> MISC_FEATURE <222> (4)..(4) <223> Xaa can be asparagine (N), glutamic acid (E), threonine (T), glycine (G), or serine (S) <220> <221> MISC_FEATURE <222> (6) <223> Xaa can be histidine (H), asparagine (N), arginine (R), or glutamine (Q) <400> 15 Val Pro Xaa Xaa Tyr Xaa Tyr Cys Pro 1 5 <210> 16 <211> 9 <212> PRT <213> Artificial sequence <220> <223> Consensus positions 421-429 <220> <221> MISC_FEATURE <222> (2)..(2) <223> Xaa can be serine (S), valine (V), or threonine (T) <220> <221> MISC_FEATURE <222> (3) <223> Xaa can be serine (S), valine (V), or threonine (T) <220> <221> MISC_FEATURE <222> (4)..(4) <223> Xaa can be phenylalanine (F) or tyrosine (Y) <220> <221> MISC_FEATURE <222> (5)..(5) <223> Xaa can be phenylalanine (F) or tyrosine (Y) <400> 16 Glu Xaa Xaa Xaa Xaa Gly Asp Thr Gly 1 5 <210> 17 <211> 495 <212> PRT <213> Artificial sequence <220> <223> Vesicular stomatitis Indiana virus glycoprotein H22N <400> 17 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Asn Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Asp Leu Ile Gly Thr Ala Ile Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ser Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr Gln 65 70 75 80 Ser Ile Arg Ser Phe Thr Pro Ser Val Glu Gln Cys Lys Glu Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Ala Val Ile Val Gln 115 120 125 Val Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Ile Asn Gly Lys Cys Ser Asn Tyr Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Lys Gly Leu 165 170 175 Cys Asp Ser Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Glu Leu Ser Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Thr Gly Gly Lys Ala Cys Lys Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Leu Phe Ala Ala Ala Arg Phe Pro Glu Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Gly Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Ala Pro Ile Leu Ser Arg Met Val Gly Met Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asp Asp Trp Ala Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Arg Thr Ser Ser Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Leu Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Ser Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Ser 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Ile Ile Gly Leu Phe Leu 450 455 460 Val Leu Arg Val Gly Ile His Leu Cys Ile Lys Leu Lys His Thr Lys 465 470 475 480 Lys Arg Gln Ile Tyr Thr Asp Ile Glu Met Asn Arg Leu Gly Lys 485 490 495 <210> 18 <211> 495 <212> PRT <213> Artificial sequence <220> <223> Vesicular stomatitis Indiana virus glycoprotein S422I <400> 18 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Asn Tyr His Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Asp Leu Ile Gly Thr Ala Ile Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ser Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr Gln 65 70 75 80 Ser Ile Arg Ser Phe Thr Pro Ser Val Glu Gln Cys Lys Glu Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Ala Val Ile Val Gln 115 120 125 Val Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Ile Asn Gly Lys Cys Ser Asn Tyr Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Lys Gly Leu 165 170 175 Cys Asp Ser Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Glu Leu Ser Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Thr Gly Gly Lys Ala Cys Lys Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Leu Phe Ala Ala Ala Arg Phe Pro Glu Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Gly Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Ala Pro Ile Leu Ser Arg Met Val Gly Met Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asp Asp Trp Ala Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Arg Thr Ser Ser Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Leu Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Ile Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Ser 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Ile Ile Gly Leu Phe Leu 450 455 460 Val Leu Arg Val Gly Ile His Leu Cys Ile Lys Leu Lys His Thr Lys 465 470 475 480 Lys Arg Gln Ile Tyr Thr Asp Ile Glu Met Asn Arg Leu Gly Lys 485 490 495 <210> 19 <211> 495 <212> PRT <213> Artificial Sequence <220> <223> Vesicular stomatitis Indiana virus glycoprotein S422L <400> 19 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Asn Tyr His Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Asp Leu Ile Gly Thr Ala Ile Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ser Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr Gln 65 70 75 80 Ser Ile Arg Ser Phe Thr Pro Ser Val Glu Gln Cys Lys Glu Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Ala Val Ile Val Gln 115 120 125 Val Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Ile Asn Gly Lys Cys Ser Asn Tyr Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Lys Gly Leu 165 170 175 Cys Asp Ser Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Glu Leu Ser Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Thr Gly Gly Lys Ala Cys Lys Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Leu Phe Ala Ala Ala Arg Phe Pro Glu Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Gly Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Ala Pro Ile Leu Ser Arg Met Val Gly Met Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asp Asp Trp Ala Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Arg Thr Ser Ser Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Leu Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Leu Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Ser 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Ile Ile Gly Leu Phe Leu 450 455 460 Val Leu Arg Val Gly Ile His Leu Cys Ile Lys Leu Lys His Thr Lys 465 470 475 480 Lys Arg Gln Ile Tyr Thr Asp Ile Glu Met Asn Arg Leu Gly Lys 485 490 495 <210> 20 <211> 494 <212> PRT <213> Artificial Sequence <220> <223> Vesicular stomatitis Indiana virus glycoprotein S422F <400> 20 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Asn Tyr His Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Asp Leu Ile Gly Thr Ala Ile Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ser Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr Gln 65 70 75 80 Ser Ile Arg Ser Phe Thr Pro Ser Val Glu Gln Cys Lys Glu Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Ala Val Ile Val Gln 115 120 125 Val Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Ile Asn Gly Lys Cys Ser Asn Tyr Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Lys Gly Leu 165 170 175 Cys Asp Ser Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Glu Leu Ser Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Thr Gly Gly Lys Ala Cys Lys Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Leu Phe Ala Ala Ala Arg Phe Pro Glu Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Gly Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Ala Pro Ile Leu Ser Arg Met Val Gly Met Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asp Asp Trp Ala Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Arg Thr Ser Ser Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Leu Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Phe Leu Phe Gly Asp Thr Gly Leu Ser Lys Asn 420 425 430 Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Ser Ile 435 440 445 Ala Ser Phe Phe Phe Ile Ile Gly Leu Ile Ile Gly Leu Phe Leu Val 450 455 460 Leu Arg Val Gly Ile His Leu Cys Ile Lys Leu Lys His Thr Lys Lys 465 470 475 480 Arg Gln Ile Tyr Thr Asp Ile Glu Met Asn Arg Leu Gly Lys 485 490 <210> 21 <211> 495 <212> PRT <213> Artificial sequence <220> <223> Vesicular stomatitis Indiana virus glycoprotein S422M <400> 21 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Asn Tyr His Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Asp Leu Ile Gly Thr Ala Ile Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ser Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr Gln 65 70 75 80 Ser Ile Arg Ser Phe Thr Pro Ser Val Glu Gln Cys Lys Glu Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Ala Val Ile Val Gln 115 120 125 Val Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Ile Asn Gly Lys Cys Ser Asn Tyr Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Lys Gly Leu 165 170 175 Cys Asp Ser Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Glu Leu Ser Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Thr Gly Gly Lys Ala Cys Lys Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Leu Phe Ala Ala Ala Arg Phe Pro Glu Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Gly Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Ala Pro Ile Leu Ser Arg Met Val Gly Met Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asp Asp Trp Ala Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Arg Thr Ser Ser Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Leu Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Met Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Ser 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Ile Ile Gly Leu Phe Leu 450 455 460 Val Leu Arg Val Gly Ile His Leu Cys Ile Lys Leu Lys His Thr Lys 465 470 475 480 Lys Arg Gln Ile Tyr Thr Asp Ile Glu Met Asn Arg Leu Gly Lys 485 490 495 <210> 22 <211> 495 <212> PRT <213> Artificial Sequence <220> <223> Vesicular Stomatitis Indiana Virus Glycoprotein S422V <400> 22 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Asn Tyr His Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Asp Leu Ile Gly Thr Ala Ile Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ser Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr Gln 65 70 75 80 Ser Ile Arg Ser Phe Thr Pro Ser Val Glu Gln Cys Lys Glu Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Ala Val Ile Val Gln 115 120 125 Val Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Ile Asn Gly Lys Cys Ser Asn Tyr Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Lys Gly Leu 165 170 175 Cys Asp Ser Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Glu Leu Ser Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Thr Gly Gly Lys Ala Cys Lys Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Leu Phe Ala Ala Ala Arg Phe Pro Glu Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Gly Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Ala Pro Ile Leu Ser Arg Met Val Gly Met Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asp Asp Trp Ala Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Arg Thr Ser Ser Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Leu Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Val Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Ser 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Ile Ile Gly Leu Phe Leu 450 455 460 Val Leu Arg Val Gly Ile His Leu Cys Ile Lys Leu Lys His Thr Lys 465 470 475 480 Lys Arg Gln Ile Tyr Thr Asp Ile Glu Met Asn Arg Leu Gly Lys 485 490 495 <210> 23 <211> 495 <212> PRT <213> Artificial Sequence <220> <223> Vesicular stomatitis Indiana virus glycoprotein H22N S422I <400> 23 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Asn Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Asp Leu Ile Gly Thr Ala Ile Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ser Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr Gln 65 70 75 80 Ser Ile Arg Ser Phe Thr Pro Ser Val Glu Gln Cys Lys Glu Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Ala Val Ile Val Gln 115 120 125 Val Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Ile Asn Gly Lys Cys Ser Asn Tyr Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Lys Gly Leu 165 170 175 Cys Asp Ser Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Glu Leu Ser Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Thr Gly Gly Lys Ala Cys Lys Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Leu Phe Ala Ala Ala Arg Phe Pro Glu Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Gly Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Ala Pro Ile Leu Ser Arg Met Val Gly Met Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asp Asp Trp Ala Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Arg Thr Ser Ser Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Leu Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Ile Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Ser 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Ile Ile Gly Leu Phe Leu 450 455 460 Val Leu Arg Val Gly Ile His Leu Cys Ile Lys Leu Lys His Thr Lys 465 470 475 480 Lys Arg Gln Ile Tyr Thr Asp Ile Glu Met Asn Arg Leu Gly Lys 485 490 495 <210> 24 <211> 495 <212> PRT <213> Synthetic Sequence <220> <223> Vesicular stomatitis Indiana virus glycoprotein H22N S422L <400> 24 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Asn Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Asp Leu Ile Gly Thr Ala Ile Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ser Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr Gln 65 70 75 80 Ser Ile Arg Ser Phe Thr Pro Ser Val Glu Gln Cys Lys Glu Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Ala Val Ile Val Gln 115 120 125 Val Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Ile Asn Gly Lys Cys Ser Asn Tyr Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Lys Gly Leu 165 170 175 Cys Asp Ser Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Glu Leu Ser Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Thr Gly Gly Lys Ala Cys Lys Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Leu Phe Ala Ala Ala Arg Phe Pro Glu Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Gly Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Ala Pro Ile Leu Ser Arg Met Val Gly Met Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asp Asp Trp Ala Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Arg Thr Ser Ser Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Leu Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Leu Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Ser 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Ile Ile Gly Leu Phe Leu 450 455 460 Val Leu Arg Val Gly Ile His Leu Cys Ile Lys Leu Lys His Thr Lys 465 470 475 480 Lys Arg Gln Ile Tyr Thr Asp Ile Glu Met Asn Arg Leu Gly Lys 485 490 495 <210> 25 <211> 494 <212> PRT <213> Artificial Sequence <220> <223> Vesicular stomatitis Indiana virus glycoprotein H22N S422F <400> 25 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Asn Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Asp Leu Ile Gly Thr Ala Ile Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ser Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr Gln 65 70 75 80 Ser Ile Arg Ser Phe Thr Pro Ser Val Glu Gln Cys Lys Glu Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Ala Val Ile Val Gln 115 120 125 Val Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Ile Asn Gly Lys Cys Ser Asn Tyr Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Lys Gly Leu 165 170 175 Cys Asp Ser Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Glu Leu Ser Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Thr Gly Gly Lys Ala Cys Lys Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Leu Phe Ala Ala Ala Arg Phe Pro Glu Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Gly Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Ala Pro Ile Leu Ser Arg Met Val Gly Met Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asp Asp Trp Ala Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Arg Thr Ser Ser Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Leu Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Phe Leu Phe Gly Asp Thr Gly Leu Ser Lys Asn 420 425 430 Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Ser Ile 435 440 445 Ala Ser Phe Phe Phe Ile Ile Gly Leu Ile Ile Gly Leu Phe Leu Val 450 455 460 Leu Arg Val Gly Ile His Leu Cys Ile Lys Leu Lys His Thr Lys Lys 465 470 475 480 Arg Gln Ile Tyr Thr Asp Ile Glu Met Asn Arg Leu Gly Lys 485 490 <210> 26 <211> 495 <212> PRT <213> Artificial Sequence <220> <223> Vesicular stomatitis Indiana virus glycoprotein H22N S422M <400> 26 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Asn Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Asp Leu Ile Gly Thr Ala Ile Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ser Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr Gln 65 70 75 80 Ser Ile Arg Ser Phe Thr Pro Ser Val Glu Gln Cys Lys Glu Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Ala Val Ile Val Gln 115 120 125 Val Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Ile Asn Gly Lys Cys Ser Asn Tyr Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Lys Gly Leu 165 170 175 Cys Asp Ser Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Glu Leu Ser Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Thr Gly Gly Lys Ala Cys Lys Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Leu Phe Ala Ala Ala Arg Phe Pro Glu Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Gly Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Ala Pro Ile Leu Ser Arg Met Val Gly Met Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asp Asp Trp Ala Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Arg Thr Ser Ser Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Leu Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Met Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Ser 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Ile Ile Gly Leu Phe Leu 450 455 460 Val Leu Arg Val Gly Ile His Leu Cys Ile Lys Leu Lys His Thr Lys 465 470 475 480 Lys Arg Gln Ile Tyr Thr Asp Ile Glu Met Asn Arg Leu Gly Lys 485 490 495 <210> 27 <211> 495 <212> PRT <213> Artificial Sequence <220> <223> Vesicular stomatitis Indiana virus glycoprotein H22N S422V <400> 27 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Asn Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Asp Leu Ile Gly Thr Ala Ile Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ser Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr Gln 65 70 75 80 Ser Ile Arg Ser Phe Thr Pro Ser Val Glu Gln Cys Lys Glu Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Ala Val Ile Val Gln 115 120 125 Val Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Ile Asn Gly Lys Cys Ser Asn Tyr Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Lys Gly Leu 165 170 175 Cys Asp Ser Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Glu Leu Ser Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Thr Gly Gly Lys Ala Cys Lys Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Leu Phe Ala Ala Ala Arg Phe Pro Glu Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Gly Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Ala Pro Ile Leu Ser Arg Met Val Gly Met Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asp Asp Trp Ala Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Arg Thr Ser Ser Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Leu Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Val Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Ser 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Ile Ile Gly Leu Phe Leu 450 455 460 Val Leu Arg Val Gly Ile His Leu Cys Ile Lys Leu Lys His Thr Lys 465 470 475 480 Lys Arg Gln Ile Tyr Thr Asp Ile Glu Met Asn Arg Leu Gly Lys 485 490 495 <210> 28 <211> 496 <212> PRT <213> Artificial Sequence <220> <223> Maraba virus glycoprotein H22N of vesicular stomatitis <400> 28 Lys Phe Thr Ile Val Phe Pro His His Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Thr Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Thr Gly Val Ser Leu His Val Lys Ile Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Met Ser Pro Thr Leu Glu Gln Cys Lys Thr Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Val Trp Ile Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Val Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Leu Val Gly Gly Lys Cys Ser Lys Glu Val Cys Gln Thr 145 150 155 160 Val His Asn Ser Thr Val Trp His Ala Asp Tyr Lys Ile Thr Gly Leu 165 170 175 Cys Glu Ser Asn Leu Ala Ser Val Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Gln Lys Thr Ser Leu Gly Lys Pro Asn Thr Gly Phe Arg Ser Asn 195 200 205 His Phe Ala Tyr Glu Ser Gly Glu Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Thr Gln Trp Gly Ile Arg Leu Pro Ser Gly Val Trp Phe Glu Leu Val 225 230 235 240 Asp Lys Asp Leu Phe Gln Ala Ala Lys Leu Pro Glu Cys Pro Arg Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Lys Leu Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Ser Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ser 325 330 335 Asn Pro Ile Ile Pro His Met Val Gly Thr Met Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asn Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Pro Thr Gly Phe Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Ser Ser 385 390 395 400 Gln Ala Gln Val Phe Glu His Pro His Ala Lys Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Thr Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Val Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Leu Ala Ser Phe Phe Leu Ile Ile Gly Leu Gly Val Ala Leu Ile Phe 450 455 460 Ile Ile Arg Ile Ile Val Ala Ile Arg Tyr Lys Tyr Lys Gly Arg Lys 465 470 475 480 Thr Gln Lys Ile Tyr Asn Asp Val Glu Met Ser Arg Leu Gly Asn Lys 485 490 495 <210> 29 <211> 496 <212> PRT <213> Artificial Sequence <220> <223> Maraba virus glycoprotein of vesicular stomatitis T422I <400> 29 Lys Phe Thr Ile Val Phe Pro His His Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Thr Tyr His Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Thr Gly Val Ser Leu His Val Lys Ile Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Met Ser Pro Thr Leu Glu Gln Cys Lys Thr Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Val Trp Ile Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Val Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Leu Val Gly Gly Lys Cys Ser Lys Glu Val Cys Gln Thr 145 150 155 160 Val His Asn Ser Thr Val Trp His Ala Asp Tyr Lys Ile Thr Gly Leu 165 170 175 Cys Glu Ser Asn Leu Ala Ser Val Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Gln Lys Thr Ser Leu Gly Lys Pro Asn Thr Gly Phe Arg Ser Asn 195 200 205 His Phe Ala Tyr Glu Ser Gly Glu Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Thr Gln Trp Gly Ile Arg Leu Pro Ser Gly Val Trp Phe Glu Leu Val 225 230 235 240 Asp Lys Asp Leu Phe Gln Ala Ala Lys Leu Pro Glu Cys Pro Arg Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Lys Leu Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Ser Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ser 325 330 335 Asn Pro Ile Ile Pro His Met Val Gly Thr Met Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asn Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Pro Thr Gly Phe Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Ser Ser 385 390 395 400 Gln Ala Gln Val Phe Glu His Pro His Ala Lys Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Ile Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Val Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Leu Ala Ser Phe Phe Leu Ile Ile Gly Leu Gly Val Ala Leu Ile Phe 450 455 460 Ile Ile Arg Ile Ile Val Ala Ile Arg Tyr Lys Tyr Lys Gly Arg Lys 465 470 475 480 Thr Gln Lys Ile Tyr Asn Asp Val Glu Met Ser Arg Leu Gly Asn Lys 485 490 495 <210> 30 <211> 496 <212> PRT <213> Artificial Sequence <220> <223> Maraba virus glycoprotein T422L of vesicular stomatitis <400> 30 Lys Phe Thr Ile Val Phe Pro His His Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Thr Tyr His Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Thr Gly Val Ser Leu His Val Lys Ile Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Met Ser Pro Thr Leu Glu Gln Cys Lys Thr Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Val Trp Ile Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Val Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Leu Val Gly Gly Lys Cys Ser Lys Glu Val Cys Gln Thr 145 150 155 160 Val His Asn Ser Thr Val Trp His Ala Asp Tyr Lys Ile Thr Gly Leu 165 170 175 Cys Glu Ser Asn Leu Ala Ser Val Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Gln Lys Thr Ser Leu Gly Lys Pro Asn Thr Gly Phe Arg Ser Asn 195 200 205 His Phe Ala Tyr Glu Ser Gly Glu Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Thr Gln Trp Gly Ile Arg Leu Pro Ser Gly Val Trp Phe Glu Leu Val 225 230 235 240 Asp Lys Asp Leu Phe Gln Ala Ala Lys Leu Pro Glu Cys Pro Arg Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Lys Leu Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Ser Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ser 325 330 335 Asn Pro Ile Ile Pro His Met Val Gly Thr Met Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asn Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Pro Thr Gly Phe Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Ser Ser 385 390 395 400 Gln Ala Gln Val Phe Glu His Pro His Ala Lys Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Leu Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Val Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Leu Ala Ser Phe Phe Leu Ile Ile Gly Leu Gly Val Ala Leu Ile Phe 450 455 460 Ile Ile Arg Ile Ile Val Ala Ile Arg Tyr Lys Tyr Lys Gly Arg Lys 465 470 475 480 Thr Gln Lys Ile Tyr Asn Asp Val Glu Met Ser Arg Leu Gly Asn Lys 485 490 495 <210> 31 <211> 496 <212> PRT <213> Artificial sequence <220> <223> Vesicular stomatitis Maraba virus glycoprotein T422F <400> 31 Lys Phe Thr Ile Val Phe Pro His His Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Thr Tyr His Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Thr Gly Val Ser Leu His Val Lys Ile Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Met Ser Pro Thr Leu Glu Gln Cys Lys Thr Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Val Trp Ile Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Val Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Leu Val Gly Gly Lys Cys Ser Lys Glu Val Cys Gln Thr 145 150 155 160 Val His Asn Ser Thr Val Trp His Ala Asp Tyr Lys Ile Thr Gly Leu 165 170 175 Cys Glu Ser Asn Leu Ala Ser Val Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Gln Lys Thr Ser Leu Gly Lys Pro Asn Thr Gly Phe Arg Ser Asn 195 200 205 His Phe Ala Tyr Glu Ser Gly Glu Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Thr Gln Trp Gly Ile Arg Leu Pro Ser Gly Val Trp Phe Glu Leu Val 225 230 235 240 Asp Lys Asp Leu Phe Gln Ala Ala Lys Leu Pro Glu Cys Pro Arg Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Lys Leu Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Ser Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ser 325 330 335 Asn Pro Ile Ile Pro His Met Val Gly Thr Met Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asn Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Pro Thr Gly Phe Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Ser Ser 385 390 395 400 Gln Ala Gln Val Phe Glu His Pro His Ala Lys Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Phe Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Val Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Leu Ala Ser Phe Phe Leu Ile Ile Gly Leu Gly Val Ala Leu Ile Phe 450 455 460 Ile Ile Arg Ile Ile Val Ala Ile Arg Tyr Lys Tyr Lys Gly Arg Lys 465 470 475 480 Thr Gln Lys Ile Tyr Asn Asp Val Glu Met Ser Arg Leu Gly Asn Lys 485 490 495 <210> 32 <211> 496 <212> PRT <213> Artificial Sequence <220> <223> Maraba virus glycoprotein T422M of vesicular stomatitis <400> 32 ]>Lys Phe Thr Ile Val Phe Pro His His Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Thr Tyr His Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Thr Gly Val Ser Leu His Val Lys Ile Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Met Ser Pro Thr Leu Glu Gln Cys Lys Thr Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Val Trp Ile Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Val Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Leu Val Gly Gly Lys Cys Ser Lys Glu Val Cys Gln Thr 145 150 155 160 Val His Asn Ser Thr Val Trp His Ala Asp Tyr Lys Ile Thr Gly Leu 165 170 175 Cys Glu Ser Asn Leu Ala Ser Val Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Gln Lys Thr Ser Leu Gly Lys Pro Asn Thr Gly Phe Arg Ser Asn 195 200 205 His Phe Ala Tyr Glu Ser Gly Glu Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Thr Gln Trp Gly Ile Arg Leu Pro Ser Gly Val Trp Phe Glu Leu Val 225 230 235 240 Asp Lys Asp Leu Phe Gln Ala Ala Lys Leu Pro Glu Cys Pro Arg Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Lys Leu Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Ser Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ser 325 330 335 Asn Pro Ile Ile Pro His Met Val Gly Thr Met Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asn Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Pro Thr Gly Phe Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Ser Ser 385 390 395 400 Gln Ala Gln Val Phe Glu His Pro His Ala Lys Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Met Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Val Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Leu Ala Ser Phe Phe Leu Ile Ile Gly Leu Gly Val Ala Leu Ile Phe 450 455 460 Ile Ile Arg Ile Ile Val Ala Ile Arg Tyr Lys Tyr Lys Gly Arg Lys 465 470 475 480 Thr Gln Lys Ile Tyr Asn Asp Val Glu Met Ser Arg Leu Gly Asn Lys 485 490 495 <210> 33 <211> 496 <212> PRT <213> Artificial Sequence <220> <223> Maraba virus glycoprotein of vesicular stomatitis T422V <400> 33 Lys Phe Thr Ile Val Phe Pro His His Glu Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Thr Tyr His Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Thr Gly Val Ser Leu His Val Lys Ile Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Met Ser Pro Thr Leu Glu Gln Cys Lys Thr Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Val Trp Ile Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Val Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Leu Val Gly Gly Lys Cys Ser Lys Glu Val Cys Gln Thr 145 150 155 160 Val His Asn Ser Thr Val Trp His Ala Asp Tyr Lys Ile Thr Gly Leu 165 170 175 Cys Glu Ser Asn Leu Ala Ser Val Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Gln Lys Thr Ser Leu Gly Lys Pro Asn Thr Gly Phe Arg Ser Asn 195 200 205 His Phe Ala Tyr Glu Ser Gly Glu Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Thr Gln Trp Gly Ile Arg Leu Pro Ser Gly Val Trp Phe Glu Leu Val 225 230 235 240 Asp Lys Asp Leu Phe Gln Ala Ala Lys Leu Pro Glu Cys Pro Arg Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Lys Leu Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Ser Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ser 325 330 335 Asn Pro Ile Ile Pro His Met Val Gly Thr Met Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asn Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Pro Thr Gly Phe Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Ser Ser 385 390 395 400 Gln Ala Gln Val Phe Glu His Pro His Ala Lys Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Val Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Val Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Leu Ala Ser Phe Phe Leu Ile Ile Gly Leu Gly Val Ala Leu Ile Phe 450 455 460 Ile Ile Arg Ile Ile Val Ala Ile Arg Tyr Lys Tyr Lys Gly Arg Lys 465 470 475 480 Thr Gln Lys Ile Tyr Asn Asp Val Glu Met Ser Arg Leu Gly Asn Lys 485 490 495 <210> 34 <211> 496 <212> PRT <213> Artificial Sequence <220> <223> Maraba virus glycoprotein H22N T422I of vesicular stomatitis <400> 34 Lys Phe Thr Ile Val Phe Pro His His Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Thr Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Thr Gly Val Ser Leu His Val Lys Ile Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Met Ser Pro Thr Leu Glu Gln Cys Lys Thr Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Val Trp Ile Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Val Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Leu Val Gly Gly Lys Cys Ser Lys Glu Val Cys Gln Thr 145 150 155 160 Val His Asn Ser Thr Val Trp His Ala Asp Tyr Lys Ile Thr Gly Leu 165 170 175 Cys Glu Ser Asn Leu Ala Ser Val Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Gln Lys Thr Ser Leu Gly Lys Pro Asn Thr Gly Phe Arg Ser Asn 195 200 205 His Phe Ala Tyr Glu Ser Gly Glu Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Thr Gln Trp Gly Ile Arg Leu Pro Ser Gly Val Trp Phe Glu Leu Val 225 230 235 240 Asp Lys Asp Leu Phe Gln Ala Ala Lys Leu Pro Glu Cys Pro Arg Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Lys Leu Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Ser Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ser 325 330 335 Asn Pro Ile Ile Pro His Met Val Gly Thr Met Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asn Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Pro Thr Gly Phe Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Ser Ser 385 390 395 400 Gln Ala Gln Val Phe Glu His Pro His Ala Lys Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Ile Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Val Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Leu Ala Ser Phe Phe Leu Ile Ile Gly Leu Gly Val Ala Leu Ile Phe 450 455 460 Ile Ile Arg Ile Ile Val Ala Ile Arg Tyr Lys Tyr Lys Gly Arg Lys 465 470 475 480 Thr Gln Lys Ile Tyr Asn Asp Val Glu Met Ser Arg Leu Gly Asn Lys 485 490 495 <210> 35 <211> 496 <212> PRT <213> Artificial Sequence <220> <223> Maraba virus glycoprotein H22N T422L of vesicular stomatitis <400> 35 Lys Phe Thr Ile Val Phe Pro His His Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Thr Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Thr Gly Val Ser Leu His Val Lys Ile Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Met Ser Pro Thr Leu Glu Gln Cys Lys Thr Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Val Trp Ile Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Val Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Leu Val Gly Gly Lys Cys Ser Lys Glu Val Cys Gln Thr 145 150 155 160 Val His Asn Ser Thr Val Trp His Ala Asp Tyr Lys Ile Thr Gly Leu 165 170 175 Cys Glu Ser Asn Leu Ala Ser Val Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Gln Lys Thr Ser Leu Gly Lys Pro Asn Thr Gly Phe Arg Ser Asn 195 200 205 His Phe Ala Tyr Glu Ser Gly Glu Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Thr Gln Trp Gly Ile Arg Leu Pro Ser Gly Val Trp Phe Glu Leu Val 225 230 235 240 Asp Lys Asp Leu Phe Gln Ala Ala Lys Leu Pro Glu Cys Pro Arg Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Lys Leu Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Ser Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ser 325 330 335 Asn Pro Ile Ile Pro His Met Val Gly Thr Met Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asn Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Pro Thr Gly Phe Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Ser Ser 385 390 395 400 Gln Ala Gln Val Phe Glu His Pro His Ala Lys Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Leu Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Val Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Leu Ala Ser Phe Phe Leu Ile Ile Gly Leu Gly Val Ala Leu Ile Phe 450 455 460 Ile Ile Arg Ile Ile Val Ala Ile Arg Tyr Lys Tyr Lys Gly Arg Lys 465 470 475 480 Thr Gln Lys Ile Tyr Asn Asp Val Glu Met Ser Arg Leu Gly Asn Lys 485 490 495 <210> 36 <211> 496 <212> PRT <213> Artificial Sequence <220> <223> Maraba virus glycoprotein H22N T422F of vesicular stomatitis <400> 36 Lys Phe Thr Ile Val Phe Pro His His Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Thr Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Thr Gly Val Ser Leu His Val Lys Ile Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Met Ser Pro Thr Leu Glu Gln Cys Lys Thr Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Val Trp Ile Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Val Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Leu Val Gly Gly Lys Cys Ser Lys Glu Val Cys Gln Thr 145 150 155 160 Val His Asn Ser Thr Val Trp His Ala Asp Tyr Lys Ile Thr Gly Leu 165 170 175 Cys Glu Ser Asn Leu Ala Ser Val Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Gln Lys Thr Ser Leu Gly Lys Pro Asn Thr Gly Phe Arg Ser Asn 195 200 205 His Phe Ala Tyr Glu Ser Gly Glu Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Thr Gln Trp Gly Ile Arg Leu Pro Ser Gly Val Trp Phe Glu Leu Val 225 230 235 240 Asp Lys Asp Leu Phe Gln Ala Ala Lys Leu Pro Glu Cys Pro Arg Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Lys Leu Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Ser Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ser 325 330 335 Asn Pro Ile Ile Pro His Met Val Gly Thr Met Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asn Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Pro Thr Gly Phe Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Ser Ser 385 390 395 400 Gln Ala Gln Val Phe Glu His Pro His Ala Lys Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Phe Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Val Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Leu Ala Ser Phe Phe Leu Ile Ile Gly Leu Gly Val Ala Leu Ile Phe 450 455 460 Ile Ile Arg Ile Ile Val Ala Ile Arg Tyr Lys Tyr Lys Gly Arg Lys 465 470 475 480 Thr Gln Lys Ile Tyr Asn Asp Val Glu Met Ser Arg Leu Gly Asn Lys 485 490 495 <210> 37 <211> 496 <212> PRT <213> Artificial sequence <220> <223> Maraba virus glycoprotein H22N T422M of vesicular stomatitis <400> 37 Lys Phe Thr Ile Val Phe Pro His His Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Thr Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Thr Gly Val Ser Leu His Val Lys Ile Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Met Ser Pro Thr Leu Glu Gln Cys Lys Thr Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Val Trp Ile Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Val Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Leu Val Gly Gly Lys Cys Ser Lys Glu Val Cys Gln Thr 145 150 155 160 Val His Asn Ser Thr Val Trp His Ala Asp Tyr Lys Ile Thr Gly Leu 165 170 175 Cys Glu Ser Asn Leu Ala Ser Val Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Gln Lys Thr Ser Leu Gly Lys Pro Asn Thr Gly Phe Arg Ser Asn 195 200 205 His Phe Ala Tyr Glu Ser Gly Glu Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Thr Gln Trp Gly Ile Arg Leu Pro Ser Gly Val Trp Phe Glu Leu Val 225 230 235 240 Asp Lys Asp Leu Phe Gln Ala Ala Lys Leu Pro Glu Cys Pro Arg Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Lys Leu Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Ser Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ser 325 330 335 Asn Pro Ile Ile Pro His Met Val Gly Thr Met Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asn Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Pro Thr Gly Phe Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Ser Ser 385 390 395 400 Gln Ala Gln Val Phe Glu His Pro His Ala Lys Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Met Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Val Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Leu Ala Ser Phe Phe Leu Ile Ile Gly Leu Gly Val Ala Leu Ile Phe 450 455 460 Ile Ile Arg Ile Ile Val Ala Ile Arg Tyr Lys Tyr Lys Gly Arg Lys 465 470 475 480 Thr Gln Lys Ile Tyr Asn Asp Val Glu Met Ser Arg Leu Gly Asn Lys 485 490 495 <210> 38 <211> 496 <212> PRT <213> Artificial Sequence <220> <223> Maraba virus glycoprotein H22N T422V of vesicular stomatitis <400> 38 Lys Phe Thr Ile Val Phe Pro His His Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Thr Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Thr Gly Val Ser Leu His Val Lys Ile Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Met Ser Pro Thr Leu Glu Gln Cys Lys Thr Ser Ile 85 90 95 Glu Gln Thr Lys Gln Gly Val Trp Ile Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Thr Val Thr Asp Ala Glu Val Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Leu Val Gly Gly Lys Cys Ser Lys Glu Val Cys Gln Thr 145 150 155 160 Val His Asn Ser Thr Val Trp His Ala Asp Tyr Lys Ile Thr Gly Leu 165 170 175 Cys Glu Ser Asn Leu Ala Ser Val Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Gln Lys Thr Ser Leu Gly Lys Pro Asn Thr Gly Phe Arg Ser Asn 195 200 205 His Phe Ala Tyr Glu Ser Gly Glu Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Thr Gln Trp Gly Ile Arg Leu Pro Ser Gly Val Trp Phe Glu Leu Val 225 230 235 240 Asp Lys Asp Leu Phe Gln Ala Ala Lys Leu Pro Glu Cys Pro Arg Gly 245 250 255 Ser Ser Ile Ser Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala Lys Leu Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Ser Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ser 325 330 335 Asn Pro Ile Ile Pro His Met Val Gly Thr Met Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Asn Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Pro Thr Gly Phe Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Ser Ser 385 390 395 400 Gln Ala Gln Val Phe Glu His Pro His Ala Lys Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Val Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Val Glu Leu Val Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Leu Ala Ser Phe Phe Leu Ile Ile Gly Leu Gly Val Ala Leu Ile Phe 450 455 460 Ile Ile Arg Ile Ile Val Ala Ile Arg Tyr Lys Tyr Lys Gly Arg Lys 465 470 475 480 Thr Gln Lys Ile Tyr Asn Asp Val Glu Met Ser Arg Leu Gly Asn Lys 485 490 495 <210> 39 <211> 495 <212> PRT <213> artificial sequence <220> <223> H22N <400> 39 Light Phe Ser Ile Val Phe Pro Gln Ser Gln Light Gly Asn Trp Light Asn 1 5 10 15 Val Pro Ser Ser Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Leu Gly Ile Thr Met Lys Val Lys Met Pro Lys Thr 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Ile Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Ile Gln Pro Thr Ser Glu Gln Cys Lys Glu Ser Ile 85 90 95 Lys Gln Thr Lys Gln Gly Thr Trp Met Ser Pro Gly Phe Pro Pro Gln 100 105 110 Asn Cys Gly Tyr Ala Thr Val Thr Asp Ser Val Ala Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Phe Pro Asn Gly Lys Cys Glu Thr Glu Glu Cys Glu Thr 145 150 155 160 Val His Asn Ser Thr Val Trp Tyr Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Thr Leu Val Asp Thr Glu Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Lys Glu Ser Ile Gly Lys Pro Asn Thr Gly Tyr Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Lys Gly Asp Lys Val Cys Lys Met Asn Tyr Cys 210 215 220 Lys His Ala Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Phe Val 225 230 235 240 Asp Gln Asp Val Tyr Ala Ala Ala Lys Leu Pro Glu Cys Pro Val Gly 245 250 255 Ala Thr Ile Ser Ala Pro Thr Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Leu Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ser Lys Gln Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Ile Asp Ile Asp 325 330 335 Asn Pro Ile Ile Ser Lys Met Val Gly Lys Ile Ser Gly Ser Gln Thr 340 345 350 Glu Arg Glu Leu Trp Thr Glu Trp Phe Pro Tyr Glu Gly Val Glu Ile 355 360 365 Gly Pro Asn Gly Ile Leu Lys Thr Pro Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Phe Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Thr Ser 385 390 395 400 Gln Ala Glu Val Phe Glu His Pro His Leu Ala Glu Ala Pro Lys Gln 405 410 415 Leu Pro Glu Glu Glu Thr Leu Phe Phe Gly Asp Thr Gly Ile Ser Lys 420 425 430 Asn Pro Val Glu Leu Ile Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Val Val Thr Phe Phe Phe Ala Ile Gly Val Phe Ile Leu Leu Tyr Val 450 455 460 Val Ala Arg Ile Val Ile Ala Val Arg Tyr Arg Tyr Gln Gly Ser Asn 465 470 475 480 Asn Lys Arg Ile Tyr Asn Asp Ile Glu Met Ser Arg Phe Arg Lys 485 490 495 <210> 40 <211> 495 <212> PRT <213> Artificial Sequence <220> <223> Vesicular stomatitis Cocal virus glycoprotein T422I <400> 40 Lys Phe Ser Ile Val Phe Pro Gln Ser Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Ser Tyr His Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Leu Gly Ile Thr Met Lys Val Lys Met Pro Lys Thr 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Ile Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Ile Gln Pro Thr Ser Glu Gln Cys Lys Glu Ser Ile 85 90 95 Lys Gln Thr Lys Gln Gly Thr Trp Met Ser Pro Gly Phe Pro Pro Gln 100 105 110 Asn Cys Gly Tyr Ala Thr Val Thr Asp Ser Val Ala Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Phe Pro Asn Gly Lys Cys Glu Thr Glu Glu Cys Glu Thr 145 150 155 160 Val His Asn Ser Thr Val Trp Tyr Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Thr Leu Val Asp Thr Glu Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Lys Glu Ser Ile Gly Lys Pro Asn Thr Gly Tyr Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Lys Gly Asp Lys Val Cys Lys Met Asn Tyr Cys 210 215 220 Lys His Ala Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Phe Val 225 230 235 240 Asp Gln Asp Val Tyr Ala Ala Ala Lys Leu Pro Glu Cys Pro Val Gly 245 250 255 Ala Thr Ile Ser Ala Pro Thr Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Leu Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ser Lys Gln Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Ile Asp Ile Asp 325 330 335 Asn Pro Ile Ile Ser Lys Met Val Gly Lys Ile Ser Gly Ser Gln Thr 340 345 350 Glu Arg Glu Leu Trp Thr Glu Trp Phe Pro Tyr Glu Gly Val Glu Ile 355 360 365 Gly Pro Asn Gly Ile Leu Lys Thr Pro Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Phe Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Thr Ser 385 390 395 400 Gln Ala Glu Val Phe Glu His Pro His Leu Ala Glu Ala Pro Lys Gln 405 410 415 Leu Pro Glu Glu Glu Ile Leu Phe Phe Gly Asp Thr Gly Ile Ser Lys 420 425 430 Asn Pro Val Glu Leu Ile Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Val Val Thr Phe Phe Phe Ala Ile Gly Val Phe Ile Leu Leu Tyr Val 450 455 460 Val Ala Arg Ile Val Ile Ala Val Arg Tyr Arg Tyr Gln Gly Ser Asn 465 470 475 480 Asn Lys Arg Ile Tyr Asn Asp Ile Glu Met Ser Arg Phe Arg Lys 485 490 495 <210> 41 <211> 495 <212> PRT <213> Artificial sequence <220> <223> Vesicular stomatitis Cocal virus glycoprotein T422L <400> 41 Lys Phe Ser Ile Val Phe Pro Gln Ser Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Ser Tyr His Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Leu Gly Ile Thr Met Lys Val Lys Met Pro Lys Thr 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Ile Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Ile Gln Pro Thr Ser Glu Gln Cys Lys Glu Ser Ile 85 90 95 Lys Gln Thr Lys Gln Gly Thr Trp Met Ser Pro Gly Phe Pro Pro Gln 100 105 110 Asn Cys Gly Tyr Ala Thr Val Thr Asp Ser Val Ala Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Phe Pro Asn Gly Lys Cys Glu Thr Glu Glu Cys Glu Thr 145 150 155 160 Val His Asn Ser Thr Val Trp Tyr Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Thr Leu Val Asp Thr Glu Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Lys Glu Ser Ile Gly Lys Pro Asn Thr Gly Tyr Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Lys Gly Asp Lys Val Cys Lys Met Asn Tyr Cys 210 215 220 Lys His Ala Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Phe Val 225 230 235 240 Asp Gln Asp Val Tyr Ala Ala Ala Lys Leu Pro Glu Cys Pro Val Gly 245 250 255 Ala Thr Ile Ser Ala Pro Thr Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Leu Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ser Lys Gln Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Ile Asp Ile Asp 325 330 335 Asn Pro Ile Ile Ser Lys Met Val Gly Lys Ile Ser Gly Ser Gln Thr 340 345 350 Glu Arg Glu Leu Trp Thr Glu Trp Phe Pro Tyr Glu Gly Val Glu Ile 355 360 365 Gly Pro Asn Gly Ile Leu Lys Thr Pro Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Phe Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Thr Ser 385 390 395 400 Gln Ala Glu Val Phe Glu His Pro His Leu Ala Glu Ala Pro Lys Gln 405 410 415 Leu Pro Glu Glu Glu Leu Leu Phe Phe Gly Asp Thr Gly Ile Ser Lys 420 425 430 Asn Pro Val Glu Leu Ile Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Val Val Thr Phe Phe Phe Ala Ile Gly Val Phe Ile Leu Leu Tyr Val 450 455 460 Val Ala Arg Ile Val Ile Ala Val Arg Tyr Arg Tyr Gln Gly Ser Asn 465 470 475 480 Asn Lys Arg Ile Tyr Asn Asp Ile Glu Met Ser Arg Phe Arg Lys 485 490 495 <210> 42 <211> 495 <212> PRT <213> Artificial Sequence <220> <223> Vesicular Stomatitis Cocal Virus Glycoprotein T422F <400> 42 Lys Phe Ser Ile Val Phe Pro Gln Ser Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Ser Tyr His Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Leu Gly Ile Thr Met Lys Val Lys Met Pro Lys Thr 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Ile Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Ile Gln Pro Thr Ser Glu Gln Cys Lys Glu Ser Ile 85 90 95 Lys Gln Thr Lys Gln Gly Thr Trp Met Ser Pro Gly Phe Pro Pro Gln 100 105 110 Asn Cys Gly Tyr Ala Thr Val Thr Asp Ser Val Ala Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Phe Pro Asn Gly Lys Cys Glu Thr Glu Glu Cys Glu Thr 145 150 155 160 Val His Asn Ser Thr Val Trp Tyr Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Thr Leu Val Asp Thr Glu Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Lys Glu Ser Ile Gly Lys Pro Asn Thr Gly Tyr Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Lys Gly Asp Lys Val Cys Lys Met Asn Tyr Cys 210 215 220 Lys His Ala Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Phe Val 225 230 235 240 Asp Gln Asp Val Tyr Ala Ala Ala Lys Leu Pro Glu Cys Pro Val Gly 245 250 255 Ala Thr Ile Ser Ala Pro Thr Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Leu Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ser Lys Gln Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Ile Asp Ile Asp 325 330 335 Asn Pro Ile Ile Ser Lys Met Val Gly Lys Ile Ser Gly Ser Gln Thr 340 345 350 Glu Arg Glu Leu Trp Thr Glu Trp Phe Pro Tyr Glu Gly Val Glu Ile 355 360 365 Gly Pro Asn Gly Ile Leu Lys Thr Pro Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Phe Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Thr Ser 385 390 395 400 Gln Ala Glu Val Phe Glu His Pro His Leu Ala Glu Ala Pro Lys Gln 405 410 415 Leu Pro Glu Glu Glu Phe Leu Phe Phe Gly Asp Thr Gly Ile Ser Lys 420 425 430 Asn Pro Val Glu Leu Ile Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Val Val Thr Phe Phe Phe Ala Ile Gly Val Phe Ile Leu Leu Tyr Val 450 455 460 Val Ala Arg Ile Val Ile Ala Val Arg Tyr Arg Tyr Gln Gly Ser Asn 465 470 475 480 Asn Lys Arg Ile Tyr Asn Asp Ile Glu Met Ser Arg Phe Arg Lys 485 490 495 <210> 43 <211> 495 <212> PRT <213> Artificial Sequence <220> <223> Vesicular stomatitis Cocal virus glycoprotein T422M <400> 43 Lys Phe Ser Ile Val Phe Pro Gln Ser Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Ser Tyr His Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Leu Gly Ile Thr Met Lys Val Lys Met Pro Lys Thr 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Ile Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Ile Gln Pro Thr Ser Glu Gln Cys Lys Glu Ser Ile 85 90 95 Lys Gln Thr Lys Gln Gly Thr Trp Met Ser Pro Gly Phe Pro Pro Gln 100 105 110 Asn Cys Gly Tyr Ala Thr Val Thr Asp Ser Val Ala Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Phe Pro Asn Gly Lys Cys Glu Thr Glu Glu Cys Glu Thr 145 150 155 160 Val His Asn Ser Thr Val Trp Tyr Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Thr Leu Val Asp Thr Glu Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Lys Glu Ser Ile Gly Lys Pro Asn Thr Gly Tyr Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Lys Gly Asp Lys Val Cys Lys Met Asn Tyr Cys 210 215 220 Lys His Ala Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Phe Val 225 230 235 240 Asp Gln Asp Val Tyr Ala Ala Ala Lys Leu Pro Glu Cys Pro Val Gly 245 250 255 Ala Thr Ile Ser Ala Pro Thr Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Leu Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ser Lys Gln Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Ile Asp Ile Asp 325 330 335 Asn Pro Ile Ile Ser Lys Met Val Gly Lys Ile Ser Gly Ser Gln Thr 340 345 350 Glu Arg Glu Leu Trp Thr Glu Trp Phe Pro Tyr Glu Gly Val Glu Ile 355 360 365 Gly Pro Asn Gly Ile Leu Lys Thr Pro Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Phe Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Thr Ser 385 390 395 400 Gln Ala Glu Val Phe Glu His Pro His Leu Ala Glu Ala Pro Lys Gln 405 410 415 Leu Pro Glu Glu Glu Met Leu Phe Phe Gly Asp Thr Gly Ile Ser Lys 420 425 430 Asn Pro Val Glu Leu Ile Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Val Val Thr Phe Phe Phe Ala Ile Gly Val Phe Ile Leu Leu Tyr Val 450 455 460 Val Ala Arg Ile Val Ile Ala Val Arg Tyr Arg Tyr Gln Gly Ser Asn 465 470 475 480 Asn Lys Arg Ile Tyr Asn Asp Ile Glu Met Ser Arg Phe Arg Lys 485 490 495 <210> 44 <211> 495 <212> PRT <213> Artificial Sequence <220> <223> Vesicular stomatitis Cocal virus glycoprotein T422V <400> 44 Lys Phe Ser Ile Val Phe Pro Gln Ser Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Ser Tyr His Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Leu Gly Ile Thr Met Lys Val Lys Met Pro Lys Thr 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Ile Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Ile Gln Pro Thr Ser Glu Gln Cys Lys Glu Ser Ile 85 90 95 Lys Gln Thr Lys Gln Gly Thr Trp Met Ser Pro Gly Phe Pro Pro Gln 100 105 110 Asn Cys Gly Tyr Ala Thr Val Thr Asp Ser Val Ala Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Phe Pro Asn Gly Lys Cys Glu Thr Glu Glu Cys Glu Thr 145 150 155 160 Val His Asn Ser Thr Val Trp Tyr Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Thr Leu Val Asp Thr Glu Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Lys Glu Ser Ile Gly Lys Pro Asn Thr Gly Tyr Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Lys Gly Asp Lys Val Cys Lys Met Asn Tyr Cys 210 215 220 Lys His Ala Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Phe Val 225 230 235 240 Asp Gln Asp Val Tyr Ala Ala Ala Lys Leu Pro Glu Cys Pro Val Gly 245 250 255 Ala Thr Ile Ser Ala Pro Thr Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Leu Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ser Lys Gln Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Ile Asp Ile Asp 325 330 335 Asn Pro Ile Ile Ser Lys Met Val Gly Lys Ile Ser Gly Ser Gln Thr 340 345 350 Glu Arg Glu Leu Trp Thr Glu Trp Phe Pro Tyr Glu Gly Val Glu Ile 355 360 365 Gly Pro Asn Gly Ile Leu Lys Thr Pro Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Phe Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Thr Ser 385 390 395 400 Gln Ala Glu Val Phe Glu His Pro His Leu Ala Glu Ala Pro Lys Gln 405 410 415 Leu Pro Glu Glu Glu Val Leu Phe Phe Gly Asp Thr Gly Ile Ser Lys 420 425 430 Asn Pro Val Glu Leu Ile Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Val Val Thr Phe Phe Phe Ala Ile Gly Val Phe Ile Leu Leu Tyr Val 450 455 460 Val Ala Arg Ile Val Ile Ala Val Arg Tyr Arg Tyr Gln Gly Ser Asn 465 470 475 480 Asn Lys Arg Ile Tyr Asn Asp Ile Glu Met Ser Arg Phe Arg Lys 485 490 495 <210> 45 <211> 495 <212> PRT <213> Artificial Sequence <220> <223> Vesicular stomatitis Cocal virus glycoprotein H22N T422I <400> 45 Lys Phe Ser Ile Val Phe Pro Gln Ser Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Ser Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Leu Gly Ile Thr Met Lys Val Lys Met Pro Lys Thr 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Ile Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Ile Gln Pro Thr Ser Glu Gln Cys Lys Glu Ser Ile 85 90 95 Lys Gln Thr Lys Gln Gly Thr Trp Met Ser Pro Gly Phe Pro Pro Gln 100 105 110 Asn Cys Gly Tyr Ala Thr Val Thr Asp Ser Val Ala Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Phe Pro Asn Gly Lys Cys Glu Thr Glu Glu Cys Glu Thr 145 150 155 160 Val His Asn Ser Thr Val Trp Tyr Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Thr Leu Val Asp Thr Glu Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Lys Glu Ser Ile Gly Lys Pro Asn Thr Gly Tyr Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Lys Gly Asp Lys Val Cys Lys Met Asn Tyr Cys 210 215 220 Lys His Ala Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Phe Val 225 230 235 240 Asp Gln Asp Val Tyr Ala Ala Ala Lys Leu Pro Glu Cys Pro Val Gly 245 250 255 Ala Thr Ile Ser Ala Pro Thr Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Leu Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ser Lys Gln Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Ile Asp Ile Asp 325 330 335 Asn Pro Ile Ile Ser Lys Met Val Gly Lys Ile Ser Gly Ser Gln Thr 340 345 350 Glu Arg Glu Leu Trp Thr Glu Trp Phe Pro Tyr Glu Gly Val Glu Ile 355 360 365 Gly Pro Asn Gly Ile Leu Lys Thr Pro Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Phe Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Thr Ser 385 390 395 400 Gln Ala Glu Val Phe Glu His Pro His Leu Ala Glu Ala Pro Lys Gln 405 410 415 Leu Pro Glu Glu Glu Ile Leu Phe Phe Gly Asp Thr Gly Ile Ser Lys 420 425 430 Asn Pro Val Glu Leu Ile Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Val Val Thr Phe Phe Phe Ala Ile Gly Val Phe Ile Leu Leu Tyr Val 450 455 460 Val Ala Arg Ile Val Ile Ala Val Arg Tyr Arg Tyr Gln Gly Ser Asn 465 470 475 480 Asn Lys Arg Ile Tyr Asn Asp Ile Glu Met Ser Arg Phe Arg Lys 485 490 495 <210> 46 <211> 495 <212> PRT <213> Artificial Sequence <220> <223> Vesicular Stomatitis Cocal Virus Glycoprotein H22N T422L <400> 46 Lys Phe Ser Ile Val Phe Pro Gln Ser Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Ser Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Leu Gly Ile Thr Met Lys Val Lys Met Pro Lys Thr 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Ile Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Ile Gln Pro Thr Ser Glu Gln Cys Lys Glu Ser Ile 85 90 95 Lys Gln Thr Lys Gln Gly Thr Trp Met Ser Pro Gly Phe Pro Pro Gln 100 105 110 Asn Cys Gly Tyr Ala Thr Val Thr Asp Ser Val Ala Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Phe Pro Asn Gly Lys Cys Glu Thr Glu Glu Cys Glu Thr 145 150 155 160 Val His Asn Ser Thr Val Trp Tyr Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Thr Leu Val Asp Thr Glu Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Lys Glu Ser Ile Gly Lys Pro Asn Thr Gly Tyr Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Lys Gly Asp Lys Val Cys Lys Met Asn Tyr Cys 210 215 220 Lys His Ala Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Phe Val 225 230 235 240 Asp Gln Asp Val Tyr Ala Ala Ala Lys Leu Pro Glu Cys Pro Val Gly 245 250 255 Ala Thr Ile Ser Ala Pro Thr Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Leu Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ser Lys Gln Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Ile Asp Ile Asp 325 330 335 Asn Pro Ile Ile Ser Lys Met Val Gly Lys Ile Ser Gly Ser Gln Thr 340 345 350 Glu Arg Glu Leu Trp Thr Glu Trp Phe Pro Tyr Glu Gly Val Glu Ile 355 360 365 Gly Pro Asn Gly Ile Leu Lys Thr Pro Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Phe Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Thr Ser 385 390 395 400 Gln Ala Glu Val Phe Glu His Pro His Leu Ala Glu Ala Pro Lys Gln 405 410 415 Leu Pro Glu Glu Glu Leu Leu Phe Phe Gly Asp Thr Gly Ile Ser Lys 420 425 430 Asn Pro Val Glu Leu Ile Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Val Val Thr Phe Phe Phe Ala Ile Gly Val Phe Ile Leu Leu Tyr Val 450 455 460 Val Ala Arg Ile Val Ile Ala Val Arg Tyr Arg Tyr Gln Gly Ser Asn 465 470 475 480 Asn Lys Arg Ile Tyr Asn Asp Ile Glu Met Ser Arg Phe Arg Lys 485 490 495 <210> 47 <211> 495 <212> PRT <213> Artificial Sequence <220> <223> Vesicular stomatitis Cocal virus glycoprotein H22N T422F <400> 47 Lys Phe Ser Ile Val Phe Pro Gln Ser Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Ser Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Leu Gly Ile Thr Met Lys Val Lys Met Pro Lys Thr 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Ile Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Ile Gln Pro Thr Ser Glu Gln Cys Lys Glu Ser Ile 85 90 95 Lys Gln Thr Lys Gln Gly Thr Trp Met Ser Pro Gly Phe Pro Pro Gln 100 105 110 Asn Cys Gly Tyr Ala Thr Val Thr Asp Ser Val Ala Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Phe Pro Asn Gly Lys Cys Glu Thr Glu Glu Cys Glu Thr 145 150 155 160 Val His Asn Ser Thr Val Trp Tyr Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Thr Leu Val Asp Thr Glu Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Lys Glu Ser Ile Gly Lys Pro Asn Thr Gly Tyr Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Lys Gly Asp Lys Val Cys Lys Met Asn Tyr Cys 210 215 220 Lys His Ala Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Phe Val 225 230 235 240 Asp Gln Asp Val Tyr Ala Ala Ala Lys Leu Pro Glu Cys Pro Val Gly 245 250 255 Ala Thr Ile Ser Ala Pro Thr Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Leu Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ser Lys Gln Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Ile Asp Ile Asp 325 330 335 Asn Pro Ile Ile Ser Lys Met Val Gly Lys Ile Ser Gly Ser Gln Thr 340 345 350 Glu Arg Glu Leu Trp Thr Glu Trp Phe Pro Tyr Glu Gly Val Glu Ile 355 360 365 Gly Pro Asn Gly Ile Leu Lys Thr Pro Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Phe Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Thr Ser 385 390 395 400 Gln Ala Glu Val Phe Glu His Pro His Leu Ala Glu Ala Pro Lys Gln 405 410 415 Leu Pro Glu Glu Glu Phe Leu Phe Phe Gly Asp Thr Gly Ile Ser Lys 420 425 430 Asn Pro Val Glu Leu Ile Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Val Val Thr Phe Phe Phe Ala Ile Gly Val Phe Ile Leu Leu Tyr Val 450 455 460 Val Ala Arg Ile Val Ile Ala Val Arg Tyr Arg Tyr Gln Gly Ser Asn 465 470 475 480 Asn Lys Arg Ile Tyr Asn Asp Ile Glu Met Ser Arg Phe Arg Lys 485 490 495 <210> 48 <211> 495 <212> PRT <213> Artificial Sequence <220> <223> Vesicular Stomatitis Cocal Virus Glycoprotein H22N T422M <400> 48 Lys Phe Ser Ile Val Phe Pro Gln Ser Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Ser Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Leu Gly Ile Thr Met Lys Val Lys Met Pro Lys Thr 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Ile Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Ile Gln Pro Thr Ser Glu Gln Cys Lys Glu Ser Ile 85 90 95 Lys Gln Thr Lys Gln Gly Thr Trp Met Ser Pro Gly Phe Pro Pro Gln 100 105 110 Asn Cys Gly Tyr Ala Thr Val Thr Asp Ser Val Ala Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Phe Pro Asn Gly Lys Cys Glu Thr Glu Glu Cys Glu Thr 145 150 155 160 Val His Asn Ser Thr Val Trp Tyr Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Thr Leu Val Asp Thr Glu Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Lys Glu Ser Ile Gly Lys Pro Asn Thr Gly Tyr Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Lys Gly Asp Lys Val Cys Lys Met Asn Tyr Cys 210 215 220 Lys His Ala Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Phe Val 225 230 235 240 Asp Gln Asp Val Tyr Ala Ala Ala Lys Leu Pro Glu Cys Pro Val Gly 245 250 255 Ala Thr Ile Ser Ala Pro Thr Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Leu Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ser Lys Gln Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Ile Asp Ile Asp 325 330 335 Asn Pro Ile Ile Ser Lys Met Val Gly Lys Ile Ser Gly Ser Gln Thr 340 345 350 Glu Arg Glu Leu Trp Thr Glu Trp Phe Pro Tyr Glu Gly Val Glu Ile 355 360 365 Gly Pro Asn Gly Ile Leu Lys Thr Pro Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Phe Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Thr Ser 385 390 395 400 Gln Ala Glu Val Phe Glu His Pro His Leu Ala Glu Ala Pro Lys Gln 405 410 415 Leu Pro Glu Glu Glu Met Leu Phe Phe Gly Asp Thr Gly Ile Ser Lys 420 425 430 Asn Pro Val Glu Leu Ile Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Val Val Thr Phe Phe Phe Ala Ile Gly Val Phe Ile Leu Leu Tyr Val 450 455 460 Val Ala Arg Ile Val Ile Ala Val Arg Tyr Arg Tyr Gln Gly Ser Asn 465 470 475 480 Asn Lys Arg Ile Tyr Asn Asp Ile Glu Met Ser Arg Phe Arg Lys 485 490 495 <210> 49 <211> 495 <212> PRT <213> Artificial Sequence <220> <223> Vesicular Stomatitis Cocal Virus Glycoprotein H22N T422V <400> 49 Lys Phe Ser Ile Val Phe Pro Gln Ser Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ser Ser Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Gln Asn Trp 20 25 30 His Asn Asp Leu Leu Gly Ile Thr Met Lys Val Lys Met Pro Lys Thr 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Ile Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Ile Gln Pro Thr Ser Glu Gln Cys Lys Glu Ser Ile 85 90 95 Lys Gln Thr Lys Gln Gly Thr Trp Met Ser Pro Gly Phe Pro Pro Gln 100 105 110 Asn Cys Gly Tyr Ala Thr Val Thr Asp Ser Val Ala Val Val Val Gln 115 120 125 Ala Thr Pro His His Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Ile 130 135 140 Asp Ser Gln Phe Pro Asn Gly Lys Cys Glu Thr Glu Glu Cys Glu Thr 145 150 155 160 Val His Asn Ser Thr Val Trp Tyr Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Thr Leu Val Asp Thr Glu Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Lys Glu Ser Ile Gly Lys Pro Asn Thr Gly Tyr Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Lys Gly Asp Lys Val Cys Lys Met Asn Tyr Cys 210 215 220 Lys His Ala Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Phe Val 225 230 235 240 Asp Gln Asp Val Tyr Ala Ala Ala Lys Leu Pro Glu Cys Pro Val Gly 245 250 255 Ala Thr Ile Ser Ala Pro Thr Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Leu Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ser Lys Gln Pro Val Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ala Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Ile Asp Ile Asp 325 330 335 Asn Pro Ile Ile Ser Lys Met Val Gly Lys Ile Ser Gly Ser Gln Thr 340 345 350 Glu Arg Glu Leu Trp Thr Glu Trp Phe Pro Tyr Glu Gly Val Glu Ile 355 360 365 Gly Pro Asn Gly Ile Leu Lys Thr Pro Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Phe Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Lys Thr Ser 385 390 395 400 Gln Ala Glu Val Phe Glu His Pro His Leu Ala Glu Ala Pro Lys Gln 405 410 415 Leu Pro Glu Glu Glu Val Leu Phe Phe Gly Asp Thr Gly Ile Ser Lys 420 425 430 Asn Pro Val Glu Leu Ile Glu Gly Trp Phe Ser Ser Trp Lys Ser Thr 435 440 445 Val Val Thr Phe Phe Phe Ala Ile Gly Val Phe Ile Leu Leu Tyr Val 450 455 460 Val Ala Arg Ile Val Ile Ala Val Arg Tyr Arg Tyr Gln Gly Ser Asn 465 470 475 480 Asn Lys Arg Ile Tyr Asn Asp Ile Glu Met Ser Arg Phe Arg Lys 485 490 495 <210> 50 <211> 496 <212> PRT <213> Artificial Sequence <220> <223> Vesicular stomatitis Morreton virus glycoprotein Q22N <400> 50 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ala Asn Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Gly Leu Ile Gly Thr Ser Leu Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Val Thr His 65 70 75 80 Ser Ile Lys Ser Met Ile Pro Thr Val Asp Gln Cys Lys Glu Ser Ile 85 90 95 Ala Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Ser Val Thr Asp Ala Glu Ala Val Ile Val Lys 115 120 125 Ala Thr Pro His Gln Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Pro Thr Gly Lys Cys Asn Lys Asp Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Leu Thr Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Asn Gly Asp Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Ile Tyr Asn Asp Ala Lys Phe Pro Asp Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ala Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala His Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ser Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Gly Pro Ile Ile Pro Gln Met Arg Gly Val Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Thr Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Ala Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Ile Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Thr Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Gly Trp Lys Ser Thr 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Val Ile Gly Leu Tyr Leu 450 455 460 Val Leu Arg Ile Gly Ile Ala Leu Cys Ile Lys Cys Arg Val Gln Glu 465 470 475 480 Lys Arg Pro Lys Ile Tyr Thr Asp Val Glu Met Asn Arg Leu Asp Arg 485 490 495 <210> 51 <211> 496 <212> PRT <213> Artificial sequence <220> <223> Vesicular stomatitis Morreton virus glycoprotein T422I <400> 51 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ala Asn Tyr Gln Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Gly Leu Ile Gly Thr Ser Leu Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Val Thr His 65 70 75 80 Ser Ile Lys Ser Met Ile Pro Thr Val Asp Gln Cys Lys Glu Ser Ile 85 90 95 Ala Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Ser Val Thr Asp Ala Glu Ala Val Ile Val Lys 115 120 125 Ala Thr Pro His Gln Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Pro Thr Gly Lys Cys Asn Lys Asp Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Leu Thr Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Asn Gly Asp Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Ile Tyr Asn Asp Ala Lys Phe Pro Asp Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ala Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala His Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ser Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Gly Pro Ile Ile Pro Gln Met Arg Gly Val Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Thr Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Ala Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Ile Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Ile Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Gly Trp Lys Ser Thr 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Val Ile Gly Leu Tyr Leu 450 455 460 Val Leu Arg Ile Gly Ile Ala Leu Cys Ile Lys Cys Arg Val Gln Glu 465 470 475 480 Lys Arg Pro Lys Ile Tyr Thr Asp Val Glu Met Asn Arg Leu Asp Arg 485 490 495 <210> 52 <211> 496 <212> PRT <213> Artificial Sequence <220> <223> Vesicular Stomatitis Morreton Virus Glycoprotein T422L <400> 52 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ala Asn Tyr Gln Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Gly Leu Ile Gly Thr Ser Leu Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Val Thr His 65 70 75 80 Ser Ile Lys Ser Met Ile Pro Thr Val Asp Gln Cys Lys Glu Ser Ile 85 90 95 Ala Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Ser Val Thr Asp Ala Glu Ala Val Ile Val Lys 115 120 125 Ala Thr Pro His Gln Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Pro Thr Gly Lys Cys Asn Lys Asp Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Leu Thr Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Asn Gly Asp Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Ile Tyr Asn Asp Ala Lys Phe Pro Asp Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ala Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala His Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ser Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Gly Pro Ile Ile Pro Gln Met Arg Gly Val Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Thr Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Ala Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Ile Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Leu Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Gly Trp Lys Ser Thr 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Val Ile Gly Leu Tyr Leu 450 455 460 Val Leu Arg Ile Gly Ile Ala Leu Cys Ile Lys Cys Arg Val Gln Glu 465 470 475 480 Lys Arg Pro Lys Ile Tyr Thr Asp Val Glu Met Asn Arg Leu Asp Arg 485 490 495 <210> 53 <211> 496 <212> PRT <213> Artificial sequence <220> <223> Vesicular stomatitis Morreton virus glycoprotein T422F <400> 53 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ala Asn Tyr Gln Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Gly Leu Ile Gly Thr Ser Leu Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Val Thr His 65 70 75 80 Ser Ile Lys Ser Met Ile Pro Thr Val Asp Gln Cys Lys Glu Ser Ile 85 90 95 Ala Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Ser Val Thr Asp Ala Glu Ala Val Ile Val Lys 115 120 125 Ala Thr Pro His Gln Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Pro Thr Gly Lys Cys Asn Lys Asp Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Leu Thr Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Asn Gly Asp Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Ile Tyr Asn Asp Ala Lys Phe Pro Asp Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ala Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala His Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ser Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Gly Pro Ile Ile Pro Gln Met Arg Gly Val Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Thr Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Ala Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Ile Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Phe Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Gly Trp Lys Ser Thr 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Val Ile Gly Leu Tyr Leu 450 455 460 Val Leu Arg Ile Gly Ile Ala Leu Cys Ile Lys Cys Arg Val Gln Glu 465 470 475 480 Lys Arg Pro Lys Ile Tyr Thr Asp Val Glu Met Asn Arg Leu Asp Arg 485 490 495 <210> 54 <211> 496 <212> PRT <213> Artificial Sequence <220> <223> Vesicular stomatitis Morreton virus glycoprotein T422M <400> 54 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ala Asn Tyr Gln Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Gly Leu Ile Gly Thr Ser Leu Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Val Thr His 65 70 75 80 Ser Ile Lys Ser Met Ile Pro Thr Val Asp Gln Cys Lys Glu Ser Ile 85 90 95 Ala Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Ser Val Thr Asp Ala Glu Ala Val Ile Val Lys 115 120 125 Ala Thr Pro His Gln Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Pro Thr Gly Lys Cys Asn Lys Asp Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Leu Thr Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Asn Gly Asp Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Ile Tyr Asn Asp Ala Lys Phe Pro Asp Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ala Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala His Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ser Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Gly Pro Ile Ile Pro Gln Met Arg Gly Val Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Thr Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Ala Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Ile Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Met Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Gly Trp Lys Ser Thr 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Val Ile Gly Leu Tyr Leu 450 455 460 Val Leu Arg Ile Gly Ile Ala Leu Cys Ile Lys Cys Arg Val Gln Glu 465 470 475 480 Lys Arg Pro Lys Ile Tyr Thr Asp Val Glu Met Asn Arg Leu Asp Arg 485 490 495 <210> 55 <211> 496 <212> PRT <213> Artificial Sequence <220> <223> Vesicular stomatitis Morreton virus glycoprotein T422V <400> 55 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ala Asn Tyr Gln Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Gly Leu Ile Gly Thr Ser Leu Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Val Thr His 65 70 75 80 Ser Ile Lys Ser Met Ile Pro Thr Val Asp Gln Cys Lys Glu Ser Ile 85 90 95 Ala Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Ser Val Thr Asp Ala Glu Ala Val Ile Val Lys 115 120 125 Ala Thr Pro His Gln Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Pro Thr Gly Lys Cys Asn Lys Asp Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Leu Thr Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Asn Gly Asp Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Ile Tyr Asn Asp Ala Lys Phe Pro Asp Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ala Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala His Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ser Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Gly Pro Ile Ile Pro Gln Met Arg Gly Val Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Thr Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Ala Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Ile Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Val Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Gly Trp Lys Ser Thr 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Val Ile Gly Leu Tyr Leu 450 455 460 Val Leu Arg Ile Gly Ile Ala Leu Cys Ile Lys Cys Arg Val Gln Glu 465 470 475 480 Lys Arg Pro Lys Ile Tyr Thr Asp Val Glu Met Asn Arg Leu Asp Arg 485 490 495 <210> 56 <211> 496 <212> PRT <213> Artificial sequence <220> <223> Vesicular stomatitis Morreton virus glycoprotein Q22N T422I <400> 56 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ala Asn Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Gly Leu Ile Gly Thr Ser Leu Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Val Thr His 65 70 75 80 Ser Ile Lys Ser Met Ile Pro Thr Val Asp Gln Cys Lys Glu Ser Ile 85 90 95 Ala Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Ser Val Thr Asp Ala Glu Ala Val Ile Val Lys 115 120 125 Ala Thr Pro His Gln Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Pro Thr Gly Lys Cys Asn Lys Asp Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Leu Thr Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Asn Gly Asp Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Ile Tyr Asn Asp Ala Lys Phe Pro Asp Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ala Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala His Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ser Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Gly Pro Ile Ile Pro Gln Met Arg Gly Val Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Thr Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Ala Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Ile Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Ile Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Gly Trp Lys Ser Thr 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Val Ile Gly Leu Tyr Leu 450 455 460 Val Leu Arg Ile Gly Ile Ala Leu Cys Ile Lys Cys Arg Val Gln Glu 465 470 475 480 Lys Arg Pro Lys Ile Tyr Thr Asp Val Glu Met Asn Arg Leu Asp Arg 485 490 495 <210> 57 <211> 496 <212> PRT <213> Artificial Sequence <220> <223> Vesicular stomatitis Morreton virus glycoprotein Q22N T422L <400> 57 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ala Asn Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Gly Leu Ile Gly Thr Ser Leu Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Val Thr His 65 70 75 80 Ser Ile Lys Ser Met Ile Pro Thr Val Asp Gln Cys Lys Glu Ser Ile 85 90 95 Ala Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Ser Val Thr Asp Ala Glu Ala Val Ile Val Lys 115 120 125 Ala Thr Pro His Gln Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Pro Thr Gly Lys Cys Asn Lys Asp Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Leu Thr Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Asn Gly Asp Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Ile Tyr Asn Asp Ala Lys Phe Pro Asp Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ala Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala His Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ser Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Gly Pro Ile Ile Pro Gln Met Arg Gly Val Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Thr Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Ala Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Ile Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Leu Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Gly Trp Lys Ser Thr 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Val Ile Gly Leu Tyr Leu 450 455 460 Val Leu Arg Ile Gly Ile Ala Leu Cys Ile Lys Cys Arg Val Gln Glu 465 470 475 480 Lys Arg Pro Lys Ile Tyr Thr Asp Val Glu Met Asn Arg Leu Asp Arg 485 490 495 <210> 58 <211> 496 <212> PRT <213> Synthetic sequence <220> <223> Vesicular stomatitis Morreton virus glycoprotein Q22N T422F <400> 58 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ala Asn Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Gly Leu Ile Gly Thr Ser Leu Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Val Thr His 65 70 75 80 Ser Ile Lys Ser Met Ile Pro Thr Val Asp Gln Cys Lys Glu Ser Ile 85 90 95 Ala Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Ser Val Thr Asp Ala Glu Ala Val Ile Val Lys 115 120 125 Ala Thr Pro His Gln Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Pro Thr Gly Lys Cys Asn Lys Asp Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Leu Thr Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Asn Gly Asp Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Ile Tyr Asn Asp Ala Lys Phe Pro Asp Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ala Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala His Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ser Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Gly Pro Ile Ile Pro Gln Met Arg Gly Val Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Thr Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Ala Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Ile Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Phe Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Gly Trp Lys Ser Thr 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Val Ile Gly Leu Tyr Leu 450 455 460 Val Leu Arg Ile Gly Ile Ala Leu Cys Ile Lys Cys Arg Val Gln Glu 465 470 475 480 Lys Arg Pro Lys Ile Tyr Thr Asp Val Glu Met Asn Arg Leu Asp Arg 485 490 495 <210> 59 <211> 496 <212> PRT <213> Artificial Sequence <220> <223> Vesicular stomatitis Morreton virus glycoprotein Q22N T422M <400> 59 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ala Asn Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Gly Leu Ile Gly Thr Ser Leu Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Val Thr His 65 70 75 80 Ser Ile Lys Ser Met Ile Pro Thr Val Asp Gln Cys Lys Glu Ser Ile 85 90 95 Ala Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Ser Val Thr Asp Ala Glu Ala Val Ile Val Lys 115 120 125 Ala Thr Pro His Gln Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Pro Thr Gly Lys Cys Asn Lys Asp Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Leu Thr Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Asn Gly Asp Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Ile Tyr Asn Asp Ala Lys Phe Pro Asp Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ala Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala His Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ser Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Gly Pro Ile Ile Pro Gln Met Arg Gly Val Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Thr Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Ala Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Ile Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Met Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Gly Trp Lys Ser Thr 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Val Ile Gly Leu Tyr Leu 450 455 460 Val Leu Arg Ile Gly Ile Ala Leu Cys Ile Lys Cys Arg Val Gln Glu 465 470 475 480 Lys Arg Pro Lys Ile Tyr Thr Asp Val Glu Met Asn Arg Leu Asp Arg 485 490 495 <210> 60 <211> 496 <212> PRT <213> Artificial Sequence <220> <223> Vesicular stomatitis Morreton virus glycoprotein Q22N T422V <400> 60 Lys Phe Thr Ile Val Phe Pro His Asn Gln Lys Gly Asn Trp Lys Asn 1 5 10 15 Val Pro Ala Asn Tyr Asn Tyr Cys Pro Ser Ser Ser Asp Leu Asn Trp 20 25 30 His Asn Gly Leu Ile Gly Thr Ser Leu Gln Val Lys Met Pro Lys Ser 35 40 45 His Lys Ala Ile Gln Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Phe Arg Trp Tyr Gly Pro Lys Tyr Val Thr His 65 70 75 80 Ser Ile Lys Ser Met Ile Pro Thr Val Asp Gln Cys Lys Glu Ser Ile 85 90 95 Ala Gln Thr Lys Gln Gly Thr Trp Leu Asn Pro Gly Phe Pro Pro Gln 100 105 110 Ser Cys Gly Tyr Ala Ser Val Thr Asp Ala Glu Ala Val Ile Val Lys 115 120 125 Ala Thr Pro His Gln Val Leu Val Asp Glu Tyr Thr Gly Glu Trp Val 130 135 140 Asp Ser Gln Phe Pro Thr Gly Lys Cys Asn Lys Asp Ile Cys Pro Thr 145 150 155 160 Val His Asn Ser Thr Thr Trp His Ser Asp Tyr Lys Val Thr Gly Leu 165 170 175 Cys Asp Ala Asn Leu Ile Ser Met Asp Ile Thr Phe Phe Ser Glu Asp 180 185 190 Gly Lys Leu Thr Ser Leu Gly Lys Glu Gly Thr Gly Phe Arg Ser Asn 195 200 205 Tyr Phe Ala Tyr Glu Asn Gly Asp Lys Ala Cys Arg Met Gln Tyr Cys 210 215 220 Lys His Trp Gly Val Arg Leu Pro Ser Gly Val Trp Phe Glu Met Ala 225 230 235 240 Asp Lys Asp Ile Tyr Asn Asp Ala Lys Phe Pro Asp Cys Pro Glu Gly 245 250 255 Ser Ser Ile Ala Ala Pro Ser Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Gln Asp Val Glu Arg Ile Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Ile Arg Ala His Leu Pro Ile Ser Pro Val Asp Leu Ser Tyr 290 295 300 Leu Ser Pro Lys Asn Pro Gly Thr Gly Pro Ala Phe Thr Ile Ile Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Glu Thr Arg Tyr Ile Arg Val Asp Ile Ala 325 330 335 Gly Pro Ile Ile Pro Gln Met Arg Gly Val Ile Ser Gly Thr Thr Thr 340 345 350 Glu Arg Glu Leu Trp Thr Asp Trp Tyr Pro Tyr Glu Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Ala Thr Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Met Leu Asp Ser Asp Leu His Ile Ser Ser 385 390 395 400 Lys Ala Gln Val Phe Glu His Pro His Ile Gln Asp Ala Ala Ser Gln 405 410 415 Leu Pro Asp Asp Glu Val Leu Phe Phe Gly Asp Thr Gly Leu Ser Lys 420 425 430 Asn Pro Ile Glu Leu Val Glu Gly Trp Phe Ser Gly Trp Lys Ser Thr 435 440 445 Ile Ala Ser Phe Phe Phe Ile Ile Gly Leu Val Ile Gly Leu Tyr Leu 450 455 460 Val Leu Arg Ile Gly Ile Ala Leu Cys Ile Lys Cys Arg Val Gln Glu 465 470 475 480 Lys Arg Pro Lys Ile Tyr Thr Asp Val Glu Met Asn Arg Leu Asp Arg 485 490 495 <210> 61 <211> 494 <212> PRT <213> Artificial sequence <220> <223> Vesicular stomatitis Alagoa virus glycoprotein R22N <400> 61 Lys Phe Thr Ile Val Phe Pro Gln Ser Gln Lys Gly Asp Trp Lys Asp 1 5 10 15 Val Pro Pro Asn Tyr Asn Tyr Cys Pro Ser Ser Ala Asp Gln Asn Trp 20 25 30 His Gly Asp Leu Leu Gly Val Asn Ile Arg Ala Lys Met Pro Lys Val 35 40 45 His Lys Ala Ile Lys Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Tyr Arg Trp Tyr Gly Pro Gln Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Phe Ile Pro Thr Lys Ala Gln Cys Glu Glu Ser Ile 85 90 95 Lys Gln Thr Lys Glu Gly Val Trp Ile Asn Pro Gly Phe Pro Pro Lys 100 105 110 Asn Cys Gly Tyr Ala Ser Val Ser Asp Ala Glu Ser Ile Ile Val Gln 115 120 125 Ala Thr Ala His Ser Val Met Ile Asp Glu Tyr Ser Gly Asp Trp Leu 130 135 140 Asp Ser Gln Phe Pro Thr Gly Arg Cys Thr Gly Ser Thr Cys Glu Thr 145 150 155 160 Ile His Asn Ser Thr Leu Trp Tyr Ala Asp Tyr Gln Val Thr Gly Leu 165 170 175 Cys Asp Ser Ala Leu Val Ser Thr Glu Val Thr Phe Tyr Ser Glu Asp 180 185 190 Gly Leu Met Thr Ser Ile Gly Arg Gln Asn Thr Gly Tyr Arg Ser Asn 195 200 205 Tyr Phe Pro Tyr Glu Lys Gly Ala Ala Ala Cys Arg Met Lys Tyr Cys 210 215 220 Thr His Glu Gly Ile Arg Leu Pro Ser Gly Val Trp Phe Glu Met Val 225 230 235 240 Asp Lys Glu Leu Leu Glu Ser Val Gln Met Pro Glu Cys Pro Ala Gly 245 250 255 Leu Thr Ile Ser Ala Pro Thr Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Leu Asp Val Glu Arg Met Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Val His Ser Gly Leu Pro Ile Ser Pro Val Asp Leu Gly Tyr 290 295 300 Ile Ala Pro Lys Asn Pro Gly Ala Gly Pro Ala Phe Thr Ile Val Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Asp Thr Arg Tyr Leu Arg Ile Asp Ile Glu 325 330 335 Gly Pro Val Leu Lys Lys Met Thr Gly Lys Val Ser Gly Thr Pro Thr 340 345 350 Lys Arg Glu Leu Trp Thr Glu Trp Phe Pro Tyr Asp Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Pro Glu Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Leu Leu Asp Ser Asp Leu Gln Lys Thr Ser 385 390 395 400 Gln Ala Glu Val Phe His His Pro Gln Ile Ala Glu Ala Val Gln Lys 405 410 415 Leu Pro Asp Asp Glu Thr Leu Phe Phe Gly Asp Thr Gly Ile Ser Lys 420 425 430 Asn Pro Val Glu Val Ile Glu Gly Trp Phe Ser Asn Trp Arg Ser Ser 435 440 445 Val Met Ala Ile Val Phe Ala Ile Leu Leu Leu Val Ile Thr Val Leu 450 455 460 Met Val Arg Leu Cys Val Ala Phe Arg His Phe Cys Cys Gln Lys Arg 465 470 475 480 His Lys Ile Tyr Asn Asp Leu Glu Met Asn Gln Leu Arg Arg 485 490 <210> 62 <211> 494 <212> PRT <213> Artificial Sequence <220> <223> Vesicular stomatitis Alagoa virus glycoprotein T422I <400> 62 Lys Phe Thr Ile Val Phe Pro Gln Ser Gln Lys Gly Asp Trp Lys Asp 1 5 10 15 Val Pro Pro Asn Tyr Arg Tyr Cys Pro Ser Ser Ala Asp Gln Asn Trp 20 25 30 His Gly Asp Leu Leu Gly Val Asn Ile Arg Ala Lys Met Pro Lys Val 35 40 45 His Lys Ala Ile Lys Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Tyr Arg Trp Tyr Gly Pro Gln Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Phe Ile Pro Thr Lys Ala Gln Cys Glu Glu Ser Ile 85 90 95 Lys Gln Thr Lys Glu Gly Val Trp Ile Asn Pro Gly Phe Pro Pro Lys 100 105 110 Asn Cys Gly Tyr Ala Ser Val Ser Asp Ala Glu Ser Ile Ile Val Gln 115 120 125 Ala Thr Ala His Ser Val Met Ile Asp Glu Tyr Ser Gly Asp Trp Leu 130 135 140 Asp Ser Gln Phe Pro Thr Gly Arg Cys Thr Gly Ser Thr Cys Glu Thr 145 150 155 160 Ile His Asn Ser Thr Leu Trp Tyr Ala Asp Tyr Gln Val Thr Gly Leu 165 170 175 Cys Asp Ser Ala Leu Val Ser Thr Glu Val Thr Phe Tyr Ser Glu Asp 180 185 190 Gly Leu Met Thr Ser Ile Gly Arg Gln Asn Thr Gly Tyr Arg Ser Asn 195 200 205 Tyr Phe Pro Tyr Glu Lys Gly Ala Ala Ala Cys Arg Met Lys Tyr Cys 210 215 220 Thr His Glu Gly Ile Arg Leu Pro Ser Gly Val Trp Phe Glu Met Val 225 230 235 240 Asp Lys Glu Leu Leu Glu Ser Val Gln Met Pro Glu Cys Pro Ala Gly 245 250 255 Leu Thr Ile Ser Ala Pro Thr Gln Thr Ser Val Asp Val Ser Leu Ile 260 265 270 Leu Asp Val Glu Arg Met Leu Asp Tyr Ser Leu Cys Gln Glu Thr Trp 275 280 285 Ser Lys Val His Ser Gly Leu Pro Ile Ser Pro Val Asp Leu Gly Tyr 290 295 300 Ile Ala Pro Lys Asn Pro Gly Ala Gly Pro Ala Phe Thr Ile Val Asn 305 310 315 320 Gly Thr Leu Lys Tyr Phe Asp Thr Arg Tyr Leu Arg Ile Asp Ile Glu 325 330 335 Gly Pro Val Leu Lys Lys Met Thr Gly Lys Val Ser Gly Thr Pro Thr 340 345 350 Lys Arg Glu Leu Trp Thr Glu Trp Phe Pro Tyr Asp Asp Val Glu Ile 355 360 365 Gly Pro Asn Gly Val Leu Lys Thr Pro Glu Gly Tyr Lys Phe Pro Leu 370 375 380 Tyr Met Ile Gly His Gly Leu Leu Asp Ser Asp Leu Gln Lys Thr Ser 385 390 395 400 Gln Ala Glu Val Phe His His Pro Gln Ile Ala Glu Ala Val Gln Lys 405 410 415 Leu Pro Asp Asp Glu Ile Leu Phe Phe Gly Asp Thr Gly Ile Ser Lys 420 425 430 Asn Pro Val Glu Val Ile Glu Gly Trp Phe Ser Asn Trp Arg Ser Ser 435 440 445 Val Met Ala Ile Val Phe Ala Ile Leu Leu Leu Val Ile Thr Val Leu 450 455 460 Met Val Arg Leu Cys Val Ala Phe Arg His Phe Cys Cys Gln Lys Arg 465 470 475 480 His Lys Ile Tyr Asn Asp Leu Glu Met Asn Gln Leu Arg Arg 485 490 <210> 63 <211> 494 <212> PRT <213> Artificial Sequence <220> <223> Vesicular stomatitis Alagoa virus glycoprotein T422L <400> 63 Lys Phe Thr Ile Val Phe Pro Gln Ser Gln Lys Gly Asp Trp Lys Asp 1 5 10 15 Val Pro Pro Asn Tyr Arg Tyr Cys Pro Ser Ser Ala Asp Gln Asn Trp 20 25 30 His Gly Asp Leu Leu Gly Val Asn Ile Arg Ala Lys Met Pro Lys Val 35 40 45 His Lys Ala Ile Lys Ala Asp Gly Trp Met Cys His Ala Ala Lys Trp 50 55 60 Val Thr Thr Cys Asp Tyr Arg Trp Tyr Gly Pro Gln Tyr Ile Thr His 65 70 75 80 Ser Ile His Ser Phe Ile Pro Thr Lys Ala Gln Cys Glu Glu Ser Ile 85 90 95 Lys Gln Thr Lys Glu Gly Val Trp Ile Asn Pro Gly Phe Pro Pro Lys 100 105 110 Asn Cys Gly Tyr Ala Ser Val Ser Asp Ala Glu Ser Ile Ile Val Gln 115 120 125 Ala Thr Ala His Ser Val Met Ile Asp Glu Tyr Ser Gly Asp Trp Leu 130 135 140 Asp Ser Gln Phe Pro Thr Gly Arg Cys Thr Gly Ser Thr Cys Glu Thr 145 150 155 160 Ile His Asn Ser Thr Leu Trp Tyr Ala Asp Tyr Gln Val Thr Gly Leu 165 170 175 Cys Asp Ser Ala Leu Val Ser Thr Glu Val Thr Phe Tyr Ser Glu Asp 180 185 1...

Claims

1. A mutant polypeptide comprising the amino acid sequence of the glycoprotein G extracellular domain of a vesicular stomatitis virus strain, wherein the extracellular domain consists of: The amino acid sequence listed in SEQ ID NO:2, wherein the histidine (H) amino acid residue at position 22 of the sequence is substituted with an asparagine (N) amino acid residue, and the serine (S) amino acid residue at position 422 is substituted with an isoleucine (I), phenylalanine (F), methionine (M), leucine (L) or valine (V) amino acid residue; or the histidine (H) amino acid residue at position 407 of the sequence is substituted with an alanine (A) amino acid residue, and the serine (S) amino acid residue at position 422 is substituted with an isoleucine (I), phenylalanine (F), methionine (M), leucine (L) or valine (V) amino acid residue.

2. A fusion polypeptide comprising a mutant polypeptide according to claim 1 and an additional polypeptide, wherein the additional polypeptide is inserted at: the N-terminus of the mutant polypeptide, or between any two consecutive amino acids in the region corresponding to positions 192 to 202, 240 to 257, 347 to 353, 364 to 366 or 376 to 379 of SEQ ID NO:

2.

3. The fusion polypeptide according to claim 2, wherein the additional polypeptide is inserted at: the N-terminus of the mutant polypeptide, or between amino acids 351 and 352 of SEQ ID NO:

2.

4. A fusion polypeptide according to claim 2 or 3, wherein the additional polypeptide is at least a part of a ligand of a cell receptor.

5. The fusion polypeptide of claim 4, wherein the additional polypeptide is an antibody or a functional antibody fragment.

6. The fusion polypeptide according to claim 5, wherein the antibody or functional antibody fragment is an anti-HER2, anti-MUC18, anti-PD-1, anti-EGFR, anti-CD20 or anti-CD52 antibody or functional antibody fragment.

7. The fusion polypeptide according to claim 5 or 6, wherein the antibody or functional antibody fragment is a nanobody.

8. A nucleic acid molecule encoding a mutant polypeptide according to claim 1 or a fusion polypeptide according to any one of claims 2 to 7.

9. A vector comprising at least one nucleic acid molecule according to claim 8, or expressing a mutant polypeptide according to claim 1 or a fusion polypeptide according to any one of claims 2 to 7.

10. The vector according to claim 9, which is a viral vector.

11. The vector according to claim 10, wherein the viral vector is a vesicular stomatitis virus vector.

12. The vector of claim 10, wherein the viral vector is in the form of infectious viral particles.

13. A host cell containing or expressing the mutant polypeptide according to claim 1 or the fusion polypeptide according to any one of claims 2 to 7, or containing the nucleic acid molecule according to claim 8, or containing the vector according to any one of claims 9 to 12.

14. A composition comprising the mutant polypeptide according to claim 1, the fusion polypeptide according to any one of claims 2 to 7, the nucleic acid molecule according to claim 8, the vector according to any one of claims 9 to 12, the host cell according to claim 13, or any combination thereof.

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