RU2820522C2 - Multimerizing polypeptides derived from domain with roll-type pentone base of adenovirus - Google Patents

Abstract

FIELD: biotechnology.

SUBSTANCE: described is a polypeptide for presentation of oligopeptide, polypeptide, protein and / or protein complex, having structure A-L₁-B-L₂-C (formula (I)), where A is the N-terminal amino acid portion of the adenovirus pentone base protein, B is the adenovirus pentone base amino acid portion, C is the adenovirus pentone base C-terminal amino acid portion, where B is an amino acid region located between A and C in the sequence of said adenovirus pentone base, where A, B and C form a roll-type domain (jellyrollfold) of said pentonaadenovirus base protein, L₁ and L₂ are independently selected from a group consisting of an oligopeptide, a polypeptide, a protein and a protein complex, where said oligopeptide, polypeptide, protein and protein complex, respectively, are either substantially non-adenoviral, or if adenoviral, A-L₁-B-L₂-C forms a pentone base chimera, where A, B and C form a roll-type domain of the adenovirus pentone base of one adenovirus subtype, and L₁ and L₂ form a "crown" domain of a pentone base of adenovirus subtype different from the subtype adenovirus roll-type domain. Described is a nucleic acid coding said polypeptide. Disclosed is nucleic acid for producing nucleic acid by inserting nucleotide sequences coding L₁ and L₂ containing a sequence having following common 5'-a-is₁-l₁-is₂-b-is₃-l₂-is₄-c-3', where a is a nucleotide sequence coding A of formula (I), b is a nucleotide sequence coding B of general formula (I), c is a nucleotide sequence coding C of general formula (I), and l₁, l₂ each represents a nucleotide sequence, is 1 to is 4 each independently represents a nucleotide sequence containing at least one insertion site. Disclosed vector to obtain said polypeptide. Described is a recombinant host cell for producing said polypeptide. Described is a pentameric polypeptide complex for presenting an oligopeptide, a polypeptide, a protein and/or a protein complex, where A-L₁-B-L₂-C forms a pentone base chimera and where A, B and C form roll-type domainadenovirus pentone base of one adenovirus subtype, and L₁ and L₂ form a "crown" domain of adenovirus subtype of adenovirus subtype different from the adenovirus subtype of the roll-type domain. Disclosed is a virus-like particle (VLP) for the presentation of an oligopeptide, a protein and / or a protein complex containing 12 pentameric complexes. Disclosed is a pharmaceutical composition for the presentation of an oligopeptide, a protein and/or a protein complex containing a polypeptide, a nucleic acid, a vector, a host cell or HPV together with at least one pharmaceutically acceptable carrier, excipient and/or diluent. Disclosed is a method of producing a polypeptide. Polypeptide frameworks according to the invention are intended for optimal presentation of peptides, polypeptide sequences, protein domains, proteins and protein complexes consisting of two, several or many subunits.

EFFECT: such oligopeptides, polypeptide sequences, protein domains and proteins represented by polypeptide scaffolds according to the present invention may include antigenic particles which stimulate the immune system to elicit an immune response, for example, for vaccination purposes, or for producing antibodies or other binding molecules in a cell culture, or in a test tube.

36 cl, 5 dwg, 5 tbl, 1 ex

Description

The present invention relates to the design and production of new polypeptide scaffolds for optimal presentation of oligopeptides, polypeptide sequences, protein domains, proteins and/or protein complexes consisting of two, several or many subunits. Such oligopeptides, polypeptide sequences, protein domains and/or proteins represented by the polypeptide scaffolds of the present invention may include antigenic particles that stimulate the immune system to elicit an immune response, for example, for vaccination or for the production of antibodies or other binding molecules in cell culture , either in vivo or in vitro in vitro. In a preferred embodiment, the polypeptides of the present invention are assembled into virus-like particles (VLPs) optimized to present antigens useful in the context of vaccination against infectious agents or tumors.

A prerequisite for the successful development of a protein scaffold for the presentation of oligopeptides, polypeptide sequences, protein domains, proteins and/or protein complexes is a compact, stable multimerization domain, which can include modalities that are open and flexible loop structures that can accommodate such oligopeptides, polypeptide sequences , protein domains, proteins and/or protein complexes. Preferably, such display particles may be immunogenic antigens that are presented to the immune system. Penton base proteins (protomers) from a number of adenovirus (Ag) serotypes assemble into pentamers, which then form dodecahedrons resembling virus-like particles. Unlike a live virus, they do not carry genetic material, so such HPVs are useful from a safety point of view.

Adenovirus is one of the most commonly used gene therapy vectors in humans. The adenovirus envelope is predominantly composed of two different types of proteins, the hexon protein and the penton base protein, the latter forming pentameric assemblies to which fibrils characteristic of the virus are attached. The penton base proteins of some adenovirus serotypes have been shown to spontaneously self-assemble into a multimeric superstructure when expressed recombinantly in the absence of other adenoviral components. This superstructure is a dodecamer formed by a total of 60 adenovirus base proteins arranged in twelve identical copies of a pentameric “crown” assembly (Fig. 1). The adenovirus base protein itself has a two-domain architecture in which one domain is a beta-barrel connected to a second domain stabilized by alpha-helices (Fig. 1B). The former mediates multimerization into the dodecahedron, as confirmed by mutation studies, while the latter presents extensive solvent loops on the surface of the dodecahedron. Such loops are extremely variable in length and sequence content among different adenovirus serotypes, while the base protein residue is highly conserved across species. The adenovirus dodecahedron provides a very versatile display scaffold, for example for immunogenic peptides that can be inserted into loops to replace naturally occurring sequences. Thus, literally hundreds of heterologous peptides can effectively map onto a single dodecahedron if all insertion sites are occupied. The dodecahedron can be produced recombinantly in very large quantities, is extremely stable and can be stored at ambient temperatures indefinitely. Taking advantage of such highly advantageous characteristics, synthetic dodecahedron-based particles exhibiting immunogenic peptides in their open loops have been developed for potential applications including oncoimmunology and emerging infectious diseases.

WO 2017167988 A1 discloses synthetic adenovirus dodecahedrons that facilitate epitope insertion into open loops, and also discloses the production of an adenovirus base protein.

The objective of the present invention is to provide a new system for presenting antigens or other cargo through protein scaffolds that can assemble into HPV structures.

The above technical object is provided by embodiments of the present invention, as defined in the claims of the present invention, and is further described herein and illustrated by the accompanying drawings.

The present invention is based, at least in part, on the discovery that the structure of the adenovirus penton base proteins is a true two-domain structure that may have evolved through gene fusions (Fig. 1B). These two domains, as it turns out, can be easily divided into two separate compact particles: a beta-barrel containing information about multimerization, and an alpha-helix domain resembling a “crown”.

Therefore, the present invention provides a "minimally" multimerizing polypeptide that can be associated with antigen or other cargo-carrying particles, thereby providing maximum versatility and flexibility. The thus constructed polypeptide of the present invention is derived from the amino acid sequences of the adenovirus penton base proteins (also referred to herein as “penton base protomers”) that form the beta-barrel domain of the adenovirus penton base. The beta-barrel domain of the adenovirus penton base proteins forms a so-called jelly roll fold domain containing eight beta sheets 1 to 8 (see Fig. 2), Zubieta et al. (2005) Mol. Cell 17, 121-135. The inventors of the present invention have surprisingly discovered that for efficient multimerization and thus display of bound cargo, e.g., oligopeptides or polypeptides, such as antigens or other bound entities, e.g., drugs, tags, nucleic acids, two loops (forming a " crown") inserted into the sequences between the amino acid regions forming the roll-fold domain may be completely or in other embodiments partially replaced by desired non-adenoviral sequences such as oligopeptide linkers (to which, in turn, antigens or other cargo may be associated ) or any desired amino acid sequence, such as polypeptides, proteins, protein domains, protein complexes, etc.

Therefore, in preferred embodiments of the present invention, the nucleic acid, drug, label and/or binding partner of the biological binding pair is/are attached to L ₁ and/or L ₂ . A “biologically binding” pair in accordance with the present invention are pairs of biological particles or compounds, respectively, that are commonly found in nature or that at least originate from binding pairs that are naturally occurring. Examples include, but are not limited to, antigens, antibodies, antibody fragments, diabodies, antibody mimetics, receptors and their ligands, biotin, streptavidin, and the like.

Such particles can be associated with L ₁ and/or L ₂ using means known in the art. If desired, linkers of any type can be linked to a suitable group at a position in L ₁ and/or L ₂ and this linker is then attached to the desired particle. Typical groups present on L ₁ and/or L ₂ that may be involved in chemical coupling include the NH ₂ and SH groups of amino acid residues present on L ₁ and/or L ₂ . However, the binding of cargo to L ₁ and/or L ₂ is not limited to chemical bonds, but also includes any other interactions such as ionic interactions, hydrogen bonds and van der Waals interactions.

The roll-fold domain of the present invention is formed by three amino acid regions (which may also be referred to, for example, as “segments” or “regions”): an N-terminal region, an intermediate region, and a C-terminal region. In the native adenovirus penton base protomer, loop segments are found between the N-terminal amino acid region and the intermediate region (large loop) and between the intermediate amino acid region and the C-terminal amino acid region (small loop). As stated above, exemplary non-adenoviral polypeptide sequences of the present invention, which may be referred to herein as “linkers,” replace loop segments of the native adenovirus penton base protomer. In other embodiments of the present invention, one of the large loops and the small loop of the native penton base may be present in the polypeptide of the present invention and form L ₁ or L ₂ .

Thus, the polypeptide of the present invention generally has the structure represented by the following general formula (I)

Where

A is the N-terminal amino acid region of the adenovirus penton base protein,

B represents the amino acid region of the adenovirus penton base protein,

C represents the C-terminal amino acid region of the adenovirus penton base,

where B is an amino acid region located between A and C in the sequence of the specified adenovirus penton base,

where A, B and C form a roll-fold domain of the specified adenovirus penton base protein.

L ₁ and L ₂ are linkers as above. Thus, L ₁ and L ₂ can be selected from virtually any amino acid sequence (provided that it does not interfere with multimerization of the polypeptide). Thus, L ₁ and L ₂ may be the same or different and are independently selected from the group consisting of an oligopeptide, a polypeptide, a protein and a protein complex. The L ₁ and L ₂ sequences, as a rule, are not adenoviral, i.e. have an amino acid sequence of at least 5, 6, 7, 8, 9, 10 or more amino acids, such sequence not existing or found in known penton base protomer sequences of any adenovirus serotype, more preferably any adenoviral protein.

In an alternative embodiment of the present invention, the linkers L ₁ and L ₂ can be selected from loop sequences (ie regions containing the first and second RGD loops and/or variable loop, as disclosed in WO 2017/167988 A1) of the adenovirus penton base. However, in this embodiment, the loop segment sequences are derived from an adenovirus having a serotype different from the adenovirus serotype from which said amino acid regions A, B, and C are derived. Accordingly, in this embodiment of the present invention, chimeras of penton base protomers are provided, wherein the beta-barrel, the roll fold domain is derived from one adenovirus subtype, whereas L ₁ and L ₂ are polypeptides containing RGD loop segments and/or variable VL loop segments (forming the crown domain) derived from a different adenovirus subtype , from which the roll-type domain originates.

In a preferred embodiment of the present invention, as shown in FIG. 2, amino acid region A contains beta sheets 1, 2 and 3 of the domain with the roll type folding of the protomer of the adenovirus penton base, amino acid region B contains beta sheets 4 and 5 of the domain with the roll type folding of the specified protomer of the adenovirus penton base, and amino acid region C contains beta -sheets 6, 7 and 8 of the domain with a roll-type fold of the indicated protomer of the adenovirus penton base. It should be understood that segments A, B and C may each be independently derived from the same or different adenoviruses.

Preferably, amino acid regions A, B and C have an amino acid sequence each independently derived from penton base sequences selected from the group consisting of human adenovirus serotype 2 (hAd2) penton bases, human adenovirus serotype 3 (hAd3), human adenovirus serotype 4 (hAd4), human adenovirus serotype 5 (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus serotype 25 (hAd25 ), human adenovirus serotype 35 (hAd35), human adenovirus serotype 37 (hAd37), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd1S), simian adenovirus serotype 20 (sAd20), simian adenovirus serotype 49 (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53).

Preferred amino acid sequences of the above adenoviral penton bases are available in publicly available databases such as UniProt and UniProtE, and particularly preferred sequences described herein for the above adenovirus subtypes are provided in UniProt Ace. No. Q2Y0H9 (human adenovirus serotype 3, SEQ ID NO: 1), UniProt Ace. No. P03276 (human adenovirus serotype 2, SEQ ID NO: 2), UniProt Ace. No. Q2KSF3 (human adenovirus serotype 4, SEQ ID NO: 3), UniProt Ace. No. P12538 (human adenovirus serotype 5, SEQ ID NO: 4), UniProt Ace. No. Q9JFT6 (human adenovirus serotype 7, SEQ ID NO: 5), UniProt Ace. No. D2DM93 (human adenovirus serotype 11, SEQ ID NO: 6), UniProt Ace. No. P36716 (human adenovirus serotype 12, SEQ ID NO: 7), UniProt Ace. No. F1DT65 (human adenovirus serotype 17, SEQ ID NO: 8), UniProt Ace. No. M0QUK0 (human adenovirus serotype 25, SEQ ID NO: 9), UniProt Ace. No. Q7T941 (human adenovirus serotype 35, SEQ ID NO: 10), UniProt Ace. No. Q912J1 (human adenovirus serotype 37, SEQ ID NO: 11), UniProt Ace. No. F8WQN4 (human adenovirus serotype 41, SEQ ID NO: 12), UniProt Ace. No. E5L3Q9 (gorilla adenovirus, SEQ ID NO: 13), UniProt Ace. No. G9G849 (chimpanzee adenovirus, SEQ ID NO: 14), UniProt Ace. No. H8PFZ9 (simian adenovirus serotype 18, SEQ ID NO: 15), UniProt Ace. No. F6KSU4 (simian adenovirus serotype 18, SEQ ID NO: 16), UniProt Ace. No. F2WTK5 (simian adenovirus serotype 49, SEQ ID NO: 17), UniProt Ace. No. A0A0A1EWW1 (rhesus macaque adenovirus serotype 51, SEQ ID NO: 18), UniProt Ace. No. A0A0A1EWX7 (rhesus macaque adenovirus serotype 52, SEQ ID NO: 19) and UniProt Ace. No. A0A0A1EWZ7 (rhesus macaque adenovirus serotype 53, SEQ ID NO: 20).

The amino acid sequences of the above penton bases are (the corresponding UniProt Ace number is indicated in parentheses):

Human adenovirus serotype 3 hAd3 penton base (Q2Y0H9), SEQ ID NO: 1:

hAd2 (P03276), SEQ ID NO: 2:

hAd4 (Q2KSF3), SEQ ID NO: 3:

hAd5 (P12538), SEQ ID NO: 4:

hAd7 (Q9JFT6), SEQ ID NO: 5:

hAd11 (D2DM93), SEQ ID NO: 6:

hAd12 (P36716), SEQ ID NO: 7:

hAd17 (F1DT65), SEQ ID NO: 8:

hAd25 (MOQUKO), SEQ ID NO: 9:

hAd35 (Q7T941), SEQ ID NO: 10:

hAd37 (Q912J1), SEQ ID NO: 11

hAd41 (F8WQN4), SEQ ID NO: 12:

Gorilla adenovirus penton base gorAd (E5L3Q9), SEQ ID NO: 13:

Chimpanzee adenovirus penton base chimpAd (G9G849), SEQ ID NO: 14:

Simian adenovirus serotype 18 penton base, sAd18 (H8PFZ9); SEQ ID NO: 15:

sAd20 (F6KSU4), SEQ ID NO: 16:

sAd49 (F2WTK5), SEQ ID NO: 17:

Rhesus adenovirus penton base serotype 51, rhAd51 (A0A0A1EWW1), SEQ ID NO: 18:

rhAd52 (A0A0A1EWX7), SEQ ID NO: 19:

rhAd53 (A0A0A1EWZ7), SEQ ID NO: NO 20:

The polypeptide of the present invention is not limited to those known specific sequences for the amino acid regions A, B and C forming the roll-fold multimerization domain of the above-mentioned sub- and serotypes of adenovirus, respectively. The amino acid segments A, B and C may also have amino acid sequences similar to the sequences of known adenovirus penton base protomers, provided that the sequences of A, B and C are such that the resulting polypeptide adopts a roll fold and assembles into pentameric complexes (also referred to as "Penton proteins"), twelve of which, in turn, self-assemble to form the dodecameric supercomplex (DSC of the present invention) under appropriate conditions, as further described below. Typically, such similar sequences of segments A, B and C will have an amino acid sequence identity of at least 85%, more preferably at least 90%, even more preferably 95%, especially preferably at least 98%, most preferably at least 99%, with the corresponding amino acid sequence a known penton base of an adenovirus, preferably the sequences SEQ ID NO: 1 to 20, more preferably amino acid regions A, B and C, as presented in Tables 1-3 below.

In this context, amino acid sequences are indicated from N to C terminus using the IUPAC one-letter code unless otherwise noted.

In a preferred embodiment of the present invention, amino acid region A has the following consensus sequence (SEQ ID NO: 21):

where: amino acid section A ends at the C-terminus before Z ₁ at residue T or at amino acids Z ₁ to Z15,

U represents any amino acid or is absent,

X ₁ represents E or G,

X ₂ represents E or S,

X ₃ represents L or V,

X ₄ represents A or S,

X ₅ represents L or Q,

X ₆ represents Y or E,

X ₇ represents R or K,

X ₈ represents V or L,

X ₉ represents V or I,

X ₁₀ represents F or Y,

X ₁₁ represents T or S,

X ₁₂ represents A, or T, or I, or G,

X ₁₃ represents S or G,

X ₁₄ represents F or L,

X ₁₅ represents E or D,

X ₁₆ represents A or G,

X ₁₇ represents D or Q,

X ₁₈ represents L or M,

X ₁₉ represents H or R,

Z ₁ , if present, represents N,

Z ₂ , if present, represents M,

Z ₃ , if present, represents P,

Z ₄ , if present, is N,

Z ₅ , if present, is V or I,

Z ₆ , if present, is N,

Z ₇ , if present, is E or D,

Z ₈ , if present, is Y or F,

Z ₉ , if present, is M,

Z ₁₀ , if present, is F or S or Y,

Z ₁₁ , if present, is T or S,

Z ₁₂ , if present, is S or N,

Z ₁₃ , if present, represents K,

Z ₁₄ , if present, is F,

Z ₁₆ if present represents K.

More preferred amino acid sequences of the A segment of the polypeptide of the present invention are presented in the following table 1:

According to another preferred embodiment of the present invention, amino acid region B of the above general formula (I) has the following sequence (SEQ ID NO: 22):

where: amino acid section B begins at the N-terminus of amino acids Z ₁₇ to Z ₂₇ or amino acid Q after Z ₂₇ ,

amino acid section B ends at the C-terminus before Z ₂₈ of amino acid L or amino acids Z ₂₈ to Z ₃₀ ,

Z ₁₇ , if present, is L or S,

Z ₁₈ , if present, is T or P or C,

Z ₁₉ , if present, is T or P,

Z ₂₀ , if present, is P or S or A or R,

Z ₂₁ , if present, is N or D,

Z ₂₂ , if present, is G or V,

Z ₂₃ , if present, is H or T,

Z ₂₄ , if present, is C,

Z ₂₅ , if present, represents G,

Z ₂₆ , if present, is A, or V, or S,

Z ₂₇ , if present, is E or Q,

X ₂₀ represents L or M,

X ₂₁ represents Q or K,

X ₂₂ represents Q or R or S,

X ₂₃ represents V or I,

X ₂₄ represents S or N,

X ₂₅ represents Y or F,

X ₂₆ represents A or V,

Z ₂₈ , if present, is M or L,

Z ₂₉ , if present, is P,

Z ₃₀ , if present, is V or F.

More preferred amino acid sequences of the B segment of the polypeptide of the present invention are presented in the following table 2:

According to a further preferred embodiment of the present invention, segment C of the above general formula (I) has the following sequence (SEQ ID NO: 23):

where: amino acid section C begins at the N-terminus of amino acids Z ₃₁ to Z ₃₃ or amino acid A after Z ₃₃ ,

Z ₃₁ , if present, is N,

Z ₃₂ , if present, represents V,

Z ₃₃ , if present, is P,

X ₂₇ represents R or S or G,

X ₂₈ represents V or I,

X ₂₉ represents Y or H,

X ₃₀ represents A or S,

X ₃₁ represents R or K.

More preferred amino acid sequences of the C segment of the polypeptide of the present invention are presented in the following table 3:

Particularly preferred polypeptides of the present invention are based on the roll-fold domain of the hAd3 penton base protomer. Particularly preferred are polypeptides wherein amino acid region A has an amino acid sequence starting from a position selected from amino acids 1 to 48, most preferably amino acid position 1, to an amino acid position selected from positions 129 to 144, most preferably amino acid position 132, wherein amino acid region B has an amino acid sequence starting from a position selected from positions 398 to 409, most preferably amino acid position 407, to a position selected from positions 440 to 443, most preferably amino acid position 442, and where amino acid region C has an amino acid a sequence starting at a position selected from positions 492 to 495, most preferably amino acid position 493, to amino acid position 544, where the amino acid positions refer to the sequence presented in UniProt Ace. No. QY0H9 (SEQ ID NO: 1).

The L ₁ and L ₂ binding segments of the polypeptide of the present invention can be selected from oligo peptide linkers, such as oligopeptides containing from 4 to 10 amino acids, preferably containing amino acids G and S. A preferred example is GGGS (SEQ ID 24). Another example is a linker consisting of G and S and having multiple GGS repeats, for example, 2, 3, 4, 5 or more GGS repeats. A particularly preferred linker of this type is id GGSGGS (SEQ ID NO: 25).

In other preferred embodiments, L ₁ is a polypeptide sequence comprising the RGD loop of a penton base of an adenovirus having a serotype different from the serotype of the adenovirus(es) from which said amino acid regions A, B and C are derived and/or D is a polypeptide sequence comprising a penton base variable loop of an adenovirus having a serotype different from the serotype of the adenovirus from which the indicated amino acid regions A, B and C are derived.

In further embodiments of the present invention, L ₁ is an RDG loop and L ₂ is preferably a non-adenoviral oligopeptide, preferably 4 to 20 amino acids, more preferably 4 to 10 amino acids, especially preferably an oligopeptide linker consisting of G and S, as defined above. In similar embodiments, L ₂ is or contains a variable loop and L ₁ is an oligopeptide linker as defined above. According to the present invention, it is also contemplated that L ₂ is or contains an RGD loop and L ₁ is an oligopeptide linker, and it is also contemplated that L ₁ is a variable loop and L ₂ is an oligopeptide linker.

In other preferred embodiments, as mentioned above, the L ₁ and L ₂ sequences, respectively, may be selected from the penton base protein crown domain sequences of an adenovirus other than the adenovirus from which the multimerization domain is derived. Generally, the combination of a crown domain chimera and a multimerization domain is not limited. Preferred chimeras are selected from combinations of crown domains and multimerization domains as described above. Crown domains, optionally and preferably including non-adenoviral sequences embedded in the RGD loop and/or variable loop of the corresponding crown domain, are more preferably disclosed in WO 2017/167988 A1.

Thus, it is clear that the crown domains of adenovirus penton bases usually consist of two amino acid regions: the so-called large fragment and small fragment. The large fragment of the crown domain is usually located at the N-terminus in the amino acid sequence of the corresponding adenovirus penton base protein, while the small fragment of the crown domain is usually located at the C-terminus. According to the present invention, it is preferable that the large fragment (containing the RGD loop as mentioned above) corresponds to L ₁ of the general formula (I), and it is further preferable that the small fragment (containing the variable loop) corresponds to L ₂ of the general formula (I). In some embodiments of the present invention, the large and small fragments are derived from the same adenovirus penton base. In other embodiments of the present invention, the large fragment and the small fragment are derived from different adenovirus penton bases, or that only one of the large and small fragments is derived from an adenovirus penton base protein different from the adenovirus from which the multimerization domain is derived, i.e. from which amino acid regions A, B and C are derived.

Preferred crown domains for use in the chimeric constructs of the present invention include crown domains selected from the group consisting of the penton bases of human adenovirus serotype 2 (hAd2), human adenovirus serotype 3 (hAd3), human adenovirus serotype 4 (hAd4) , human adenovirus serotype 5 (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus serotype 25 (hAd25), adenovirus human serotype 35 (hAd35), human adenovirus serotype 37 (hAd37), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd1S), simian adenovirus serotype 20 (sAd20) , simian adenovirus serotype 49 (sAd 49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53).

Preferred amino acid sequences of the above adenovirus penton bases used for the crown domain are provided in publicly available databases such as UniProt and UniProtE, and particularly preferred sequences described herein for the above adenovirus subtypes are provided in UniProt Ace. No. Q2Y0H9 (human adenovirus serotype 3, SEQ ID NO: 1), UniProt Ace. No. P03276 (human adenovirus serotype 2, SEQ ID NO: 2), UniProt Ace. No. Q2KSF3 (human adenovirus serotype 4, SEQ ID NO: 3), UniProt Ace. No. PI2538 (human adenovirus serotype 5, SEQ ID NO: 4), UniProt Ace. No. Q9JFT6 (human adenovirus serotype 7, SEQ ID NO: 5), UniProt Ace. No. D2DM93 (human adenovirus serotype 11, SEQ ID NO: 6), UniProt Ace. No. P36716 (human adenovirus serotype 12, SEQ ID NO: 7), UniProt Ace. No. F1DT65 (human adenovirus serotype 17, SEQ ID NO: 8), UniProt Ace. No. M0QUK0 (human adenovirus serotype 25, SEQ ID NO: 9), UniProt Ace. No. Q7T941 (human adenovirus serotype 35, SEQ ID NO: 10), UniProt Ace. No. Q912J1 (human adenovirus serotype 37, SEQ ID NO: 11), UniProt Ace. No. F8WQN4 (human adenovirus serotype 41, SEQ ID NO: 12), UniProt Ace. No. E5L3Q9 (gorilla adenovirus, SEQ ID NO: 13), UniProt Ace. No. G9G849 (chimpanzee adenovirus, SEQ ID NO: 14), UniProt Ace. No. H8PFZ9 (simian adenovirus serotype 18, SEQ ID NO: 15), UniProt Ace. No. F6KSU4 (simian adenovirus serotype 20, SEQ ID NO: 16), UniProt Ace. No. F2WTK5 (simian adenovirus serotype 49, SEQ ID NO: 17), UniProt Ace. No. A0A0A1EWW1 (rhesus macaque adenovirus serotype 51, SEQ ID NO: 18), UniProt Ace. No. A0A0A1EWX7 (rhesus macaque adenovirus serotype 52, SEQ ID NO: 19) and UniProt Ace. No. A0A0A1EWZ7 (rhesus macaque adenovirus serotype 53, SEQ ID NO: 20).

The most preferred sequences of large fragments of crown domains for use in the chimeric constructs of the present invention are shown in the following table 4:

The most preferred large crown domain fragment sequences for use in the chimeric constructs of the present invention are shown in the following Table 5:

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of human adenovirus serotype 2 (hAd2) is combined with the penton base crown domain of an adenovirus selected from human adenovirus serotype 3 (hAd3), human adenovirus serotype 4 (hAd4), human adenovirus 5 serotype (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus serotype 25 (hAd25), human adenovirus serotype 35 ( hAd35), human adenovirus serotype 37 (hAd37), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd18), simian adenovirus serotype 20 (sAd20), simian adenovirus 49 serotype (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of human adenovirus serotype 3 (hAd3) is combined with the penton base crown domain of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 4 (hAd4), human adenovirus 5 serotype (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus serotype 25 (hAd25), human adenovirus serotype 35 ( hAd35), human adenovirus serotype 37 (hAd37), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd18), simian adenovirus serotype 20 (sAd20), simian adenovirus 49 serotype (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of human adenovirus serotype 4 (hAd4) is combined with the penton base crown domain of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 3 (hAd3), human adenovirus 5 serotype (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus serotype 25 (hAd25), human adenovirus serotype 35 ( hAd35), human adenovirus serotype 37 (hAd37), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd18), simian adenovirus serotype 20 (sAd20), simian adenovirus 49 serotype (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of human adenovirus serotype 5 (hAd5) is combined with the penton base crown domain of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 3 (hAd3), human adenovirus 4 serotype (hAd4), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus serotype 25 (hAd25), human adenovirus serotype 35 ( hAd35), human adenovirus serotype 37 (hAd37), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd18), simian adenovirus serotype 20 (sAd20), simian adenovirus 49 serotype (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of human adenovirus serotype 7 (hAd7) is combined with the penton base crown domain of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 3 (hAd3), human adenovirus 4 serotype (hAd4), human adenovirus serotype 5 (hAd5), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus serotype 25 (hAd25), human adenovirus serotype 35 ( hAd35), human adenovirus serotype 37 (hAd37), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd18), simian adenovirus serotype 20 (sAd20), simian adenovirus 49 serotype (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of human adenovirus serotype 11 (hAd11) is combined with the penton base crown domain of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 3 (hAd3), human adenovirus 4 serotype (hAd4), human adenovirus serotype 5 (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus serotype 25 (hAd25), human adenovirus serotype 35 ( hAd35), human adenovirus serotype 37 (hAd37), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd18), simian adenovirus serotype 20 (sAd20), simian adenovirus 49 serotype (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of human adenovirus serotype 12 (hAd12) is combined with the penton base crown domain of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 3 (hAd3), human adenovirus 4 serotype (hAd4), human adenovirus serotype 5 (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 17 (hAd17), human adenovirus serotype 25 (hAd25), human adenovirus serotype 35 ( hAd35), human adenovirus serotype 37 (hAd37), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd18), simian adenovirus serotype 20 (sAd20), simian adenovirus 49 serotype (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of human adenovirus serotype 17 (hAd17) is combined with the penton base crown domain of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 3 (hAd3), human adenovirus 4 serotype (hAd4), human adenovirus serotype 5 (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 25 (hAd25), human adenovirus serotype 35 ( hAd35), human adenovirus serotype 37 (hAd37), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd18), simian adenovirus serotype 20 (sAd20), simian adenovirus 49 serotype (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of human adenovirus serotype 25 (hAd25) is combined with the penton base crown domain of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 3 (hAd3), human adenovirus 4 serotype (hAd4), human adenovirus serotype 5 (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus serotype 35 ( hAd35), human adenovirus serotype 37 (hAd37), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd18), simian adenovirus serotype 20 (sAd20), simian adenovirus 49 serotype (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of human adenovirus serotype 35 (hAd35) is combined with the penton base crown domain of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 3 (hAd3), human adenovirus 4 serotype (hAd4), human adenovirus serotype 5 (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus serotype 25 ( hAd25), human adenovirus serotype 37 (hAd37), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd18), simian adenovirus serotype 20 (sAd20), simian adenovirus 49 serotype (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of human adenovirus serotype 37 (hAd37) is combined with the penton base crown domain of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 3 (hAd3), human adenovirus 4 serotype (hAd4), human adenovirus serotype 5 (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus serotype 25 ( hAd25), human adenovirus serotype 35 (hAd35), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd18), simian adenovirus serotype 20 (sAd20), simian adenovirus 49 serotype (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of human adenovirus serotype 41 (hAd41) is combined with the penton base crown domain of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 3 (hAd3), human adenovirus 4 serotype (hAd4), human adenovirus serotype 5 (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus serotype 25 ( hAd25), human adenovirus serotype 35 (hAd35), human adenovirus serotype 37 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd18), simian adenovirus serotype 20 (sAd20), simian adenovirus 49 serotype (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of a gorilla adenovirus (gorAd) is combined with the crown domain of a penton base of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 3 (hAd3), human adenovirus serotype 4 ( hAd4), human adenovirus serotype 5 (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus serotype 25 (hAd25) , human adenovirus serotype 35 (hAd35), human adenovirus serotype 37 (hAd41), human adenovirus serotype 41 (hAd41), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd18), simian adenovirus serotype 20 (sAd20), simian adenovirus 49 serotype (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of a chimpanzee adenovirus (ChimpAd) is combined with the penton base crown domain of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 3 (hAd3), human adenovirus serotype 4 ( hAd4), human adenovirus serotype 5 (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus serotype 25 (hAd25) , human adenovirus serotype 35 (hAd35), human adenovirus serotype 37 (hAd41), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), simian adenovirus serotype 18 (sAd18), simian adenovirus serotype 20 (sAd20), simian adenovirus 49 serotype (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of simian adenovirus serotype 18 (sAd1S) is combined with the penton base crown domain of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 3 (hAd3), human adenovirus 4 serotype (hAd4), human adenovirus serotype 5 (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus serotype 25 ( hAd25), human adenovirus serotype 35 (hAd35), human adenovirus serotype 37 (hAd41), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 20 (sAd20), simian adenovirus 49 serotype (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of simian adenovirus serotype 20 (sAd20) is combined with the penton base crown domain of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 3 (hAd3), human adenovirus 4 serotype (hAd4), human adenovirus serotype 5 (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus serotype 25 ( hAd25), human adenovirus serotype 35 (hAd35), human adenovirus serotype 37 (hAd41), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd1S), simian adenovirus 49 serotype (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of simian adenovirus serotype 49 (sAd49) is combined with the penton base crown domain of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 3 (hAd3), human adenovirus 4 serotype (hAd4), human adenovirus serotype 5 (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus serotype 25 ( hAd25), human adenovirus serotype 35 (hAd35), human adenovirus serotype 37 (hAd41), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd18), simian adenovirus 20 serotype (sAd20), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of rhesus macaque adenovirus serotype 51 (rhAd51) is combined with the penton base crown domain of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 3 (hAd3), adenovirus human adenovirus serotype 4 (hAd4), human adenovirus serotype 5 (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus 25 serotype (hAd25), human adenovirus serotype 35 (hAd35), human adenovirus serotype 37 (hAd41), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd18), adenovirus monkey serotype 20 (sAd20), simian adenovirus serotype 49 (sAd49), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of rhesus macaque adenovirus serotype 52 (rhAd52) is combined with the penton base crown domain of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 3 (hAd3), adenovirus human adenovirus serotype 4 (hAd4), human adenovirus serotype 5 (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus 25 serotype (hAd25), human adenovirus serotype 35 (hAd35), human adenovirus serotype 37 (hAd41), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd18), adenovirus monkey serotype 20 (sAd20), simian adenovirus serotype 49 (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A preferred embodiment of the present invention is a chimera wherein the multimerization domain of rhesus macaque adenovirus serotype 53 (rhAd53) is combined with the penton base crown domain of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 3 (hAd3), adenovirus human adenovirus serotype 4 (hAd4), human adenovirus serotype 5 (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus 25 serotype (hAd25), human adenovirus serotype 35 (hAd35), human adenovirus serotype 37 (hAd41), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd18), adenovirus monkey serotype 20 (sAd20), simian adenovirus serotype 49 (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51) and rhesus macaque adenovirus serotype 52 (rhAd52). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A particularly preferred crown domain for producing chimeras of the present invention is the crown domain of the penton base protein of human adenovirus serotype 3 (hAd3). Preferred sequences with respect to amino acid positions of SEQ ID NO: 1 are presented in Table 4 (large fragment) and Table 5 (small fragment).

In even more preferred chimeras of the present invention, the crown domain of the penton base protein of human adenovirus serotype 3 (hAd3) is combined with the multimerization domain of the penton base protein of an adenovirus selected from human adenovirus serotype 2 (hAd2), human adenovirus serotype 4 (hAd4), adenovirus human adenovirus serotype 5 (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus serotype 25 (hAd25), human adenovirus 35 serotype (hAd35), human adenovirus serotype 37 (hAd37), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), chimpanzee adenovirus (ChimpAd), simian adenovirus serotype 18 (sAd18), simian adenovirus serotype 20 (sAd20), adenovirus monkey serotype 49 (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

A particularly preferred crown domain for producing chimeras of the present invention is the chimpanzee adenovirus penton base crown domain (ChimpAd). Preferred sequences with respect to amino acid positions of SEQ ID NO: 14 are presented in Table 4 (large fragment) and Table 5 (small fragment).

In even more preferred chimeras of the present invention, the crown domain of a chimpanzee adenovirus penton base protein (ChimpAd) is combined with the multimerization domain of an adenovirus penton base protein selected from human adenovirus serotype 3 (hAd3), human adenovirus serotype 2 (hAd2), human adenovirus 4 serotype (hAd4), human adenovirus serotype 5 (hAd5), human adenovirus serotype 7 (hAd7), human adenovirus serotype 11 (hAd11), human adenovirus serotype 12 (hAd12), human adenovirus serotype 17 (hAd17), human adenovirus serotype 25 ( hAd25), human adenovirus serotype 35 (hAd35), human adenovirus serotype 37 (hAd37), human adenovirus serotype 41 (hAd41), gorilla adenovirus (gorAd), simian adenovirus serotype 18 (sAd18), simian adenovirus serotype 20 (sAd20), adenovirus monkey serotype 49 (sAd49), rhesus macaque adenovirus serotype 51 (rhAd51), rhesus macaque adenovirus serotype 52 (rhAd52) and rhesus macaque adenovirus serotype 53 (rhAd53). The specific multimerization domain and crown domain sequences selected for this combination refer to specific examples in accordance with Tables 1 to 5.

As already indicated above, one of the main embodiments of the present invention is the inclusion of an antigen, more particularly an antigen of an infectious agent such as a virus, bacterium or other pathogen, or a tumor or cancer antigen, in one or both of L ₁ and L ₂ . Preferred insertion sites for antigens in RGD loops and/or variable loops of adenoviral crown domains are disclosed in WO 2017/167988 A1. As used herein, the term "antigen" refers to a structure recognized by immune response molecules, such as antibodies, T cell receptors (TCRs), etc.

Infectious agent antigens include, but are not limited to, for example, viral infectious agents such as HIV, hepatitis viruses such as hepatitis A virus, hepatitis B virus or hepatitis C virus, herpes virus, varicella zoster virus, rubella virus, yellow fever virus , Dengue fever virus, flaviviruses (eg Zika virus), influenza viruses, Marburg virus disease, Ebola viruses and arboviruses such as chikungunya virus. Antigens of bacterial infectious agents include, but are not limited to, antigens, for example, Legionella, Helicobacter, Vibrio, infectious strains of E. coli, Staphylococci, Salmonella and Streptococci. Antigens of infectious protozoan pathogens include, but are not limited to, Plasmodium, Trypanosoma, Leishmania, and Toxoplasma antigens. Additional examples of pathogen antigens include fungal pathogen antigens, such as those of Cryptococcus neoformans, Histoplasma capsulatum, Coccidioides immitis, Blastomyces dermatitidis, and Candida albicans.

Specific examples of tumor antigens that can be used in accordance with the present invention include, but are not limited to, 707-AP, AFP, ART-4, BAGE, beta-catenin/m, Bcr-abl, CAMEL, CAP-1, CASP -8, CDC27/m, CDK4/m, CEA, CT, Cyp-B, DAM, ELF2M, ETV6-AML1, G250, GAGE, GnT-V, Gp100, HAGE, HER-2/neu, HLA-A*0201 -R170I, HPV-E7, HSP70-2M, HAST-2, hTERT (or hTRT), iCE, KIAA0205, LAGE, LDLR/FUT, MAGE, MART-1/Melan-A, MC1R, myosin/m, MUC1, MUM -1, -2, -3, NA88-A, NY-ESO-1, pl90 minor bcr-abl, Pml/RAR.alpha., PRAME, PSA, PSM, RAGE, RU1 or RU2, SAGE, SART-1 or SART-3, TEL/AML1, TPI/m, TRP-1, TRP-2, TRP-2/TNT2h WT1.

Particularly in the context of antigens included in the polypeptides of the present invention, such as L ₁ and/or L ₂ , but also in relation to any protein-protein interaction, such as receptor-ligand binding, a process of selection and/or evolution can be involved to provide sequences, optimized for target binding, such as optimized antigens, to exhibit an improved immune response. The preferred method is ribosomal display, as described in detail in Schaffitzel et al. (2001) in: Protein-Protein Interactions, A Molecular Cloning Manual: In vitro selection and evolution of protein-ligand interaction by ribosome display (Golemis E., ed.), pages 535-567, Cold Spring Harbor Laboratory Press, New York . The advantage of the ribosomal display method is its complete implementation in vitro at all stages of selection. Other possible selection methods are also known in the art and include phage display (Smith (1985) Science 228, 1315-1317; Winter et al. (1994) Annu. Rev. Immunol. 12, 433-455), yeast two-hybrid system ( Fields and Song (19899 Nature 340, 245-246, Chien et al. (1983) Proc. Natl. Acad. Sci. USA 88, 9578-9582) and cell surface display methods (Georgiu et al. (1993) Trends Biotechnol 11, 6-10, Boder and Wittrup (1997) Nat. Biotechnol. 15, 553-557).

The ribosomal display method can generally be used in two ways to optimize antigens or other amino acid sequences involved in targeting a particular molecule using the polypeptides of the present invention. Alternatively, the antigen (or other binding agent) sequence may be selected first from an initial library of polypeptide sequences, which may be up to 10 ¹⁴ individual sequences, typically 10 ⁹ to 10 ¹⁰ sequences, optionally using evolutionary procedures as detailed in Schaffitzel et al . (2001), supra. After selecting the optimized antigen sequences, the nucleotide sequence encoding it is cloned into the corresponding vector of the present invention, so that a polypeptide in which the optimized antigen is included or is L ₁ and/or L ₂ according to the above formula (I) is expressed.

According to an alternative embodiment of this aspect of the present invention, a library of potential antigen coding sequences is directly cloned into a nucleic acid of the present invention such that each sequence encodes a polypeptide that is part of or represents, respectively, one or both of L ₁ and L ₂ as defined in formula (I) above. The polypeptides of the present invention containing the initial library of antigen sequences (or, in other embodiments, other binding sequences) are then expressed in vitro, and the selection of optimized antigen (or other binding agent) sequences is carried out in accordance with the ribosomal display method, as described in detail in Schaffitzel et al. (2001), supra.

A further embodiment of the polypeptides of the present invention relates to polypeptides wherein L ₁ and/or L ₂ are or are linked to, respectively, antibody sequences or portions of antibodies, such as antibody fragments. In the context of the present invention, the term "antibody" means an immunoglobulin that specifically binds to an antigen.

The term "antibody fragment" refers to the portion of an antibody that retains the ability of the complete antibody to specifically bind an antigen. Examples of antibody fragments include, but are not limited to, Fab fragments, Fab' fragments, F(ab') ₂ fragments, heavy chain only antibodies, single domain antibodies (sdAbs), scFv fragments, variable fragments (Fv), VH domains , VL domains, nanobodies, IgNARs (immunoglobulin novel antigen receptors), di-scFvs, bispecific T cell agents (BITEs), dual affinity antibody retargeting (DART) molecules, ternary bodies, diabodies, single-chain diabodies, etc.

A "diabody" is a fusion protein or bivalent antibody that can bind various antigens. The diabody consists of two single protein chains (usually two scFv fragments), each of which contains variable antibody fragments. Thus, diabodies contain two antigen-binding sites and thus can target the same (monospecific diabody) or different antigens (bispecific diabody).

The term "single domain antibody", as used herein, refers to antibody fragments consisting of a single monomeric antibody variable domain. They simply include only the variable regions of the monomeric heavy chain of antibodies consisting only of heavy chains produced by cartilaginous fish or camelids. Due to their different origins, they are also called VHH or VNAR (variable new antigen receptor) fragments. Alternatively, single domain antibodies can be produced by monomerizing the variable domains of conventional mouse or human antibodies using genetic engineering. They have a molecular weight of approximately 12 to 15 kDa and are thus the smallest antibody fragments capable of recognizing antigen. Additional examples include nanobodies or nanoantibodies.

Antigen-binding particles useful in the context of the present invention also include "antibody mimetics", as used herein, referring to compounds that specifically bind antigens similar to antibodies, but which are not structurally related to antibodies. Typically, antibody mimetics are artificial peptides or proteins with a molar mass of approximately 3 to 20 kDa that contain one, two, or more accessible domains that specifically bind an antigen. Examples include, but are not limited to, LACI-D1 (lipoprotein-associated coagulation inhibitor), affins such as human-γB crystalline or human ubiquitin, cystatin, Sac7D from Sulfolobus acidocaldarius, lipocalin and lipocalin-derived anticalins, DARPins (designed repeating ankyrin domains), Fyn CH3 domain, Kunits protease inhibitor domain, monobodies, e.g. fibronectin type III type 10 domain, adnectins: knottins (cysteine knot miniproteins), atrimers, evibodies, e.g. CTLA4-based binders, affibodies, e.g. , triple-stranded bundle from the Z domain of protein A from Staphylococcus aureus, trans-bodies, e.g. human transferrin, tetranectins, e.g. monomeric or trimeric domain of human C-type lectin, microbodies, e.g. trypsin inhibitor-P, affilins, armadillo repeat-bearing proteins. Nucleic acids and small molecules are sometimes also considered antibody mimetics (aptamers), but not artificial antibodies, antibody fragments, and fusion proteins composed of them. General advantages over antibodies are better solubility, tissue penetration, resistance to heat and enzymes, and relatively low production costs.

Like native penton base proteins, the polypeptides of the present invention assemble into pentameric complexes, 12 of which are in turn assembled into virus-like particles (VLPs) in a buffer solution at a pH preferably from about 5.0 to about 8.0. Preferred examples are buffer conditions at or near physiological conditions, such as phosphate-buffered saline (PBS), pH 7.4, or Tris-buffered saline (TBS) or TBS-T pH 7.2 to 7.6. Under such conditions, the polypeptides of the present invention form VLPs at a temperature of approximately 20 to 42°C. The present invention also relates to such pentameric complexes and HPV.

Another aspect of the present invention relates to a nucleic acid encoding a polypeptide as defined herein.

According to the present invention, the terms "nucleic acid" and "polynucleotide" are used interchangeably and refer to DNA, RNA, or species containing one or more nucleotide analogues. Preferred nucleic acids or polynucleotides of the present invention are DNA, more preferably double-stranded (ds) DNA. The nucleotide sequences of the present invention are presented in the 5' to 3' direction, and the single letter IUPAC code for bases is used unless otherwise indicated.

Another embodiment relates to a nucleic acid prepared to insert universal segments L ₁ and L ₂ as defined in general formula (1). That is, this nucleic acid variant encodes segments A, B, and C, but has insertion sites between the segments encoding A and B, and between the segments encoding B and C.

Thus, this embodiment can be represented by the following general formula (II):

Where

a is a nucleotide sequence encoding A of general formula (I),

b is a nucleotide sequence encoding B of general formula (I),

c is a nucleotide sequence encoding C of general formula (I), and

l ₁ , l ₂ each represents a nucleotide sequence,

is ₁ to is ₄ each independently represent a nucleotide sequence containing at least one insertion site.

The insertion site in the context of this embodiment of the present invention is preferably a restriction enzyme or homing endonuclease recognition sequence. More preferably, is ₁ to is ₄ each represents a different insertion site, more specifically, each is ₁ to is ₄ represents a different restriction enzyme recognition sequence. A preferred embodiment of the nucleic acid prepared for the insertion of nucleotide sequences encoding L ₁ and L ₂ has a nucleotide sequence where is ₁ contains an EcoRI site, is ₂ contains a RsrII site, is3 contains a SacI site and 1&4 contains an XLa site!

Restriction enzyme sites are usually well known to one skilled in the art. Preferred examples are as defined above, but restriction sites can be selected from a wide variety and recommendations can be found from various restriction enzyme manufacturers such as New England Biolabs, Inc., Ipswich, MA, USA.

Examples of such homing endonuclease (HE) sites include, but are not limited to, the recognition sequences PI-SceI, I-CeuI, I-PpoI, I-HmuI, I-CreI, I-DmoI, PI-PfuI, and I-MsoI. PI-PspI, I-Scel, other members of the LAGLIDAG group and their variants, SegH and Hef or other homing endonucleases GIY-YIG, I-ApeII, I-Anil, cytochrome b mRNA maturase bl3, PI-THI and PI-TfuII, PI-ThyI and others, see Stoddard B.L. (2005) Q. Rev. Biophys. 38, 49-95. Suitable enzymes are commercially available, for example, from New England Biolabs Inc., Ipswich, MA, USA.

In preferred embodiments of the present invention, the above nucleic acid further comprises at least one site for integration of the nucleic acid into the vector or host cell. The integration site may allow transient or genomic inclusion.

With regard to integration into a vector, particularly a plasmid or virus, the integration site is preferably compatible for integration of the nucleic acid into an adenovirus, adeno-associated virus (AAV), autonomous parvovirus, herpes simplex virus (HSV), retrovirus, rhadinovirus, Epstein-Barr virus, lentivirus, Semliki forest virus or baculovirus.

Particularly preferred integration sites that may be included in the nucleic acid of the present invention may be selected from the Tn7 transposon element, λ integrase-specific binding sites, and site-specific recombinases (SSRs), in particular the LoxP site or recombination site, specific for FLP recombinase (FRT). Other preferred nucleic acid integration mechanisms of the present invention are specific homologous recombination sequences, such as Ief2-603/Orf1629.

In other preferred embodiments of the present invention, the nucleic acid described herein further comprises one or more resistance markers for selection against toxic substances. Preferred examples of resistance markers useful in the context of the present invention include, but are not limited to, antibiotics such as ampicillin, chloramphenicol, gentamicin, spectinomycin and kanamycin resistance markers.

The nucleic acid of the present invention may also contain one or more ribosome binding sites (RBS).

Another aspect of the present invention relates to a vector containing a nucleic acid as defined above.

Preferred vectors of the present invention are plasmids, expression vectors, transfer vectors, more preferably eukaryotic gene transfer vectors, transient-mediated or viral vector-mediated gene transfer vectors. Other vectors of the present invention are viruses, such as adenovirus vectors, adeno-associated virus (AAV) vectors, autonomous parvovirus vectors, herpes simplex virus (HSV) vectors, retroviral vectors, rhadinovirus vectors, Epstein-Barr virus vectors, lentivirus vectors, virus vectors Semliki forests and baculovirus vectors.

Baculovirus vectors suitable for integrating the nucleic acid of the present invention (e.g., present on a suitable plasmid, such as a transfer vector) are also subject to the present invention and preferably contain site-specific integration sites, such as a Tn7 attachment site (which may be inserted into the lacZ gene for blue/white screening for productive integration) and/or the LoxP site. Further preferred baculoviruses of the present invention contain (alternatively or in addition to the integration sites described above) a host toxic expression gene flanked by sequences for homologous recombination. An example of a gene expressing a toxic substance is the diphtheria toxin A gene. A preferred sequence pair for homologous recombination is, for example, Isf2-603/Orf1629. The baculovirus may also contain additional marker gene(s) as described above, including also fluorescent markers such as GFP, YFP and so on. Specific examples of corresponding baculoviruses are disclosed, for example, in WO 2010/100278 A1.

Other useful vectors for use in the present invention are disclosed in WO 2005/085456 A1.

Vectors useful in prokaryotic host cells preferably contain, in addition to the above examples of marker genes (one or more of them), an origin of replication (ori). Examples are BR322, ColE1 and conditional origins of replication such as OriV and R6Ky, the latter being the preferred conditional origin of replication that makes propagation of the vector of the present invention dependent on the pir gene in the prokaryotic host. OriV makes the distribution of the vector of the present invention dependent on the trfA gene in the prokaryotic host.

In addition, the present invention relates to a host cell containing a nucleic acid of the present invention and/or a vector of the present invention.

Host cells can be prokaryotic or eukaryotic. Eukaryotic host cells may be, for example, mammalian cells, preferably human cells. Examples of human host cells include, but are not limited to, HeLa, Huh7, HEK293, HepG2, KATO-III, IMR32, MT-2, pancreatic β-cells, keratinocytes, bone marrow fibroblasts, CHP212, primary nerve cells, W12, SK-N-MC, Saos-2, WI38, primary hepatocytes, FLC4, 143TK, DLD-1, embryonic lung fibroblasts, primary foreskin fibroblasts, MRC5 and MG63 cells. Other preferred host cells of the present invention are porcine cells, preferably IBS cells, FS-13, PK-15, bovine cells, preferably MDB cells, BT cells, bovine cells such as FLL-YFT cells. Other eukaryotic cells useful in the context of the present invention are C. elegans cells. Additionally, eukaryotic cells include yeast cells such as S. cerevisiae, S. pombe, C. albicans and P. pastoris. Furthermore, the present invention relates to insect cells as host cells, which include S. frugiperda cells, more preferably Sf9, Sf21, Express Sf+, High Five H5 cells and D. melanogaster cells, in particular S2 Schneider cells. Other host cells include Dictyostelium discoideum cells and parasite cells such as Leishmania spec.

Prokaryotic hosts according to the present invention include bacteria, in particular E. coli, for example commercially available strains such as TOP10, DH5α, HB101. BL21 (DE3), etc.

One skilled in the art will readily be able to select suitable vector construct/host cell pairs for appropriate propagation and/or transfer of the nucleic acid elements of the present invention into a suitable host. Specific methods for introducing appropriate vector elements and vectors into appropriate host cells are known in the art, and methods can be found in the latest edition of Ausubel et al. (ed.) Current Protocols in Molecular Biology, John Wiley & Sons, New York, USA.

In preferred embodiments of the present invention, the vector as defined above further includes a site for site-specific recombinases (SSRs), preferably one or more LoxP sites for Cre-1ox-specific recombination. In other preferred embodiments, the vector of the present invention contains a transposon element, preferably a Tn7 attachment site.

In addition, it is preferable that the binding site, as defined above, is located within the marker gene. This arrangement makes it possible to select sequences successfully integrated into the binding site by transposition. In preferred embodiments, such a marker gene is selected from luciferase genes, β-GAL, CAT, genes encoding fluorescent proteins, preferably GFP, BFP, YFP, CFP and variants thereof, and the lacZa gene.

In addition, the present invention relates to a host cell containing a nucleic acid of the present invention and/or a vector of the present invention.

Host cells can be prokaryotic or eukaryotic. Eukaryotic host cells may be, for example, mammalian cells, preferably human cells. Examples of human host cells include, but are not limited to, HeLa, Huh7, HEK293, HepG2, KATO-III, IMR32, MT-2, pancreatic β-cells, keratinocytes, bone marrow fibroblasts, CHP212, primary nerve cells, W12, SK-N-MC, Saos-2, WI38, primary hepatocytes, FLC4, 143TK, DLD-1, embryonic lung fibroblasts, primary foreskin fibroblasts, MRC5 and MG63 cells. Further preferred host cells of the present invention are porcine cells, preferably IBS cells, FS-13, PK-15, bovine cells, preferably MDB cells, BT cells, bovine cells such as FLL-YFT cells. Other eukaryotic cells useful in the context of the present invention are C. elegans cells. Additional eukaryotic cells include yeast cells such as S. cerevisiae, S. pombe, C. albicans and P. pastoris. Furthermore, the present invention relates to insect cells as host cells, which include S. frugiperda cells, more preferably Sf9, Sf21, Express Sf+, High Five H5 cells and D. melanogaster cells, especially S2 Schneider cells. Additional host cells include cells of Dictyostelium discoideum and cells of parasites such as Leishmania spec.

Prokaryotic hosts of the present invention include bacteria, in particular E. coli, for example commercially available strains such as TOP10, DH5a, HB101, BL21 (DE3), etc.

One skilled in the art will readily be able to select suitable vector/host cell construct pairs for appropriate propagation and/or transfer of the nucleic acid elements of the present invention into a suitable host. Specific methods for introducing appropriate vector elements and vectors into appropriate host cells are equally known in the art, and methods are described in the latest edition of Ausubel et al. (ed.) Current Protocols In Molecular Biology, John Wiley & Sons, New York, USA.

The present invention also relates to a polypeptide, a nucleic acid encoding such a polypeptide, a vector containing a nucleic acid encoding a polypeptide, a host cell containing such a vector, and an HPV as defined above, for use as a drug, in particular for use in the treatment and/or prevention of an infectious disease, immune disease, tumor or cancer.

Therefore, the present invention also relates to pharmaceutical compositions containing a polypeptide as defined herein, a nucleic acid encoding such a polypeptide, a vector containing a nucleic acid encoding the polypeptide, a host cell containing such a vector, or an HPV as described above, together with at least one pharmaceutically acceptable carrier, excipient and/or diluent.

In general, the preparation of pharmaceutical compositions in the context of the present invention, their dosages and routes of administration are known to the skilled person, and guidance can be found in the latest edition of Remington's Pharmaceutical Sciences (Mack publishing Co., Eastern, PA, USA).

The pharmaceutical compositions of the present invention contain a therapeutically effective amount of the active ingredient as defined above. The therapeutically effective amount depends on the active ingredient and, in particular, on the route of administration. The pharmaceutical composition of the present invention is preferably administered by parenteral administration, in particular by infusion, such as intravenous, intra-arterial or intraosseous infusion, or by injection, such as intravenous, intra-arterial, intraperitoneal, intramuscular, intradermal, subcutaneous or intrathecal injection. In the case of antitumor therapy, a pharmaceutical composition such as a pharmaceutical composition containing HPV of the present invention can also be administered by intratumoral injection.

The injection or infusion solutions of the present invention typically contain the HPV of the present invention in water or an aqueous buffer solution, preferably an isotonic buffer at physiological pH. The liquid pharmaceutical compositions of the present invention may contain additional ingredients such as pharmaceutically acceptable stabilizers, suspending agents, emulsifiers and the like. Other ingredients of the pharmaceutical composition of the present invention are excipients, in particular in the context of the use of the constructs of the present invention for vaccination purposes.

Another aspect of the present invention relates to methods of treatment using the beneficial properties of the polypeptides, nucleic acids, host cells, vectors and/or HPVs of the present invention. In a preferred embodiment, the present invention provides a method of preventing and/or treating an infectious disease, comprising the step of administering to a subject, preferably a human, a therapeutically effective amount of a pharmaceutical composition as defined above, wherein the pharmaceutical composition contains HPVs of the present invention containing antigens (in particular, those containing in L ₁ and/or L ₂ of the polypeptide of the present invention, as defined above) of an infectious agent that causes an infectious disease. Another embodiment is a method of preventing and/or treating a tumor or cancer by administering a therapeutically effective amount of a pharmaceutical composition as defined above to a subject, preferably a human, wherein the pharmaceutical composition comprises HPVs of the present invention containing one or more tumor antigens (in particularly those contained in L ₁ and/or L ₂ of the polypeptide of the present invention, as defined above).

The present invention further provides a method for producing a polypeptide as described herein, comprising the step of culturing a recombinant host cell in a suitable medium, wherein the host cell contains a vector that contains a nucleic acid encoding the polypeptide under conditions allowing expression of said polypeptide.

Preferably, the method of producing a polypeptide of the present invention further includes the step of isolating the expressed polypeptide from host cells and/or media. More preferably, the method also includes the step of purifying the isolated polypeptide using purification means known in the art, such as centrifugation, gel permeation chromatography, affinity chromatography, etc.

The present invention also provides a method for producing VLPs, as defined herein, comprising the step of incubating a solution of the polypeptide under conditions allowing the polypeptide to assemble into the VLPs, as previously described. Proper formation of HPV can be verified by examining the sample solution using an electron microscope.

BRIEF DESCRIPTION OF GRAPHIC MATERIALS

Fig. 1: (A) Dodecahedrons formed by the base proteins of specific adenovirus serotypes constitute a universal scaffold. (B) They contain 60 copies of the adenovirus base protein, which can be divided into a crown domain (orange) and a multimerization domain (blue). In the multimerization domain, the ends formed by cleavage can be reconnected by short oligopeptide linkers to form continuous polypeptide chains. The N-terminus and C-terminus of the base protein are contained in the multimerization domain.

Fig. 2: Diagram of a roll-fold domain of a preferred embodiment of a polypeptide of the present invention based on the penton base protomer hAd3.

Fig. 3: The adenovirus base protein is shown schematically on the far left. The crown domain (see Fig. 1) is colored yellow, the multimerization domain is colored blue. The N- and C-termini of the base protein are contained in a multimerization domain that mediates penton and dodecahedron formation. Removal of the crown domain results in an autonomous multimerization domain which, instead of the former crown domain, now contains oligopeptides, polypeptides, proteins or protein complexes, as shown schematically in a middle-to-right direction. Multimerization domains now give rise to virus-like particles presenting said particles on their surface. Naturally, corona domains and engineered corona domains derived from a number of adenovirus serotypes can also be adapted to a multimerization domain framework, including engineered corona domains containing heterologous peptide and polypeptide sequences.

Fig. 4: The adenovirus-derived dodecahedral platform (ADDomer) is shown schematically. The original particle is shown on the left. The base protein is formed by a multimerization domain (blue) and a crown domain (yellow). 60 base proteins form virus-like particles (VLPs). Shown on the right are ADDomers displaying (instead of a crown domain) multiple copies of oligopeptides, polypeptides and protein domains, proteins or protein complexes. Color coding as in fig. 3.

Fig. 5: Schematic representation of the vector pACEBac VAJB-CHIK.

The present invention is further illustrated by the following non-limiting example:

Example

The nucleic acid with the sequence designated DNAsegVAJB-CHIK (SEQ ID NO: 26, flanked by a BamHI site at the 5' end and a HindIII site at the 3' end, ggatcc at the beginning of the sequence and aagctt at the end of the sequence) was obtained from a commercial supplier:

The construct was cloned into the pACEBac transfer plasmid (Geneva Biotech, Geneva, Switzerland) using BamHI and HindIII cleavage sites, resulting in the pACEBac construct VAJB-CHIK (SEQ ID NO: 27):

DNA sequencing was used to verify the correctness of the insertion. The open reading frame encodes the protein VAJB-CHIK (SEQ ID NO: 28), which contains the major neutralizing epitope of chikungunya virus STKDNFNVYKATRPYLAH (SEQ ID NO: 29) in the L1 loop.

VAJB-CHIK (SEQ ID NO: 28):

pACEBac_VAJB-CHIK was then used to transform DHlOEMBacY cells (Geneva Biotech, Geneva, Switzerland) carrying the EMBacY viral genome as an artificial chromosome (described in Fitzgerald DJ et al. Nat Methods. 2006 Dec, 3(12): 1021-32 PMID: 17117155). A composite baculovirus with an expression cassette for VAJB1 integrated via Tn7 transposition into DHlOEMBacY cells was then identified by blue/white screening, and the recombinant baculovirus was produced as described (ibid.). Insect cell cultures of Spodoptera frugiperda line 21 (Sf21) were infected with baculovirus OM prepared as described in Fitzgerald et al. (2006) Nat Methods, see above.

Large scale (100 to 500 ml) expression was carried out in Trichoplusia ni Hi5 cells in shake flasks and expression of the recombinant protein followed by measurement of yellow fluorescent protein (YFP) fluorescence as described (Fitzgerald DJ et Nat Methods. 2006 Dec;3(12): 1021-32 PMID: 17117155). When YFP fluorescence reached a plateau (usually 72 hours after cell proliferation had ceased, see Fitzgerald et al, Nat Methods 2006), insect cell cultures were harvested and cells pelleted by centrifugation (4000 g, 10 min). The cells were frozen in liquid nitrogen and stored at minus 80 degrees Celsius.

To obtain protein, cells were lysed by freeze-thawing in phosphate-buffered saline (PBS) containing whole cocktail of protease inhibitors (Roche Ltd). The protein was purified by applying a sucrose gradient from 15 to 40% w/v. sucrose and ultracentrifugation overnight at 100,000 g. The gradient was collected and protein content was determined by denaturing polyacrylamide gel electrophoresis (SDS-PAGE) followed by Coomassie brilliant blue staining. Fractions containing VAJB1 were pooled and dialyzed against PBS (or 10 mM HEPES, pH 7.4, 50 mM NaCl). The second purification step was performed on a 5 mL HiQ column (BioRAD) using a linear gradient from 50 to 500 mM NaCl. The formation of pentamer and dodecamer was confirmed by electron microscopy with negative staining (uranyl acetate).

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LIST OF SEQUENCES

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Ile Ile Asp Asn Tyr Leu Ala Val Gly Arg Gln Asn Gly Val Leu Glu

195 200 205

Ser Asp Ile Gly Val Lys Phe Asp Thr Arg Asn Phe Arg Leu Gly Trp

210 215 220

Asp Pro Val Thr Glu Leu Val Met Pro Gly Val Tyr Thr Asn Glu Ala

225 230 235 240

Phe His Pro Asp Ile Val Leu Leu Pro Gly Cys Gly Val Asp Phe Thr

245 250 255

Glu Ser Arg Leu Ser Asn Leu Leu Gly Ile Arg Lys Arg Gln Pro Phe

260 265 270

Gln Glu Gly Phe Gln Ile Met Tyr Glu Asp Leu Asp Gly Gly Asn Ile

275 280 285

Pro Ala Leu Leu Asp Val Glu Ala Tyr Glu Lys Ser Lys Glu Glu Ser

290 295 300

Val Ala Ala Ala Thr Thr Ala Val Ala Thr Ala Ser Thr Glu Val Arg

305 310 315 320

Asp Asp Asn Phe Ala Ser Ala Ala Ala Val Ala Ala Val Lys Ala Asp

325 330 335

Glu Thr Lys Ser Lys Ile Val Ile Gln Pro Val Glu Lys Asp Ser Lys

340 345 350

Glu Arg Ser Tyr Asn Val Leu Ser Asp Lys Lys Asn Thr Ala Tyr Arg

355 360 365

Ser Trp Tyr Leu Ala Tyr Asn Tyr Gly Asp Arg Asp Lys Gly Val Arg

370 375 380

Ser Trp Thr Leu Leu Thr Thr Ser Asp Val Thr Cys Gly Val Glu Gln

385 390 395 400

Val Tyr Trp Ser Leu Pro Asp Met Met Gln Asp Pro Val Thr Phe Arg

405 410 415

Ser Thr His Gln Val Ser Asn Tyr Pro Val Val Gly Ala Glu Leu Leu

420 425 430

Pro Val Tyr Ser Lys Ser Phe Phe Asn Glu Gln Ala Val Tyr Ser Gln

435 440 445

Gln Leu Arg Ala Phe Thr Ser Leu Thr His Val Phe Asn Arg Phe Pro

450 455 460

Glu Asn Gln Ile Leu Val Arg Pro Pro Ala Pro Thr Ile Thr Thr Val

465 470 475 480

Ser Glu Asn Val Pro Ala Leu Thr Asp His Gly Thr Leu Pro Leu Arg

485 490 495

Ser Ser Ile Arg Gly Val Gln Arg Val Thr Val Thr Asp Ala Arg Arg

500 505 510

Arg Thr Cys Pro Tyr Val Tyr Lys Ala Leu Gly Ile Val Ala Pro Arg

515 520 525

Val Leu Ser Ser Arg Thr Phe

530 535

<210> 4

<211> 571

<212> PRT

<213> Human adenovirus C serotype 5

<400> 4

Met Arg Arg Ala Ala Met Tyr Glu Glu Gly Pro Pro Pro Ser Tyr Glu

1 5 10 15

Ser Val Val Ser Ala Ala Pro Val Ala Ala Ala Leu Gly Ser Pro Phe

20 25 30

Asp Ala Pro Leu Asp Pro Pro Phe Val Pro Pro Arg Tyr Leu Arg Pro

35 40 45

Thr Gly Gly Arg Asn Ser Ile Arg Tyr Ser Glu Leu Ala Pro Leu Phe

50 55 60

Asp Thr Thr Arg Val Tyr Leu Val Asp Asn Lys Ser Thr Asp Val Ala

65 70 75 80

Ser Leu Asn Tyr Gln Asn Asp His Ser Asn Phe Leu Thr Thr Val Ile

85 90 95

Gln Asn Asn Asp Tyr Ser Pro Gly Glu Ala Ser Thr Gln Thr Ile Asn

100 105 110

Leu Asp Asp Arg Ser His Trp Gly Gly Asp Leu Lys Thr Ile Leu His

115 120 125

Thr Asn Met Pro Asn Val Asn Glu Phe Met Phe Thr Asn Lys Phe Lys

130 135 140

Ala Arg Val Met Val Ser Arg Leu Pro Thr Lys Asp Asn Gln Val Glu

145 150 155 160

Leu Lys Tyr Glu Trp Val Glu Phe Thr Leu Pro Glu Gly Asn Tyr Ser

165 170 175

Glu Thr Met Thr Ile Asp Leu Met Asn Asn Ala Ile Val Glu His Tyr

180 185 190

Leu Lys Val Gly Arg Gln Asn Gly Val Leu Glu Ser Asp Ile Gly Val

195 200 205

Lys Phe Asp Thr Arg Asn Phe Arg Leu Gly Phe Asp Pro Val Thr Gly

210 215 220

Leu Val Met Pro Gly Val Tyr Thr Asn Glu Ala Phe His Pro Asp Ile

225 230 235 240

Ile Leu Leu Pro Gly Cys Gly Val Asp Phe Thr His Ser Arg Leu Ser

245 250 255

Asn Leu Leu Gly Ile Arg Lys Arg Gln Pro Phe Gln Glu Gly Phe Arg

260 265 270

Ile Thr Tyr Asp Asp Leu Glu Gly Gly Asn Ile Pro Ala Leu Leu Asp

275 280 285

Val Asp Ala Tyr Gln Ala Ser Leu Lys Asp Asp Thr Glu Gln Gly Gly

290 295 300

Gly Gly Ala Gly Gly Ser Asn Ser Ser Gly Ser Gly Ala Glu Glu Asn

305 310 315 320

Ser Asn Ala Ala Ala Ala Ala Met Gln Pro Val Glu Asp Met Asn Asp

325 330 335

His Ala Ile Arg Gly Asp Thr Phe Ala Thr Arg Ala Glu Glu Lys Arg

340 345 350

Ala Glu Ala Glu Ala Ala Ala Glu Ala Ala Ala Pro Ala Ala Gln Pro

355 360 365

Glu Val Glu Lys Pro Gln Lys Lys Pro Val Ile Lys Pro Leu Thr Glu

370 375 380

Asp Ser Lys Lys Arg Ser Tyr Asn Leu Ile Ser Asn Asp Ser Thr Phe

385 390 395 400

Thr Gln Tyr Arg Ser Trp Tyr Leu Ala Tyr Asn Tyr Gly Asp Pro Gln

405 410 415

Thr Gly Ile Arg Ser Trp Thr Leu Leu Cys Thr Pro Asp Val Thr Cys

420 425 430

Gly Ser Glu Gln Val Tyr Trp Ser Leu Pro Asp Met Met Gln Asp Pro

435 440 445

Val Thr Phe Arg Ser Thr Arg Gln Ile Ser Asn Phe Pro Val Val Gly

450 455 460

Ala Glu Leu Leu Pro Val His Ser Lys Ser Phe Tyr Asn Asp Gln Ala

465 470 475 480

Val Tyr Ser Gln Leu Ile Arg Gln Phe Thr Ser Leu Thr His Val Phe

485 490 495

Asn Arg Phe Pro Glu Asn Gln Ile Leu Ala Arg Pro Pro Ala Pro Thr

500 505 510

Ile Thr Thr Val Ser Glu Asn Val Pro Ala Leu Thr Asp His Gly Thr

515 520 525

Leu Pro Leu Arg Asn Ser Ile Gly Gly Val Gln Arg Val Thr Ile Thr

530 535 540

Asp Ala Arg Arg Arg Thr Cys Pro Tyr Val Tyr Lys Ala Leu Gly Ile

545 550 555 560

Val Ser Pro Arg Val Leu Ser Ser Arg Thr Phe

565 570

<210> 5

<211> 544

<212> PRT

<213> Human adenovirus B serotype 7

<400> 5

Met Arg Arg Arg Ala Val Leu Gly Gly Ala Met Val Tyr Pro Glu Gly

1 5 10 15

Pro Pro Pro Ser Tyr Glu Ser Val Met Gln Gln Gln Ala Ala Met Ile

20 25 30

Gln Pro Pro Leu Glu Ala Pro Phe Val Pro Pro Arg Tyr Leu Ala Pro

35 40 45

Thr Glu Gly Arg Asn Ser Ile Arg Tyr Ser Glu Leu Ser Pro Leu Tyr

50 55 60

Asp Thr Thr Lys Leu Tyr Leu Val Asp Asn Lys Ser Ala Asp Ile Ala

65 70 75 80

Ser Leu Asn Tyr Gln Asn Asp His Ser Asn Phe Leu Thr Thr Val Val

85 90 95

Gln Asn Asn Asp Phe Thr Pro Thr Glu Ala Ser Thr Gln Thr Ile Asn

100 105 110

Phe Asp Glu Arg Ser Arg Trp Gly Gly Gln Leu Lys Thr Ile Met His

115 120 125

Thr Asn Met Pro Asn Val Asn Glu Tyr Met Phe Ser Asn Lys Phe Lys

130 135 140

Ala Arg Val Met Val Ser Arg Lys Ala Pro Glu Gly Val Ile Val Asn

145 150 155 160

Asp Thr Tyr Asp His Lys Glu Asp Ile Leu Lys Tyr Glu Trp Phe Glu

165 170 175

Phe Thr Leu Pro Glu Gly Asn Phe Ser Ala Thr Met Thr Ile Asp Leu

180 185 190

Met Asn Asn Ala Ile Ile Asp Asn Tyr Leu Glu Ile Gly Arg Gln Asn

195 200 205

Gly Val Leu Glu Ser Asp Ile Gly Val Lys Phe Asp Thr Arg Asn Phe

210 215 220

Arg Leu Gly Trp Asp Pro Glu Thr Lys Leu Ile Met Pro Gly Val Tyr

225 230 235 240

Thr Tyr Glu Ala Phe His Pro Asp Ile Val Leu Leu Pro Gly Cys Gly

245 250 255

Val Asp Phe Thr Glu Ser Arg Leu Ser Asn Leu Leu Gly Ile Arg Lys

260 265 270

Arg His Pro Phe Gln Glu Gly Phe Lys Ile Met Tyr Glu Asp Leu Glu

275 280 285

Gly Gly Asn Ile Pro Ala Leu Leu Asp Val Thr Ala Tyr Glu Glu Ser

290 295 300

Lys Lys Asp Thr Thr Thr Glu Thr Thr Thr Leu Ala Val Ala Glu Glu

305 310 315 320

Thr Ser Glu Asp Asp Asn Ile Thr Arg Gly Asp Thr Tyr Ile Thr Glu

325 330 335

Lys Gln Lys Arg Glu Ala Ala Ala Ala Glu Val Lys Lys Glu Leu Lys

340 345 350

Ile Gln Pro Leu Glu Lys Asp Ser Lys Ser Arg Ser Tyr Asn Val Leu

355 360 365

Glu Asp Lys Ile Asn Thr Ala Tyr Arg Ser Trp Tyr Leu Ser Tyr Asn

370 375 380

Tyr Gly Asn Pro Glu Lys Gly Ile Arg Ser Trp Thr Leu Leu Thr Thr

385 390 395 400

Ser Asp Val Thr Cys Gly Ala Glu Gln Val Tyr Trp Ser Leu Pro Asp

405 410 415

Met Met Gln Asp Pro Val Thr Phe Arg Ser Thr Arg Gln Val Asn Asn

420 425 430

Tyr Pro Val Val Gly Ala Glu Leu Met Pro Val Phe Ser Lys Ser Phe

435 440 445

Tyr Asn Glu Gln Ala Val Tyr Ser Gln Gln Leu Arg Gln Ala Thr Ser

450 455 460

Leu Thr His Val Phe Asn Arg Phe Pro Glu Asn Gln Ile Leu Ile Arg

465 470 475 480

Pro Pro Ala Pro Thr Ile Thr Thr Val Ser Glu Asn Val Pro Ala Leu

485 490 495

Thr Asp His Gly Thr Leu Pro Leu Arg Ser Ser Ile Arg Gly Val Gln

500 505 510

Arg Val Thr Val Thr Asp Ala Arg Arg Arg Thr Cys Pro Tyr Val Tyr

515 520 525

Lys Ala Leu Gly Ile Val Ala Pro Arg Val Leu Ser Ser Arg Thr Phe

530 535 540

<210> 6

<211> 557

<212> PRT

<213> Human adenovirus B serotype 11

<400> 6

Met Arg Arg Val Val Leu Gly Gly Ala Val Val Tyr Pro Glu Gly Pro

1 5 10 15

Pro Pro Ser Tyr Glu Ser Val Met Gln Gln Gln Ala Thr Ala Val Met

20 25 30

Gln Ser Pro Leu Glu Ala Pro Phe Val Pro Pro Arg Tyr Leu Ala Pro

35 40 45

Thr Glu Gly Arg Asn Ser Ile Arg Tyr Ser Glu Leu Ala Pro Gln Tyr

50 55 60

Asp Thr Thr Arg Leu Tyr Leu Val Asp Asn Lys Ser Ala Asp Ile Ala

65 70 75 80

Ser Leu Asn Tyr Gln Asn Asp His Ser Asn Phe Leu Thr Thr Val Val

85 90 95

Gln Asn Asn Asp Phe Thr Pro Thr Glu Ala Ser Thr Gln Thr Ile Asn

100 105 110

Phe Asp Glu Arg Ser Arg Trp Gly Gly Gln Leu Lys Thr Ile Met His

115 120 125

Thr Asn Met Pro Asn Val Asn Glu Tyr Met Phe Ser Asn Asn Phe Lys

130 135 140

Ala Arg Val Met Val Ser Arg Lys Pro Pro Glu Gly Ala Ala Val Gly

145 150 155 160

Asp Thr Tyr Asp His Lys Gln Asp Ile Leu Glu Tyr Glu Trp Phe Glu

165 170 175

Phe Thr Leu Pro Glu Gly Asn Phe Ser Val Thr Met Thr Ile Asp Leu

180 185 190

Met Asn Asn Ala Ile Ile Asp Asn Tyr Leu Lys Val Gly Arg Gln Asn

195 200 205

Gly Val Leu Glu Ser Asp Ile Gly Val Lys Phe Asp Thr Arg Asn Phe

210 215 220

Lys Leu Gly Trp Asp Pro Glu Thr Lys Leu Ile Met Pro Gly Val Tyr

225 230 235 240

Thr Tyr Glu Ala Phe His Pro Asp Ile Val Leu Leu Pro Gly Cys Gly

245 250 255

Val Asp Phe Thr Glu Ser Arg Leu Ser Asn Leu Leu Gly Ile Arg Lys

260 265 270

Lys Gln Pro Phe Gln Glu Gly Phe Lys Ile Leu Tyr Glu Asp Leu Glu

275 280 285

Gly Gly Asn Ile Pro Ala Leu Leu Asp Val Asp Ala Tyr Glu Asn Ser

290 295 300

Lys Lys Glu Gln Lys Ala Lys Ile Glu Ala Ala Ala Glu Ala Lys Ala

305 310 315 320

Asn Ile Val Ala Ser Asp Ser Thr Arg Val Ala Asn Ala Gly Glu Val

325 330 335

Arg Gly Asp Asn Phe Ala Pro Thr Pro Val Pro Thr Ala Glu Ser Leu

340 345 350

Leu Ala Asp Val Ser Gly Gly Thr Asp Val Lys Leu Thr Ile Gln Pro

355 360 365

Val Glu Lys Asp Ser Lys Asn Arg Ser Tyr Asn Val Leu Glu Asp Lys

370 375 380

Ile Asn Thr Ala Tyr Arg Ser Trp Tyr Leu Ser Tyr Asn Tyr Gly Asp

385 390 395 400

Pro Glu Lys Gly Val Arg Ser Trp Thr Leu Leu Thr Thr Ser Asp Val

405 410 415

Thr Cys Gly Ala Glu Gln Val Tyr Trp Ser Leu Pro Asp Met Met Gln

420 425 430

Asp Pro Val Thr Phe Arg Ser Thr Arg Gln Val Ser Asn Tyr Pro Val

435 440 445

Val Gly Ala Glu Leu Met Pro Val Phe Ser Lys Ser Phe Tyr Asn Glu

450 455 460

Gln Ala Val Tyr Ser Gln Gln Leu Arg Gln Ser Thr Ser Leu Thr His

465 470 475 480

Val Phe Asn Arg Phe Pro Glu Asn Gln Ile Leu Ile Arg Pro Pro Ala

485 490 495

Pro Thr Ile Thr Thr Val Ser Glu Asn Val Pro Ala Leu Thr Asp His

500 505 510

Gly Thr Leu Pro Leu Arg Ser Ser Ile Arg Gly Val Gln Arg Val Thr

515 520 525

Val Thr Asp Ala Arg Arg Arg Thr Cys Pro Tyr Val Tyr Lys Ala Leu

530 535 540

Gly Ile Val Ala Pro Arg Val Leu Ser Ser Arg Thr Phe

545 550 555

<210> 7

<211> 497

<212> PRT

<213> Human adenovirus A serotype 12

<400> 7

Met Arg Arg Ala Val Glu Leu Gln Thr Val Ala Phe Pro Glu Thr Pro

1 5 10 15

Pro Pro Ser Tyr Glu Thr Val Met Ala Ala Ala Pro Pro Tyr Val Pro

20 25 30

Pro Arg Tyr Leu Gly Pro Thr Glu Gly Arg Asn Ser Ile Arg Tyr Ser

35 40 45

Glu Leu Ser Pro Leu Tyr Asp Thr Thr Arg Val Tyr Leu Val Asp Asn

50 55 60

Lys Ser Ser Asp Ile Ala Ser Leu Asn Tyr Gln Asn Asp His Ser Asn

65 70 75 80

Phe Leu Thr Thr Val Val Gln Asn Asn Asp Tyr Ser Pro Ile Glu Ala

85 90 95

Gly Thr Gln Thr Ile Asn Phe Asp Glu Arg Ser Arg Trp Gly Gly Asp

100 105 110

Leu Lys Thr Ile Leu His Thr Asn Met Pro Asn Val Asn Asp Phe Met

115 120 125

Phe Thr Thr Lys Phe Lys Ala Arg Val Met Val Ala Arg Lys Thr Asn

130 135 140

Asn Glu Gly Gln Thr Ile Leu Glu Tyr Glu Trp Ala Glu Phe Val Leu

145 150 155 160

Pro Glu Gly Asn Tyr Ser Glu Thr Met Thr Ile Asp Leu Met Asn Asn

165 170 175

Ala Ile Ile Glu His Tyr Leu Arg Val Gly Arg Gln His Gly Val Leu

180 185 190

Glu Ser Asp Ile Gly Val Lys Phe Asp Thr Arg Asn Phe Arg Leu Gly

195 200 205

Trp Asp Pro Glu Thr Gln Leu Val Thr Pro Gly Val Tyr Thr Asn Glu

210 215 220

Ala Phe His Pro Asp Ile Val Leu Leu Pro Gly Cys Gly Val Asp Phe

225 230 235 240

Thr Glu Ser Arg Leu Ser Asn Ile Leu Gly Ile Arg Lys Arg Gln Pro

245 250 255

Phe Gln Glu Gly Phe Val Ile Met Tyr Glu His Leu Glu Gly Gly Asn

260 265 270

Ile Pro Ala Leu Leu Asp Val Lys Lys Tyr Glu Asn Ser Leu Gln Asp

275 280 285

Gln Asn Thr Val Arg Gly Asp Asn Phe Ile Ala Leu Asn Lys Ala Ala

290 295 300

Arg Ile Glu Pro Val Glu Thr Asp Pro Lys Gly Arg Ser Tyr Asn Leu

305 310 315 320

Leu Pro Asp Lys Lys Asn Thr Lys Tyr Arg Ser Trp Tyr Leu Ala Tyr

325 330 335

Asn Tyr Gly Asp Pro Glu Lys Gly Val Arg Ser Trp Thr Leu Leu Thr

340 345 350

Thr Pro Asp Val Thr Gly Gly Ser Glu Gln Val Tyr Trp Ser Leu Pro

355 360 365

Asp Met Met Gln Asp Pro Val Thr Phe Arg Ser Ser Arg Gln Val Ser

370 375 380

Asn Tyr Pro Val Val Ala Ala Glu Leu Leu Pro Val His Ala Lys Ser

385 390 395 400

Phe Tyr Asn Glu Gln Ala Val Tyr Ser Gln Leu Ile Arg Gln Ser Thr

405 410 415

Ala Leu Thr Arg Val Phe Asn Arg Phe Pro Glu Asn Gln Ile Leu Val

420 425 430

Arg Pro Pro Ala Ala Thr Ile Thr Thr Val Ser Glu Asn Val Pro Ala

435 440 445

Leu Thr Asp His Gly Thr Leu Pro Leu Arg Ser Ser Ile Ser Gly Val

450 455 460

Gln Arg Val Thr Ile Thr Asp Ala Arg Arg Arg Thr Cys Pro Tyr Val

465 470 475 480

Tyr Lys Ala Leu Gly Ile Val Ser Pro Arg Val Leu Ser Ser Arg Thr

485 490 495

Phe

<210> 8

<211> 517

<212> PRT

<213> Human adenovirus D serotype 17

<400> 8

Met Arg Arg Ala Val Val Ser Ser Ser Pro Pro Pro Ser Tyr Glu Ser

1 5 10 15

Val Met Ala Gln Ala Thr Leu Glu Val Pro Phe Val Pro Pro Arg Tyr

20 25 30

Met Ala Pro Thr Glu Gly Arg Asn Ser Ile Arg Tyr Ser Glu Leu Ala

35 40 45

Pro Leu Tyr Asp Thr Thr Arg Val Tyr Leu Val Asp Asn Lys Ser Ala

50 55 60

Asp Ile Ala Ser Leu Asn Tyr Gln Asn Asp His Ser Asn Phe Leu Thr

65 70 75 80

Thr Val Val Gln Asn Asn Asp Phe Thr Pro Ala Glu Ala Ser Thr Gln

85 90 95

Thr Ile Asn Phe Asp Glu Arg Ser Arg Trp Gly Gly Asp Leu Lys Thr

100 105 110

Ile Leu His Thr Asn Met Pro Asn Val Asn Glu Tyr Met Phe Thr Ser

115 120 125

Lys Phe Lys Ala Arg Val Met Val Ala Arg Lys His Pro Gln Gly Val

130 135 140

Glu Ala Thr Asp Leu Ser Lys Asp Ile Leu Glu Tyr Glu Trp Phe Glu

145 150 155 160

Phe Thr Leu Pro Glu Gly Asn Phe Ser Glu Thr Met Thr Ile Asp Leu

165 170 175

Met Asn Asn Ala Ile Leu Glu Asn Tyr Leu Gln Val Gly Arg Gln Asn

180 185 190

Gly Val Leu Glu Ser Asp Ile Gly Val Lys Phe Asp Ser Arg Asn Phe

195 200 205

Lys Leu Gly Trp Asp Pro Val Thr Lys Leu Val Met Pro Gly Val Tyr

210 215 220

Thr Tyr Glu Ala Phe His Pro Asp Val Val Leu Leu Pro Gly Cys Gly

225 230 235 240

Val Asp Phe Thr Glu Ser Arg Leu Ser Asn Leu Leu Gly Ile Arg Lys

245 250 255

Lys Gln Pro Phe Gln Glu Gly Phe Arg Ile Met Tyr Glu Asp Leu Glu

260 265 270

Gly Gly Asn Ile Pro Ala Leu Leu Asp Val Pro Lys Tyr Leu Glu Ser

275 280 285

Lys Lys Lys Leu Glu Glu Ala Leu Glu Asn Ala Ala Lys Ala Asn Gly

290 295 300

Pro Ala Arg Gly Asp Ser Ser Val Ser Arg Glu Val Glu Lys Ala Ala

305 310 315 320

Glu Lys Glu Leu Val Ile Glu Pro Ile Lys Gln Asp Asp Ser Lys Arg

325 330 335

Ser Tyr Asn Leu Ile Glu Gly Thr Met Asp Thr Leu Tyr Arg Ser Trp

340 345 350

Tyr Leu Ser Tyr Thr Tyr Gly Asp Pro Glu Lys Gly Val Gln Ser Trp

355 360 365

Thr Leu Leu Thr Thr Pro Asp Val Thr Cys Gly Ala Glu Gln Val Tyr

370 375 380

Trp Ser Leu Pro Asp Leu Met Gln Asp Pro Val Thr Phe Arg Ser Thr

385 390 395 400

Gln Gln Val Ser Asn Tyr Pro Val Val Gly Ala Glu Leu Met Pro Phe

405 410 415

Arg Ala Lys Ser Phe Tyr Asn Asp Leu Ala Val Tyr Ser Gln Leu Ile

420 425 430

Arg Ser Tyr Thr Ser Leu Thr His Val Phe Asn Arg Phe Pro Asp Asn

435 440 445

Gln Ile Leu Cys Arg Pro Pro Ala Pro Thr Ile Thr Thr Val Ser Glu

450 455 460

Asn Val Pro Ala Leu Thr Asp His Gly Thr Leu Pro Leu Arg Ser Ser

465 470 475 480

Ile Arg Gly Val Gln Arg Val Thr Val Thr Asp Ala Arg Arg Arg Thr

485 490 495

Cys Pro Tyr Val Tyr Lys Ala Leu Gly Ile Val Ala Pro Arg Val Leu

500 505 510

Ser Ser Arg Thr Phe

515

<210> 9

<211> 520

<212> PRT

<213> Human adenovirus 25

<400> 9

Met Arg Arg Ala Val Val Ser Ser Ser Pro Pro Pro Ser Tyr Glu Ser

1 5 10 15

Val Met Ala Gln Ala Thr Leu Glu Val Pro Phe Val Pro Pro Arg Tyr

20 25 30

Met Ala Pro Thr Glu Gly Arg Asn Ser Ile Arg Tyr Ser Glu Leu Ala

35 40 45

Pro Gln Tyr Asp Thr Thr Arg Val Tyr Leu Val Asp Asn Lys Ser Ala

50 55 60

Asp Ile Ala Ser Leu Asn Tyr Gln Asn Asp His Ser Asn Phe Leu Thr

65 70 75 80

Thr Val Val Gln Asn Asn Asp Phe Thr Pro Ala Glu Ala Ser Thr Gln

85 90 95

Thr Ile Asn Phe Asp Glu Arg Ser Arg Trp Gly Gly Asp Leu Lys Thr

100 105 110

Ile Leu His Thr Asn Met Pro Asn Val Asn Glu Tyr Met Phe Thr Ser

115 120 125

Lys Phe Lys Ala Arg Val Met Val Ala Arg Lys His Pro Glu Asn Val

130 135 140

Asp Lys Thr Asp Leu Ser Gln Asp Lys Leu Glu Tyr Glu Trp Phe Glu

145 150 155 160

Phe Thr Leu Pro Glu Gly Asn Phe Ser Glu Thr Met Thr Ile Asp Leu

165 170 175

Met Asn Asn Ala Ile Leu Glu Asn Tyr Leu Gln Val Gly Arg Gln Asn

180 185 190

Gly Val Leu Glu Ser Asp Ile Gly Val Lys Phe Asp Ser Arg Asn Phe

195 200 205

Lys Leu Gly Trp Asp Pro Val Thr Lys Leu Val Met Pro Gly Val Tyr

210 215 220

Thr Tyr Glu Ala Phe His Pro Asp Val Val Leu Leu Pro Gly Cys Gly

225 230 235 240

Val Asp Phe Thr Glu Ser Arg Leu Ser Asn Leu Leu Gly Ile Arg Lys

245 250 255

Lys Gln Pro Phe Gln Glu Gly Phe Arg Ile Met Tyr Glu Asp Leu Glu

260 265 270

Gly Gly Asn Ile Pro Ala Leu Leu Asp Thr Lys Lys Tyr Leu Asp Ser

275 280 285

Lys Lys Glu Leu Glu Asp Ala Ala Lys Glu Ala Ala Lys Gln Gln Gly

290 295 300

Asp Gly Ala Val Thr Arg Gly Asp Thr His Leu Thr Val Ala Gln Glu

305 310 315 320

Lys Ala Ala Glu Lys Glu Leu Val Ile Val Pro Ile Glu Lys Asp Glu

325 330 335

Ser Asn Arg Ser Tyr Asn Leu Ile Lys Asp Thr His Asp Thr Met Tyr

340 345 350

Arg Ser Trp Tyr Leu Ser Tyr Thr Tyr Gly Asp Pro Glu Lys Gly Val

355 360 365

Gln Ser Trp Thr Leu Leu Thr Thr Pro Asp Val Thr Cys Gly Ala Glu

370 375 380

Gln Val Tyr Trp Ser Leu Pro Asp Leu Met Gln Asp Pro Val Thr Phe

385 390 395 400

Arg Ser Thr Gln Gln Val Ser Asn Tyr Pro Val Val Gly Ala Glu Leu

405 410 415

Met Pro Phe Arg Ala Lys Ser Phe Tyr Asn Asp Leu Ala Val Tyr Ser

420 425 430

Gln Leu Ile Arg Ser Tyr Thr Ser Leu Thr His Val Phe Asn Arg Phe

435 440 445

Pro Asp Asn Gln Ile Leu Cys Arg Pro Pro Ala Pro Thr Ile Thr Thr

450 455 460

Val Ser Glu Asn Val Pro Ala Leu Thr Asp His Gly Thr Leu Pro Leu

465 470 475 480

Arg Ser Ser Ile Arg Gly Val Gln Arg Val Thr Val Thr Asp Ala Arg

485 490 495

Arg Arg Thr Cys Pro Tyr Val Tyr Lys Ala Leu Gly Ile Val Ala Pro

500 505 510

Arg Val Leu Ser Ser Arg Thr Phe

515 520

<210> 10

<211> 561

<212> PRT

<213> Human adenovirus B serotype 35

<400> 10

Met Arg Arg Val Val Leu Gly Gly Ala Val Val Tyr Pro Glu Gly Pro

1 5 10 15

Pro Pro Ser Tyr Glu Ser Val Met Gln Gln Gln Gln Ala Thr Ala Val

20 25 30

Met Gln Ser Pro Leu Glu Ala Pro Phe Val Pro Pro Arg Tyr Leu Ala

35 40 45

Pro Thr Glu Gly Arg Asn Ser Ile Arg Tyr Ser Glu Leu Ala Pro Gln

50 55 60

Tyr Asp Thr Thr Arg Leu Tyr Leu Val Asp Asn Lys Ser Ala Asp Ile

65 70 75 80

Ala Ser Leu Asn Tyr Gln Asn Asp His Ser Asn Phe Leu Thr Thr Val

85 90 95

Val Gln Asn Asn Asp Phe Thr Pro Thr Glu Ala Ser Thr Gln Thr Ile

100 105 110

Asn Phe Asp Glu Arg Ser Arg Trp Gly Gly Gln Leu Lys Thr Ile Met

115 120 125

His Thr Asn Met Pro Asn Val Asn Glu Tyr Met Phe Ser Asn Lys Phe

130 135 140

Lys Ala Arg Val Met Val Ser Arg Lys Pro Pro Asp Gly Ala Ala Val

145 150 155 160

Gly Asp Thr Tyr Asp His Lys Gln Asp Ile Leu Glu Tyr Glu Trp Phe

165 170 175

Glu Phe Thr Leu Pro Glu Gly Asn Phe Ser Val Thr Met Thr Ile Asp

180 185 190

Leu Met Asn Asn Ala Ile Ile Asp Asn Tyr Leu Lys Val Gly Arg Gln

195 200 205

Asn Gly Val Leu Glu Ser Asp Ile Gly Val Lys Phe Asp Thr Arg Asn

210 215 220

Phe Lys Leu Gly Trp Asp Pro Glu Thr Lys Leu Ile Met Pro Gly Val

225 230 235 240

Tyr Thr Tyr Glu Ala Phe His Pro Asp Ile Val Leu Leu Pro Gly Cys

245 250 255

Gly Val Asp Phe Thr Glu Ser Arg Leu Ser Asn Leu Leu Gly Ile Arg

260 265 270

Lys Lys Gln Pro Phe Gln Glu Gly Phe Lys Ile Leu Tyr Glu Asp Leu

275 280 285

Glu Gly Gly Asn Ile Pro Ala Leu Leu Asp Val Asp Ala Tyr Glu Asn

290 295 300

Ser Lys Lys Glu Gln Lys Ala Lys Ile Glu Ala Ala Thr Ala Ala Ala

305 310 315 320

Glu Ala Lys Ala Asn Ile Val Ala Ser Asp Ser Thr Arg Val Ala Asn

325 330 335

Ala Gly Glu Val Arg Gly Asp Asn Phe Ala Pro Thr Pro Val Pro Thr

340 345 350

Ala Glu Ser Leu Leu Ala Asp Val Ser Glu Gly Thr Asp Val Lys Leu

355 360 365

Thr Ile Gln Pro Val Glu Lys Asp Ser Lys Asn Arg Ser Tyr Asn Val

370 375 380

Leu Glu Asp Lys Ile Asn Thr Ala Tyr Arg Ser Trp Tyr Leu Ser Tyr

385 390 395 400

Asn Tyr Gly Asp Pro Glu Lys Gly Val Arg Ser Trp Thr Leu Leu Thr

405 410 415

Thr Ser Asp Val Thr Cys Gly Ala Glu Gln Val Tyr Trp Ser Leu Pro

420 425 430

Asp Met Met Lys Asp Pro Val Thr Phe Arg Ser Thr Arg Gln Val Ser

435 440 445

Asn Tyr Pro Val Val Gly Ala Glu Leu Met Pro Val Phe Ser Lys Ser

450 455 460

Phe Tyr Asn Glu Gln Ala Val Tyr Ser Gln Gln Leu Arg Gln Ser Thr

465 470 475 480

Ser Leu Thr His Val Phe Asn Arg Phe Pro Glu Asn Gln Ile Leu Ile

485 490 495

Arg Pro Pro Ala Pro Thr Ile Thr Thr Val Ser Glu Asn Val Pro Ala

500 505 510

Leu Thr Asp His Gly Thr Leu Pro Leu Arg Ser Ser Ile Arg Gly Val

515 520 525

Gln Arg Val Thr Val Thr Asp Ala Arg Arg Arg Thr Cys Pro Tyr Val

530 535 540

Tyr Lys Ala Leu Gly Ile Val Ala Pro Arg Val Leu Ser Ser Arg Thr

545 550 555 560

Phe

<210> 11

<211> 519

<212> PRT

<213> Human adenovirus D37

<400> 11

Met Arg Arg Ala Val Val Ser Ser Ser Pro Pro Pro Ser Tyr Glu Ser

1 5 10 15

Val Met Ala Gln Ala Thr Leu Glu Val Pro Phe Val Pro Pro Arg Tyr

20 25 30

Met Ala Pro Thr Glu Gly Arg Asn Ser Ile Arg Tyr Ser Glu Leu Ala

35 40 45

Pro Leu Tyr Asp Thr Thr Arg Val Tyr Leu Val Asp Asn Lys Ser Ala

50 55 60

Asp Ile Ala Ser Leu Asn Tyr Gln Asn Asp His Ser Asn Phe Leu Thr

65 70 75 80

Thr Val Val Gln Asn Asn Asp Phe Thr Pro Ala Glu Ala Ser Thr Gln

85 90 95

Thr Ile Asn Phe Asp Glu Arg Ser Arg Trp Gly Gly Asp Leu Lys Thr

100 105 110

Ile Leu His Thr Asn Met Pro Asn Val Asn Glu Tyr Met Phe Thr Ser

115 120 125

Lys Phe Lys Ala Arg Val Met Val Ala Arg Lys Lys Ala Glu Gly Ala

130 135 140

Asp Ala Asn Asp Arg Ser Lys Asp Ile Leu Glu Tyr Gln Trp Phe Glu

145 150 155 160

Phe Thr Leu Pro Glu Gly Asn Phe Ser Glu Thr Met Thr Ile Asp Leu

165 170 175

Met Asn Asn Ala Ile Leu Glu Asn Tyr Leu Gln Val Gly Arg Gln Asn

180 185 190

Gly Val Leu Glu Ser Asp Ile Gly Val Lys Phe Asp Ser Arg Asn Phe

195 200 205

Lys Leu Gly Trp Asp Pro Val Thr Lys Leu Val Met Pro Gly Val Tyr

210 215 220

Thr Tyr Glu Ala Phe His Pro Asp Val Val Leu Leu Pro Gly Cys Gly

225 230 235 240

Val Asp Phe Thr Glu Ser Arg Leu Ser Asn Leu Leu Gly Ile Arg Lys

245 250 255

Lys Gln Pro Phe Gln Glu Gly Phe Arg Ile Met Tyr Glu Asp Leu Val

260 265 270

Gly Gly Asn Ile Pro Ala Leu Leu Asn Val Lys Glu Tyr Leu Lys Asp

275 280 285

Lys Glu Glu Ala Gly Lys Ala Asp Ala Asn Thr Ile Lys Ala Gln Asn

290 295 300

Asp Ala Val Pro Arg Gly Asp Asn Tyr Ala Ser Ala Ala Glu Ala Lys

305 310 315 320

Ala Ala Gly Lys Glu Ile Glu Leu Lys Ala Ile Leu Lys Asp Asp Ser

325 330 335

Asp Arg Ser Tyr Asn Val Ile Glu Gly Thr Thr Asp Thr Leu Tyr Arg

340 345 350

Ser Trp Tyr Leu Ser Tyr Thr Tyr Gly Asp Pro Glu Lys Gly Val Gln

355 360 365

Ser Trp Thr Leu Leu Thr Thr Pro Asp Val Thr Cys Gly Ala Glu Gln

370 375 380

Val Tyr Trp Ser Leu Pro Asp Leu Met Gln Asp Pro Val Thr Phe Arg

385 390 395 400

Ser Thr Gln Gln Val Ser Asn Tyr Pro Val Val Gly Ala Glu Leu Met

405 410 415

Pro Phe Arg Ala Lys Ser Phe Tyr Asn Asp Leu Ala Val Tyr Ser Gln

420 425 430

Leu Ile Arg Ser Tyr Thr Ser Leu Thr His Val Phe Asn Arg Phe Pro

435 440 445

Asp Asn Gln Ile Leu Cys Arg Pro Pro Ala Pro Thr Ile Thr Thr Val

450 455 460

Ser Glu Asn Val Pro Ala Leu Thr Asp His Gly Thr Leu Pro Leu Arg

465 470 475 480

Ser Ser Ile Arg Gly Val Gln Arg Val Thr Val Thr Asp Ala Arg Arg

485 490 495

Arg Thr Cys Pro Tyr Val Tyr Lys Ala Leu Gly Ile Val Ala Pro Arg

500 505 510

Val Leu Ser Ser Arg Thr Phe

515

<210> 12

<211> 508

<212> PRT

<213> Human adenovirus F serotype 41

<400> 12

Met Arg Arg Ala Val Gly Val Pro Pro Val Met Ala Tyr Ala Glu Gly

1 5 10 15

Pro Pro Pro Ser Tyr Glu Ser Val Met Gly Ser Ala Asp Ser Pro Ala

20 25 30

Thr Leu Glu Ala Leu Tyr Val Pro Pro Arg Tyr Leu Gly Pro Thr Glu

35 40 45

Gly Arg Asn Ser Ile Arg Tyr Ser Glu Leu Ala Pro Leu Tyr Asp Thr

50 55 60

Thr Arg Val Tyr Leu Val Asp Asn Lys Ser Ala Asp Ile Ala Ser Leu

65 70 75 80

Asn Tyr Gln Asn Asp His Ser Asn Phe Gln Thr Thr Val Val Gln Asn

85 90 95

Asn Asp Phe Thr Pro Ala Glu Ala Gly Thr Gln Thr Ile Asn Phe Asp

100 105 110

Glu Arg Ser Arg Trp Gly Ala Asp Leu Lys Thr Ile Leu Arg Thr Asn

115 120 125

Met Pro Asn Ile Asn Glu Phe Met Ser Thr Asn Lys Phe Lys Ala Arg

130 135 140

Leu Met Val Glu Lys Lys Asn Lys Glu Thr Gly Leu Pro Arg Tyr Glu

145 150 155 160

Trp Phe Glu Phe Thr Leu Pro Glu Gly Asn Tyr Ser Glu Thr Met Thr

165 170 175

Ile Asp Leu Met Asn Asn Ala Ile Val Asp Asn Tyr Leu Glu Val Gly

180 185 190

Arg Gln Asn Gly Val Leu Glu Ser Asp Ile Gly Val Lys Phe Asp Thr

195 200 205

Arg Asn Phe Arg Leu Gly Trp Asp Pro Val Thr Lys Leu Val Met Pro

210 215 220

Gly Val Tyr Thr Asn Glu Ala Phe His Pro Asp Ile Val Leu Leu Pro

225 230 235 240

Gly Cys Gly Val Asp Phe Thr Gln Ser Arg Leu Ser Asn Leu Leu Gly

245 250 255

Ile Arg Lys Arg Leu Pro Phe Gln Glu Gly Phe Gln Ile Met Tyr Glu

260 265 270

Asp Leu Glu Gly Gly Asn Ile Pro Ala Leu Leu Asp Val Thr Lys Tyr

275 280 285

Glu Ala Ser Ile Gln Lys Ala Lys Glu Glu Gly Lys Glu Ile Gly Asp

290 295 300

Asp Thr Phe Ala Thr Arg Pro Gln Asp Leu Val Ile Glu Pro Val Ala

305 310 315 320

Lys Asp Ser Lys Asn Arg Ser Tyr Asn Leu Leu Pro Asn Asp Gln Asn

325 330 335

Asn Thr Ala Tyr Arg Ser Trp Phe Leu Ala Tyr Asn Tyr Gly Asp Pro

340 345 350

Asn Lys Gly Val Gln Ser Trp Thr Leu Leu Thr Thr Ala Asp Val Thr

355 360 365

Cys Gly Ser Gln Gln Val Tyr Trp Ser Leu Pro Asp Met Met Gln Asp

370 375 380

Pro Val Thr Phe Arg Pro Ser Thr Gln Val Ser Asn Tyr Pro Val Val

385 390 395 400

Gly Val Glu Leu Leu Pro Val His Ala Lys Ser Phe Tyr Asn Glu Gln

405 410 415

Ala Val Tyr Ser Gln Leu Ile Arg Gln Ser Thr Ala Leu Thr His Val

420 425 430

Phe Asn Arg Phe Pro Glu Asn Gln Ile Leu Val Arg Pro Pro Ala Pro

435 440 445

Thr Ile Thr Thr Val Ser Glu Asn Val Pro Ala Leu Thr Asp His Gly

450 455 460

Thr Leu Pro Leu Arg Ser Ser Ile Ser Gly Val Gln Arg Val Thr Ile

465 470 475 480

Thr Asp Ala Arg Arg Arg Thr Cys Pro Tyr Val His Lys Ala Leu Gly

485 490 495

Ile Val Ala Pro Lys Val Leu Ser Ser Arg Thr Phe

500 505

<210> 13

<211> 575

<212> PRT

<213> Gorilla adenovirus B7

<400> 13

Met Met Arg Arg Ala Val Leu Gly Gly Ala Val Val Tyr Pro Glu Gly

1 5 10 15

Pro Pro Pro Ser Tyr Glu Ser Val Met Gln Gln Gln Ala Ala Ala Val

20 25 30

Met Gln Pro Ser Leu Glu Ala Pro Phe Val Pro Pro Arg Tyr Leu Ala

35 40 45

Pro Thr Glu Gly Arg Asn Ser Ile Arg Tyr Ser Glu Leu Ala Pro Gln

50 55 60

Tyr Asp Thr Thr Arg Leu Tyr Leu Val Asp Asn Lys Ser Ala Asp Ile

65 70 75 80

Ala Ser Leu Asn Tyr Gln Asn Asp His Ser Asn Phe Leu Thr Thr Val

85 90 95

Val Gln Asn Asn Asp Phe Thr Pro Thr Glu Ala Ser Thr Gln Thr Ile

100 105 110

Asn Phe Asp Glu Arg Ser Arg Trp Gly Gly Gln Leu Lys Thr Ile Met

115 120 125

His Thr Asn Met Pro Asn Val Asn Glu Tyr Met Phe Ser Asn Lys Phe

130 135 140

Lys Ala Arg Val Met Val Ser Arg Glu Ala Ser Lys Ile Asp Ser Glu

145 150 155 160

Lys Asn Asp Arg Ser Lys Asp Thr Leu Lys Tyr Glu Trp Phe Glu Phe

165 170 175

Thr Leu Pro Glu Gly Asn Phe Ser Ala Thr Met Thr Ile Asp Leu Met

180 185 190

Asn Asn Ala Ile Ile Asp Asn Tyr Leu Ala Val Gly Arg Gln Asn Gly

195 200 205

Val Leu Gln Ser Asp Ile Gly Val Lys Phe Asp Thr Arg Asn Phe Arg

210 215 220

Leu Gly Trp Asp Pro Val Thr Lys Leu Val Met Pro Gly Val Tyr Thr

225 230 235 240

Tyr Glu Ala Phe His Pro Asp Ile Val Leu Leu Pro Asp Cys Gly Val

245 250 255

Asp Phe Thr Glu Ser Arg Leu Ser Asn Leu Leu Gly Ile Arg Lys Arg

260 265 270

His Pro Phe Gln Glu Gly Phe Lys Ile Met Tyr Glu Asp Leu Glu Gly

275 280 285

Gly Asn Ile Pro Ala Leu Leu Asp Val Ala Glu Tyr Glu Lys Ser Lys

290 295 300

Lys Glu Ile Ala Ser Ser Thr Thr Thr Thr Ala Val Thr Thr Val Ala

305 310 315 320

Arg Asn Val Ala Asp Thr Ser Val Glu Ala Val Ala Val Ala Val Val

325 330 335

Asp Thr Ile Lys Ala Glu Asn Asp Ser Ala Val Arg Gly Asp Asn Phe

340 345 350

Gln Ser Lys Asn Asp Met Lys Ala Ser Glu Glu Val Thr Val Val Pro

355 360 365

Val Ser Pro Pro Thr Val Thr Glu Thr Glu Thr Lys Glu Pro Thr Ile

370 375 380

Lys Pro Leu Glu Lys Asp Thr Lys Asp Arg Ser Tyr Asn Val Ile Ser

385 390 395 400

Gly Thr Asn Asp Thr Ala Tyr Arg Ser Trp Tyr Leu Ala Tyr Asn Tyr

405 410 415

Gly Asp Pro Glu Lys Gly Val Arg Ser Trp Thr Leu Leu Thr Thr Ser

420 425 430

Asp Val Thr Cys Gly Ala Glu Gln Val Tyr Trp Ser Leu Pro Asp Met

435 440 445

Met Gln Asp Pro Val Thr Phe Arg Ser Thr Arg Gln Val Ser Asn Tyr

450 455 460

Pro Val Val Gly Ala Glu Leu Met Pro Val Phe Ser Lys Ser Phe Tyr

465 470 475 480

Asn Glu Gln Ala Val Tyr Ser Gln Gln Leu Arg Gln Thr Thr Ser Leu

485 490 495

Thr His Ile Phe Asp Arg Phe Pro Glu Asn Gln Ile Leu Ile Arg Pro

500 505 510

Pro Ala Pro Thr Ile Thr Thr Val Ser Glu Asn Val Pro Ala Leu Thr

515 520 525

Asp His Gly Thr Leu Pro Leu Arg Ser Ser Ile Arg Gly Val Gln Arg

530 535 540

Val Thr Val Thr Asp Ala Arg Arg Arg Thr Cys Pro Tyr Val Tyr Lys

545 550 555 560

Ala Leu Gly Ile Val Ala Pro Arg Val Leu Ser Ser Arg Thr Phe

565 570 575

<210> 14

<211> 532

<212> PRT

<213> Chimpanzee adenovirus Y25

<400> 14

Met Met Arg Arg Ala Tyr Pro Glu Gly Pro Pro Pro Ser Tyr Glu Ser

1 5 10 15

Val Met Gln Gln Ala Met Ala Ala Ala Ala Ala Met Gln Pro Pro Leu

20 25 30

Glu Ala Pro Tyr Val Pro Pro Arg Tyr Leu Ala Pro Thr Glu Gly Arg

35 40 45

Asn Ser Ile Arg Tyr Ser Glu Leu Ala Pro Leu Tyr Asp Thr Thr Arg

50 55 60

Leu Tyr Leu Val Asp Asn Lys Ser Ala Asp Ile Ala Ser Leu Asn Tyr

65 70 75 80

Gln Asn Asp His Ser Asn Phe Leu Thr Thr Val Val Gln Asn Asn Asp

85 90 95

Phe Thr Pro Thr Glu Ala Ser Thr Gln Thr Ile Asn Phe Asp Glu Arg

100 105 110

Ser Arg Trp Gly Gly Gln Leu Lys Thr Ile Met His Thr Asn Met Pro

115 120 125

Asn Val Asn Glu Phe Met Tyr Ser Asn Lys Phe Lys Ala Arg Val Met

130 135 140

Val Ser Arg Lys Thr Pro Asn Gly Val Thr Val Thr Asp Gly Ser Gln

145 150 155 160

Asp Ile Leu Glu Tyr Glu Trp Val Glu Phe Glu Leu Pro Glu Gly Asn

165 170 175

Phe Ser Val Thr Met Thr Ile Asp Leu Met Asn Asn Ala Ile Ile Asp

180 185 190

Asn Tyr Leu Ala Val Gly Arg Gln Asn Gly Val Leu Glu Ser Asp Ile

195 200 205

Gly Val Lys Phe Asp Thr Arg Asn Phe Arg Leu Gly Trp Asp Pro Val

210 215 220

Thr Glu Leu Val Met Pro Gly Val Tyr Thr Asn Glu Ala Phe His Pro

225 230 235 240

Asp Ile Val Leu Leu Pro Gly Cys Gly Val Asp Phe Thr Glu Ser Arg

245 250 255

Leu Ser Asn Leu Leu Gly Ile Arg Lys Arg Gln Pro Phe Gln Glu Gly

260 265 270

Phe Gln Ile Met Tyr Glu Asp Leu Glu Gly Gly Asn Ile Pro Ala Leu

275 280 285

Leu Asp Val Asp Ala Tyr Glu Lys Ser Lys Glu Glu Ser Ala Ala Ala

290 295 300

Ala Thr Ala Ala Val Ala Thr Ala Ser Thr Glu Val Arg Gly Asp Asn

305 310 315 320

Phe Ala Ser Pro Ala Ala Val Ala Ala Ala Glu Ala Ala Glu Thr Glu

325 330 335

Ser Lys Ile Val Ile Gln Pro Val Glu Lys Asp Ser Lys Asp Arg Ser

340 345 350

Tyr Asn Val Leu Pro Asp Lys Ile Asn Thr Ala Tyr Arg Ser Trp Tyr

355 360 365

Leu Ala Tyr Asn Tyr Gly Asp Pro Glu Lys Gly Val Arg Ser Trp Thr

370 375 380

Leu Leu Thr Thr Ser Asp Val Thr Cys Gly Val Glu Gln Val Tyr Trp

385 390 395 400

Ser Leu Pro Asp Met Met Gln Asp Pro Val Thr Phe Arg Ser Thr Arg

405 410 415

Gln Val Ser Asn Tyr Pro Val Val Gly Ala Glu Leu Leu Pro Val Tyr

420 425 430

Ser Lys Ser Phe Phe Asn Glu Gln Ala Val Tyr Ser Gln Gln Leu Arg

435 440 445

Ala Phe Thr Ser Leu Thr His Val Phe Asn Arg Phe Pro Glu Asn Gln

450 455 460

Ile Leu Val Arg Pro Pro Ala Pro Thr Ile Thr Thr Val Ser Glu Asn

465 470 475 480

Val Pro Ala Leu Thr Asp His Gly Thr Leu Pro Leu Arg Ser Ser Ile

485 490 495

Arg Gly Val Gln Arg Val Thr Val Thr Asp Ala Arg Arg Arg Thr Cys

500 505 510

Pro Tyr Val Tyr Lys Ala Leu Gly Ile Val Ala Pro Arg Val Leu Ser

515 520 525

Ser Arg Thr Phe

530

<210> 15

<211> 508

<212> PRT

<213> Monkey adenovirus 18

<400> 15

Met Arg Arg Ala Val Gly Val Pro Pro Val Met Ala Tyr Ala Glu Gly

1 5 10 15

Pro Pro Pro Ser Tyr Glu Thr Val Met Gly Ala Ala Asp Ser Pro Ala

20 25 30

Thr Leu Glu Ala Leu Tyr Val Pro Pro Arg Tyr Leu Gly Pro Thr Glu

35 40 45

Gly Arg Asn Ser Ile Arg Tyr Ser Glu Leu Ala Pro Leu Tyr Asp Thr

50 55 60

Thr Arg Val Tyr Leu Val Asp Asn Lys Ser Ala Asp Ile Ala Ser Leu

65 70 75 80

Asn Tyr Gln Asn Asp His Ser Asn Phe Leu Thr Thr Val Val Gln Asn

85 90 95

Asn Asp Phe Thr Pro Val Glu Ala Gly Thr Gln Thr Ile Asn Phe Asp

100 105 110

Glu Arg Ser Arg Trp Gly Gly Asp Leu Lys Thr Ile Leu Arg Thr Asn

115 120 125

Met Pro Asn Ile Asn Glu Phe Met Ser Thr Asn Lys Phe Arg Ala Arg

130 135 140

Leu Met Val Glu Lys Val Asn Lys Glu Thr Asn Ala Pro Arg Tyr Glu

145 150 155 160

Trp Phe Glu Phe Thr Leu Pro Glu Gly Asn Tyr Ser Glu Thr Met Thr

165 170 175

Ile Asp Leu Met Asn Asn Ala Ile Val Asp Asn Tyr Leu Glu Val Gly

180 185 190

Arg Gln Asn Gly Val Leu Glu Ser Asp Ile Gly Val Lys Phe Asp Thr

195 200 205

Arg Asn Phe Arg Leu Gly Trp Asp Pro Val Thr Lys Leu Val Met Pro

210 215 220

Gly Val Tyr Thr Asn Glu Ala Phe His Pro Asp Ile Val Leu Leu Pro

225 230 235 240

Gly Cys Gly Val Asp Phe Thr Gln Ser Arg Leu Ser Asn Leu Leu Gly

245 250 255

Ile Arg Lys Arg Met Pro Phe Gln Ala Gly Phe Gln Ile Met Tyr Glu

260 265 270

Asp Leu Glu Gly Gly Asn Ile Pro Ala Leu Leu Asp Val Ala Lys Tyr

275 280 285

Glu Ala Ser Ile Gln Lys Ala Arg Glu Gln Gly Gln Glu Ile Arg Gly

290 295 300

Asp Asn Phe Thr Val Ile Pro Arg Asp Val Glu Ile Val Pro Val Glu

305 310 315 320

Lys Asp Ser Lys Asp Arg Ser Tyr Asn Leu Leu Pro Gly Asp Gln Thr

325 330 335

Asn Thr Ala Tyr Arg Ser Trp Phe Leu Ala Tyr Asn Tyr Gly Asp Pro

340 345 350

Glu Lys Gly Val Arg Ser Trp Thr Leu Leu Thr Thr Thr Asp Val Thr

355 360 365

Cys Gly Ser Gln Gln Val Tyr Trp Ser Leu Pro Asp Met Met Gln Asp

370 375 380

Pro Val Thr Phe Arg Pro Ser Ser Gln Val Ser Asn Tyr Pro Val Val

385 390 395 400

Gly Val Glu Leu Leu Pro Val His Ala Lys Ser Phe Tyr Asn Glu Gln

405 410 415

Ala Val Tyr Ser Gln Leu Ile Arg Gln Ser Thr Ala Leu Thr His Val

420 425 430

Phe Asn Arg Phe Pro Glu Asn Gln Ile Leu Val Arg Pro Pro Ala Pro

435 440 445

Thr Ile Thr Thr Val Ser Glu Asn Val Pro Ala Leu Thr Asp His Gly

450 455 460

Thr Leu Pro Leu Arg Ser Ser Ile Ser Gly Val Gln Arg Val Thr Ile

465 470 475 480

Thr Asp Ala Arg Arg Arg Thr Cys Pro Tyr Val His Lys Ala Leu Gly

485 490 495

Ile Val Ala Pro Lys Val Leu Ser Ser Arg Thr Phe

500 505

<210> 16

<211> 512

<212> PRT

<213> Monkey adenovirus 20

<400> 16

Met Arg Arg Ala Val Ala Ile Pro Ser Ala Ala Val Ala Leu Gly Pro

1 5 10 15

Pro Pro Ser Tyr Glu Ser Val Met Ala Ser Ala Asn Leu Gln Ala Pro

20 25 30

Leu Glu Asn Pro Tyr Val Pro Pro Arg Tyr Leu Glu Pro Thr Gly Gly

35 40 45

Arg Asn Ser Ile Arg Tyr Ser Glu Leu Thr Pro Leu Tyr Asp Thr Thr

50 55 60

Arg Leu Tyr Leu Val Asp Asn Lys Ser Ala Asp Ile Ala Thr Leu Asn

65 70 75 80

Tyr Gln Asn Asp His Ser Asn Phe Leu Thr Ser Val Val Gln Asn Ser

85 90 95

Asp Tyr Thr Pro Ala Glu Ala Ser Thr Gln Thr Ile Asn Leu Asp Asp

100 105 110

Arg Ser Arg Trp Gly Gly Asp Leu Lys Thr Ile Leu His Thr Asn Met

115 120 125

Pro Asn Val Asn Glu Phe Met Phe Thr Asn Ser Phe Arg Ala Lys Leu

130 135 140

Met Val Ala His Glu Thr Asn Lys Asp Pro Val Tyr Lys Trp Val Glu

145 150 155 160

Leu Thr Leu Pro Glu Gly Asn Phe Ser Glu Thr Met Thr Ile Asp Leu

165 170 175

Met Asn Asn Ala Ile Val Asp His Tyr Leu Ala Val Gly Arg Gln Asn

180 185 190

Gly Val Lys Glu Ser Glu Ile Gly Val Lys Phe Asp Thr Arg Asn Phe

195 200 205

Arg Leu Gly Trp Asp Pro Gln Thr Glu Leu Val Met Pro Gly Val Tyr

210 215 220

Thr Asn Glu Ala Phe His Pro Asp Val Val Leu Leu Pro Gly Cys Gly

225 230 235 240

Val Asp Phe Thr Tyr Ser Arg Leu Ser Asn Leu Leu Gly Ile Arg Lys

245 250 255

Arg Met Pro Phe Gln Glu Gly Phe Gln Ile Met Tyr Glu Asp Leu Val

260 265 270

Gly Gly Asn Ile Pro Ala Leu Leu Asp Val Pro Ala Tyr Glu Ala Ser

275 280 285

Ile Thr Thr Val Ala Ala Lys Glu Val Arg Gly Asp Asn Phe Glu Ala

290 295 300

Ala Ala Ala Ala Ala Ala Thr Gly Ala Gln Pro Gln Ala Ala Pro Val

305 310 315 320

Val Arg Pro Val Thr Gln Asp Ser Lys Gly Arg Ser Tyr Asn Ile Ile

325 330 335

Thr Gly Thr Asn Asn Thr Ala Tyr Arg Ser Trp Tyr Leu Ala Tyr Asn

340 345 350

Tyr Gly Asp Pro Glu Lys Gly Val Arg Ser Trp Thr Leu Leu Thr Thr

355 360 365

Pro Asp Val Thr Cys Gly Ser Glu Gln Val Tyr Trp Ser Met Pro Asp

370 375 380

Met Tyr Val Asp Pro Val Thr Phe Arg Ser Ser Gln Gln Val Ser Ser

385 390 395 400

Tyr Pro Val Val Gly Ala Glu Leu Leu Pro Ile His Ser Lys Ser Phe

405 410 415

Tyr Asn Glu Gln Ala Val Tyr Ser Gln Leu Ile Arg Gln Gln Thr Ala

420 425 430

Leu Thr His Val Phe Asn Arg Phe Pro Glu Asn Gln Ile Leu Val Arg

435 440 445

Pro Pro Ala Pro Thr Ile Thr Thr Val Ser Glu Asn Val Pro Ala Leu

450 455 460

Thr Asp His Gly Thr Leu Pro Leu Gln Asn Ser Ile Arg Gly Val Gln

465 470 475 480

Arg Val Thr Ile Thr Asp Ala Arg Arg Arg Thr Cys Pro Tyr Val Tyr

485 490 495

Lys Ala Leu Gly Ile Val Ala Pro Arg Val Leu Ser Ser Arg Thr Phe

500 505 510

<210> 17

<211> 511

<212> PRT

<213> Monkey adenovirus 49

<400> 17

Met Arg Arg Ala Val Pro Ala Ala Ala Ile Pro Ala Thr Val Ala Tyr

1 5 10 15

Ala Asp Pro Pro Pro Ser Tyr Glu Ser Val Met Ala Gly Val Pro Ala

20 25 30

Thr Leu Glu Ala Pro Tyr Val Pro Pro Arg Tyr Leu Gly Pro Thr Glu

35 40 45

Gly Arg Asn Ser Ile Arg Tyr Ser Glu Leu Ala Pro Leu Tyr Asp Thr

50 55 60

Thr Arg Val Tyr Leu Val Asp Asn Lys Ser Ala Asp Ile Ala Ser Leu

65 70 75 80

Asn Tyr Gln Asn Asp His Ser Asn Phe Leu Thr Thr Val Val Gln Asn

85 90 95

Asn Asp Phe Thr Pro Val Glu Ala Gly Thr Gln Thr Ile Asn Phe Asp

100 105 110

Glu Arg Ser Arg Trp Gly Gly Gln Leu Lys Thr Ile Leu His Thr Asn

115 120 125

Met Pro Asn Val Asn Glu Phe Met Phe Thr Asn Ser Phe Arg Ala Lys

130 135 140

Val Met Val Ser Arg Lys Gln Asn Glu Glu Gly Gln Thr Glu Leu Glu

145 150 155 160

Tyr Glu Trp Val Glu Phe Val Leu Pro Glu Gly Asn Tyr Ser Glu Thr

165 170 175

Met Thr Leu Asp Leu Met Asn Asn Ala Ile Val Asp His Tyr Leu Leu

180 185 190

Val Gly Arg Gln Asn Gly Val Leu Glu Ser Asp Ile Gly Val Lys Phe

195 200 205

Asp Thr Arg Asn Phe Arg Leu Gly Trp Asp Pro Val Thr Lys Leu Val

210 215 220

Met Pro Gly Val Tyr Thr Asn Glu Ala Phe His Pro Asp Val Val Leu

225 230 235 240

Leu Pro Gly Cys Gly Val Asp Phe Thr Gln Ser Arg Leu Ser Asn Leu

245 250 255

Leu Gly Ile Arg Lys Arg Gln Pro Phe Gln Glu Gly Phe Arg Ile Met

260 265 270

Tyr Glu Asp Leu Glu Gly Gly Asn Ile Pro Ala Leu Leu Asn Val Lys

275 280 285

Ala Tyr Glu Asp Ser Ile Ala Ala Ala Met Arg Lys His Asn Leu Pro

290 295 300

Leu Arg Gly Asp Val Phe Ala Val Gln Pro Gln Glu Ile Val Ile Gln

305 310 315 320

Pro Val Glu Lys Asp Gly Lys Glu Arg Ser Tyr Asn Leu Leu Pro Asp

325 330 335

Asp Lys Asn Asn Thr Ala Tyr Arg Ser Trp Tyr Leu Ala Tyr Asn Tyr

340 345 350

Gly Asp Pro Leu Lys Gly Val Arg Ser Trp Thr Leu Leu Thr Thr Pro

355 360 365

Asp Val Thr Cys Gly Ser Glu Gln Val Tyr Trp Ser Leu Pro Asp Leu

370 375 380

Met Gln Asp Pro Val Thr Phe Arg Pro Ser Ser Gln Val Ser Asn Tyr

385 390 395 400

Pro Val Val Gly Ala Glu Leu Leu Pro Leu Gln Ala Lys Ser Phe Tyr

405 410 415

Asn Glu Gln Ala Val Tyr Ser Gln Leu Ile Arg Gln Ser Thr Ala Leu

420 425 430

Thr His Val Phe Asn Arg Phe Pro Glu Asn Gln Ile Leu Val Arg Pro

435 440 445

Pro Ala Ala Thr Ile Thr Thr Val Ser Glu Asn Val Pro Ala Leu Thr

450 455 460

Asp His Gly Thr Leu Pro Leu Arg Ser Ser Ile Ser Gly Val Gln Arg

465 470 475 480

Val Thr Ile Thr Asp Ala Arg Arg Arg Thr Cys Pro Tyr Val Tyr Lys

485 490 495

Ala Leu Gly Ile Val Ala Pro Arg Val Leu Ser Ser Arg Thr Phe

500 505 510

<210> 18

<211> 505

<212> PRT

<213> Rhesus macaque adenovirus 51

<400> 18

Met Arg Arg Ala Val Arg Val Thr Pro Ala Ala Tyr Glu Gly Pro Pro

1 5 10 15

Pro Ser Tyr Glu Ser Val Met Gly Ser Ala Asn Val Pro Ala Thr Leu

20 25 30

Glu Ala Pro Tyr Val Pro Pro Arg Tyr Leu Gly Pro Thr Glu Gly Arg

35 40 45

Asn Ser Ile Arg Tyr Ser Glu Leu Ala Pro Leu Tyr Asp Thr Thr Lys

50 55 60

Val Tyr Leu Val Asp Asn Lys Ser Ala Asp Ile Ala Ser Leu Asn Tyr

65 70 75 80

Gln Asn Asp His Ser Asn Phe Leu Thr Thr Val Val Gln Asn Asn Asp

85 90 95

Phe Thr Pro Thr Glu Ala Gly Thr Gln Thr Ile Asn Phe Asp Glu Arg

100 105 110

Ser Arg Trp Gly Gly Gln Leu Lys Thr Ile Leu His Thr Asn Met Pro

115 120 125

Asn Ile Asn Glu Phe Met Ser Thr Asn Lys Phe Arg Ala Lys Leu Met

130 135 140

Val Glu Lys Ser Asn Ala Glu Thr Arg Gln Pro Arg Tyr Glu Trp Phe

145 150 155 160

Glu Phe Thr Ile Pro Glu Gly Asn Tyr Ser Glu Thr Met Thr Ile Asp

165 170 175

Leu Met Asn Asn Ala Ile Val Asp Asn Tyr Leu Gln Val Gly Arg Gln

180 185 190

Asn Gly Val Leu Glu Ser Asp Ile Gly Val Lys Phe Asp Thr Arg Asn

195 200 205

Phe Arg Leu Gly Trp Asp Pro Val Thr Lys Leu Val Met Pro Gly Val

210 215 220

Tyr Thr Asn Glu Ala Phe His Pro Asp Ile Val Leu Leu Pro Gly Cys

225 230 235 240

Gly Val Asp Phe Thr Gln Ser Arg Leu Ser Asn Leu Leu Gly Ile Arg

245 250 255

Lys Arg Arg Pro Phe Gln Glu Gly Phe Gln Ile Met Tyr Glu Asp Leu

260 265 270

Glu Gly Gly Asn Ile Pro Ala Leu Leu Asp Val Ser Lys Tyr Glu Ala

275 280 285

Ser Ile Gln Arg Ala Lys Ala Glu Gly Arg Glu Ile Arg Gly Asp Thr

290 295 300

Phe Ala Val Ala Pro Gln Asp Leu Glu Ile Val Pro Leu Thr Lys Asp

305 310 315 320

Ser Lys Asp Arg Ser Tyr Asn Ile Ile Asn Asn Thr Thr Asp Thr Leu

325 330 335

Tyr Arg Ser Trp Phe Leu Ala Tyr Asn Tyr Gly Asp Pro Glu Lys Gly

340 345 350

Val Arg Ser Trp Thr Ile Leu Thr Thr Thr Asp Val Thr Cys Gly Ser

355 360 365

Gln Gln Val Tyr Trp Ser Leu Pro Asp Met Met Gln Asp Pro Val Thr

370 375 380

Phe Arg Pro Ser Thr Gln Val Ser Asn Phe Pro Val Val Gly Thr Glu

385 390 395 400

Leu Leu Pro Val His Ala Lys Ser Phe Tyr Asn Glu Gln Ala Val Tyr

405 410 415

Ser Gln Leu Ile Arg Gln Ser Thr Ala Leu Thr His Val Phe Asn Arg

420 425 430

Phe Pro Glu Asn Gln Ile Leu Val Arg Pro Pro Ala Pro Thr Ile Thr

435 440 445

Thr Val Ser Glu Asn Val Pro Ala Leu Thr Asp His Gly Thr Leu Pro

450 455 460

Leu Arg Ser Ser Ile Ser Gly Val Gln Arg Val Thr Ile Thr Asp Ala

465 470 475 480

Arg Arg Arg Thr Cys Pro Tyr Val Tyr Lys Ala Leu Gly Val Val Ala

485 490 495

Pro Lys Val Leu Ser Ser Arg Thr Phe

500 505

<210> 19

<211> 503

<212> PRT

<213> Rhesus macaque adenovirus 52

<400> 19

Met Arg Arg Ala Val Arg Val Thr Pro Ala Ala Tyr Glu Gly Pro Pro

1 5 10 15

Pro Ser Tyr Glu Ser Val Met Gly Ser Ala Asn Val Pro Ala Thr Leu

20 25 30

Glu Ala Pro Tyr Val Pro Pro Arg Tyr Leu Gly Pro Thr Glu Gly Arg

35 40 45

Asn Ser Ile Arg Tyr Ser Glu Leu Ala Pro Leu Tyr Asp Thr Thr Lys

50 55 60

Val Tyr Leu Val Asp Asn Lys Ser Ala Asp Ile Ala Ser Leu Asn Tyr

65 70 75 80

Gln Asn Asp His Ser Asn Phe Leu Thr Thr Val Val Gln Asn Asn Asp

85 90 95

Phe Thr Pro Thr Glu Ala Gly Thr Gln Thr Ile Asn Phe Asp Glu Arg

100 105 110

Ser Arg Trp Gly Gly Gln Leu Lys Thr Ile Leu His Thr Asn Met Pro

115 120 125

Asn Ile Asn Glu Phe Met Ser Thr Asn Lys Phe Arg Ala Arg Leu Met

130 135 140

Val Lys Lys Val Glu Asn Gln Pro Pro Glu Tyr Glu Trp Phe Glu Phe

145 150 155 160

Thr Ile Pro Glu Gly Asn Tyr Ser Glu Thr Met Thr Ile Asp Leu Met

165 170 175

Asn Asn Ala Ile Val Asp Asn Tyr Leu Gln Val Gly Arg Gln Asn Gly

180 185 190

Val Leu Glu Ser Asp Ile Gly Val Lys Phe Asp Thr Arg Asn Phe Arg

195 200 205

Leu Gly Trp Asp Pro Val Thr Lys Leu Val Met Pro Gly Val Tyr Thr

210 215 220

Asn Glu Ala Phe His Pro Asp Ile Val Leu Leu Pro Gly Cys Gly Val

225 230 235 240

Asp Phe Thr Gln Ser Arg Leu Ser Asn Leu Leu Gly Ile Arg Lys Arg

245 250 255

Arg Pro Phe Gln Glu Gly Phe Gln Ile Met Tyr Glu Asp Leu Glu Gly

260 265 270

Gly Asn Ile Pro Ala Leu Leu Asp Val Thr Lys Tyr Glu Gln Ser Val

275 280 285

Gln Arg Ala Lys Ala Glu Gly Arg Glu Ile Arg Gly Asp Thr Phe Ala

290 295 300

Val Ser Pro Gln Asp Leu Val Ile Glu Pro Leu Glu His Asp Ser Lys

305 310 315 320

Asn Arg Ser Tyr Asn Leu Leu Pro Asn Lys Thr Asp Thr Ala Tyr Arg

325 330 335

Ser Trp Phe Leu Ala Tyr Asn Tyr Gly Asp Pro Glu Lys Gly Val Arg

340 345 350

Ser Trp Thr Ile Leu Thr Thr Thr Asp Val Thr Cys Gly Ser Gln Gln

355 360 365

Val Tyr Trp Ser Leu Pro Asp Met Met Gln Asp Pro Val Thr Phe Arg

370 375 380

Pro Ser Thr Gln Val Ser Asn Phe Pro Val Val Gly Thr Glu Leu Leu

385 390 395 400

Pro Val His Ala Lys Ser Phe Tyr Asn Glu Gln Ala Val Tyr Ser Gln

405 410 415

Leu Ile Arg Gln Ser Thr Ala Leu Thr His Val Phe Asn Arg Phe Pro

420 425 430

Glu Asn Gln Ile Leu Val Arg Pro Pro Ala Pro Thr Ile Thr Thr Val

435 440 445

Ser Glu Asn Val Pro Ala Leu Thr Asp His Gly Thr Leu Pro Leu Arg

450 455 460

Ser Ser Ile Ser Gly Val Gln Arg Val Thr Ile Thr Asp Ala Arg Arg

465 470 475 480

Arg Thr Cys Pro Tyr Val Tyr Lys Ala Leu Gly Val Val Ala Pro Lys

485 490 495

Val Leu Ser Ser Arg Thr Phe

500

<210> 20

<211> 504

<212> PRT

<213> Rhesus macaque adenovirus 53

<400> 20

Met Arg Arg Ala Val Arg Val Thr Pro Ala Val Tyr Ala Glu Gly Pro

1 5 10 15

Pro Pro Ser Tyr Glu Ser Val Met Gly Ser Ala Asn Val Pro Ala Thr

20 25 30

Leu Glu Ala Pro Tyr Val Pro Pro Arg Tyr Leu Gly Pro Thr Glu Gly

35 40 45

Arg Asn Ser Ile Arg Tyr Ser Glu Leu Ala Pro Leu Tyr Asp Thr Thr

50 55 60

Lys Val Tyr Leu Val Asp Asn Lys Ser Ala Asp Ile Ala Ser Leu Asn

65 70 75 80

Tyr Gln Asn Asp His Ser Asn Phe Leu Thr Thr Val Val Gln Asn Asn

85 90 95

Asp Phe Thr Pro Thr Glu Ala Gly Thr Gln Thr Ile Asn Phe Asp Glu

100 105 110

Arg Ser Arg Trp Gly Gly Gln Leu Lys Thr Ile Leu His Thr Asn Met

115 120 125

Pro Asn Ile Asn Glu Phe Met Ser Thr Asn Lys Phe Arg Ala Arg Leu

130 135 140

Met Val Glu Lys Thr Ser Gly Gln Pro Pro Lys Tyr Glu Trp Phe Glu

145 150 155 160

Phe Thr Ile Pro Glu Gly Asn Tyr Ser Glu Thr Met Thr Ile Asp Leu

165 170 175

Met Asn Asn Ala Ile Val Asp Asn Tyr Leu Gln Val Gly Arg Gln Asn

180 185 190

Gly Val Leu Glu Ser Asp Ile Gly Val Lys Phe Asp Thr Arg Asn Phe

195 200 205

Arg Leu Gly Trp Asp Pro Val Thr Lys Leu Val Met Pro Gly Val Tyr

210 215 220

Thr Asn Glu Ala Phe His Pro Asp Ile Val Leu Leu Pro Gly Cys Gly

225 230 235 240

Val Asp Phe Thr Gln Ser Arg Leu Ser Asn Leu Leu Gly Ile Arg Lys

245 250 255

Arg Arg Pro Phe Gln Glu Gly Phe Gln Ile Met Tyr Glu Asp Leu Glu

260 265 270

Gly Gly Asn Ile Pro Gly Leu Leu Asp Val Pro Ala Tyr Glu Gln Ser

275 280 285

Leu Gln Gln Ala Gln Glu Glu Gly Arg Val Thr Arg Gly Asp Thr Phe

290 295 300

Ala Thr Ala Pro Asn Glu Val Val Ile Lys Pro Leu Leu Lys Asp Ser

305 310 315 320

Lys Asp Arg Ser Tyr Asn Ile Ile Thr Asp Thr Thr Asp Thr Leu Tyr

325 330 335

Arg Ser Trp Phe Leu Ala Tyr Asn Tyr Gly Asp Pro Glu Asn Gly Val

340 345 350

Arg Ser Trp Thr Ile Leu Thr Thr Thr Asp Val Thr Cys Gly Ser Gln

355 360 365

Gln Val Tyr Trp Ser Leu Pro Asp Met Met Gln Asp Pro Val Thr Phe

370 375 380

Arg Pro Ser Thr Gln Val Ser Asn Phe Pro Val Val Gly Thr Glu Leu

385 390 395 400

Leu Pro Val His Ala Lys Ser Phe Tyr Asn Glu Gln Ala Val Tyr Ser

405 410 415

Gln Leu Ile Arg Gln Ser Thr Ala Leu Thr His Val Phe Asn Arg Phe

420 425 430

Pro Glu Asn Gln Ile Leu Val Arg Pro Pro Ala Pro Thr Ile Thr Thr

435 440 445

Val Ser Glu Asn Val Pro Ala Leu Thr Asp His Gly Thr Leu Pro Leu

450 455 460

Arg Ser Ser Ile Ser Gly Val Gln Arg Val Thr Ile Thr Asp Ala Arg

465 470 475 480

Arg Arg Thr Cys Pro Tyr Val Tyr Lys Ala Leu Gly Val Val Ala Pro

485 490 495

Lys Val Leu Ser Ser Arg Thr Phe

500

<210> 21

<211> 144

<212> PRT

<213> Artificial sequence

<220>

<223> Consensus sequence of amino acid region A

<220>

<221> MISC_FEATURE

<222> (1)..(47)

<223> There is no amino acid or any amino acid at this position

<220>

<221> MISC_FEATURE

<222> (50)..(50)

<223> E or G

<220>

<221> MISC_FEATURE

<222> (59)..(59)

<223> E or S

<220>

<221> MISC_FEATURE

<222> (60)..(60)

<223> L or V

<220>

<221> MISC_FEATURE

<222> (61)..(61)

<223> A or S

<220>

<221> MISC_FEATURE

<222> (63)..(63)

<223> L or Q

<220>

<221> MISC_FEATURE

<222> (64)..(64)

<223> Y or E

<220>

<221> MISC_FEATURE

<222> (68)..(68)

<223> R or K

<220>

<221> MISC_FEATURE

<222> (69)..(69)

<223> V or L

<220>

<221> MISC_FEATURE

<222> (92)..(92)

<223> L or Q

<220>

<221> MISC_FEATURE

<222> (96)..(96)

<223> V or I

<220>i

<221> MISC_FEATURE

<222> (101)..(101)

<223> F or Y

<220>

<221> MISC_FEATURE

<222> (102)..(102)

<223> T or S

<220>

<221> MISC_FEATURE

<222> (104)..(104)

<223> A or T or I or G

<220>

<221> MISC_FEATURE

<222> (107)..(107)

<223> S or G

<220>

<221> MISC_FEATURE

<222> (113)..(113)

<223> F or L

<220>

<221> MISC_FEATURE

<222> (115)..(115)

<223> E or D

<220>

<221> MISC_FEATURE

<222> (121)..(121)

<223> A or G

<220>

<221> MISC_FEATURE

<222> (122)..(122)

<223> D or Q

<220>

<221> MISC_FEATURE

<222> (127)..(127)

<223> L or M

<220>

<221> MISC_FEATURE

<222> (128)..(128)

<223>H or R

<220>

<221> MISC_FEATURE

<222> (130)..(130)

<223> no amino acid or, if present, N

<220>

<221> MISC_FEATURE

<222> (131)..(131)

<223> no amino acid or, if present, M

<220>

<221> MISC_FEATURE

<222> (132)..(132)

<223> no amino acid or, if present, P

<220>

<221> MISC_FEATURE

<222> (133)..(133)

<223> no amino acid or, if present, N

<220>

<221> MISC_FEATURE

<222> (134)..(134)

<223> no amino acid or, if present, V, or I

<220>

<221> MISC_FEATURE

<222> (135)..(135)

<223> no amino acid or, if present, N

<220>

<221> MISC_FEATURE

<222> (136)..(136)

<223> no amino acid or, if present, E, or D

<220>

<221> MISC_FEATURE

<222> (137)..(137)

<223> no amino acid or, if present, Y, or F

<220>

<221> MISC_FEATURE

<222> (138)..(138)

<223> no amino acid or, if present, M

<220>

<221> MISC_FEATURE

<222> (139)..(139)

<223> no amino acid or, if present, F, or S, or Y

<220>

<221> MISC_FEATURE

<222> (140)..(140)

<223> no amino acid or, if present, T, or S

<220>

<221> MISC_FEATURE

<222> (141)..(141)

<223> no amino acid or, if present, S, or N

<220>

<221> MISC_FEATURE

<222> (142)..(142)

<223> no amino acid or, if present, K

<220>

<221> MISC_FEATURE

<222> (143)..(143)

<223> no amino acid or, if present, F

<220>

<221> MISC_FEATURE

<222> (144)..(144)

<223> no amino acid or, if present, K

<400> 21

Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa

1 5 10 15

Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa

20 25 30

Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Pro

35 40 45

Thr Xaa Gly Arg Asn Ser Ile Arg Tyr Ser Xaa Xaa Xaa Pro Xaa Xaa

50 55 60

Asp Thr Thr Xaa Xaa Tyr Leu Val Asp Asn Lys Ser Ala Asp Ile Ala

65 70 75 80

Ser Leu Asn Tyr Gln Asn Asp His Ser Asn Phe Xaa Thr Thr Val Xaa

85 90 95

Gln Asn Asn Asp Xaa Xaa Pro Xaa Glu Ala Xaa Thr Gln Thr Ile Asn

100 105 110

Xaa Asp Xaa Arg Ser Arg Trp Gly Xaa Xaa Leu Lys Thr Ile Xaa Xaa

115 120 125

Thr Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa

130 135 140

<210> 22

<211> 46

<212> PRT

<213> Artificial sequence

<220>

<223> Consensus sequence of amino acid region B

<220>

<221> MISC_FEATURE

<222> (1)..(1)

<223> no amino acid or, if present, L, or S

<220>

<221> MISC_FEATURE

<222> (2)..(2)

<223> no amino acid or, if present, T, or P, or C

<220>

<221> MISC_FEATURE

<222> (3)..(3)

<223> no amino acid or, if present, T, or P

<220>

<221> MISC_FEATURE

<222> (4)..(4)

<223> no amino acid or, if present, P or S or A or R

<220>

<221> MISC_FEATURE

<222> (5)..(5)

<223> no amino acid or, if present, N, or D

<220>

<221> MISC_FEATURE

<222> (6)..(6)

<223> no amino acid or, if present, G, or V

<220>

<221> MISC_FEATURE

<222> (7)..(7)

<223> no amino acid or, if present, H, or T

<220>

<221> MISC_FEATURE

<222> (8)..(8)

<223> no amino acid or, if present, C

<220>

<221> MISC_FEATURE

<222> (9)..(9)

<223> no amino acid or, if present, G

<220>

<221> MISC_FEATURE

<222> (10)..(10)

<223> no amino acid or, if present, A, or V, or S

<220>

<221> MISC_FEATURE

<222> (11)..(11)

<223> no amino acid or, if present, E, or Q

<220>

<221> MISC_FEATURE

<222> (20)..(20)

<223> L or M

<220>

<221> MISC_FEATURE

<222> (22)..(22)

<223> Q or K

<220>

<221> MISC_FEATURE

<222> (31)..(31)

<223> Q, or R, or S

<220>

<221> MISC_FEATURE

<222> (33)..(33)

<223> V or I

<220>

<221> MISC_FEATURE

<222> (34)..(34)

<223> S or N

<220>

<221> MISC_FEATURE

<222> (36)..(36)

<223> Y or F

<220>

<221> MISC_FEATURE

<222> (41)..(41)

<223> A or V

<220>

<221> MISC_FEATURE

<222> (44)..(44)

<223> no amino acid or, if present, M, or L

<220>

<221> MISC_FEATURE

<222> (45)..(45)

<223> no amino acid or, if present, P

<220>

<221> MISC_FEATURE

<222> (46)..(46)

<223> no amino acid or, if present, V, or F

<400> 22

Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Gln Val Tyr Trp Ser

1 5 10 15

Leu Pro Asp Xaa Met Xaa Asp Pro Val Thr Phe Arg Ser Thr Xaa Gln

20 25 30

Xaa Xaa Asn Xaa Pro Val Val Gly Xaa Glu Leu Xaa Xaa Xaa

35 40 45

<210> 23

<211> 53

<212> PRT

<213> Artificial sequence

<220>

<223> Consensus sequence of amino acid region C

<220>

<221> MISC_FEATURE

<222> (1)..(1)

<223> no amino acid or, if present, N

<220>

<221> MISC_FEATURE

<222> (2)..(2)

<223> no amino acid or, if present, V

<220>

<221> MISC_FEATURE

<222> (3)..(3)

<223> no amino acid or, if present, P

<220>

<221> MISC_FEATURE

<222> (18)..(18)

<223> R, or S, or G

<220>

<221> MISC_FEATURE

<222> (25)..(25)

<223> V or I

<220>

<221> MISC_FEATURE

<222> (44)..(44)

<223> A or S

<220>

<221> MISC_FEATURE

<222> (46)..(46)

<223> R or K

<400> 23

Xaa Xaa Xaa Ala Leu Thr Asp His Gly Thr Leu Pro Leu Arg Ser Ser

1 5 10 15

Ile Xaa Gly Val Gln Arg Val Thr Xaa Thr Asp Ala Arg Arg Arg Thr

20 25 30

Cys Pro Tyr Val Tyr Lys Ala Leu Gly Ile Val Xaa Pro Xaa Val Leu

35 40 45

Ser Ser Arg Thr Phe

50

<210> 24

<211> 4

<212> PRT

<213> Artificial sequence

<220>

<223> Linking segment

<400> 24

Gly Gly Gly Ser

1

<210> 25

<211> 6

<212> PRT

<213> Artificial sequence

<220>

<223> Linking segment

<400> 25

Gly Gly Ser Gly Gly Ser

15

<210> 26

<211> 778

<212> DNA

<213> Artificial sequence

<220>

<223> Design of DNAsegVAJB-CHIK

<400> 26

ggatccatga ggagacgagc cgtgctaggc ggagcggtgg tgtatccgga gggtcctcct 60

ccttcttacg agagcgtgat gcagcaacag gcggcgatga tacagccccc actggaggct 120

cccttcgtac ccccacggta cctggcgcct acggaaggga gaaacagcat tcgttactcg 180

gagctgtcgc ccctgtacga taccaccaag ttgtatctgg tggacaacaa gtcggcggac 240

atcgcctccc tgaactatca gaacgaccac agcaacttcc tgaccacggt ggtgcagaac 300

aatgacttta cccccacgga ggctagcacc cagaccatca actttgacga gcggtcgcga 360

tggggcggtc agctgaagac catcatgcac accaacatgc ccggaggtga aaacctgtat 420

tttcagagca ccaaagataa ctttaacgtg tataaagcga cccgcccgta tctggcgcat 480

ggaggtgcag agcaggtcta ctggtcgctc cctgacatga tgcaagaccc agtcaccttc 540

cgctccacaa gacaagtcaa caactaccca gtggtgggtg cagagcttat gcccggtgga 600

agcggaggta gcgttcctgc tctcacagat cacgggaccc tgccgttacg cagcagtatc 660

cggggagtcc agcgcgtgac cgttactgac gccagacgcc gcacctgtcc ctacgtttac 720

aaggccctgg gcatagtcgc gccgcgcgtt ctttcaagcc gcactttctg ataagctt 778

<210> 27

<211> 3699

<212> DNA

<213> Artificial sequence

<220>

<223> Construction pACEBac_VAJB-CHIK

<400> 27

accggttgac ttgggtcaac tgtcagacca agtttactca tatatacttt agattgattt 60

aaaacttcat ttttaattta aaaggatcta ggtgaagatc ctttttgata atctcatgac 120

caaaatccct taacgtgagt tttcgttcca ctgagcgtca gaccccgtag aaaagatcaa 180

aggatcttct tgagatcctt tttttctgcg cgtaatctgc tgcttgcaaa caaaaaaacc 240

accgctacca gcggtggttt gtttgccgga tcaagagcta ccaactcttt ttccgaaggt 300

aactggcttc agcagagcgc agataccaaa tactgttctt ctagtgtagc cgtagttagg 360

ccaccacttc aagaactctg tagcaccgcc tacatacctc gctctgctaa tcctgttacc 420

agtggctgct gccagtggcg ataagtcgtg tcttaccggg ttggactcaa gacgatagtt 480

accggataag gcgcagcggt cgggctgaac ggggggttcg tgcacacagc ccagcttgga 540

gcgaacgacc tacaccgaac tgagatacct acagcgtgag ctatgagaaa gcgccacgct 600

tcccgaaggg agaaaggcgg acaggtatcc ggtaagcggc agggtcggaa caggagagcg 660

cacgagggag cttccagggg gaaacgcctg gtatctttat agtcctgtcg ggtttcgcca 720

cctctgactt gagcgtcgat ttttgtgatg ctcgtcaggg gggcggagcc tatggaaaaa 780

cgccagcaac gcggcctttt tacggttcct ggccttttgc tggccttttg ctcacatgtt 840

ctttcctgcg ttatcccctg attgacttgg gtcgctcttc ctgtggatgc gcagatgccc 900

tgcgtaagcg ggtgtgggcg gacaataaag tcttaaactg aacaaaatag atctaaacta 960

tgacaataaa gtcttaaact agacagaata gttgtaaact gaaatcagtc cagttatgct 1020

gtgaaaaagc atactggact tttgttatgg ctaaagcaaa ctcttcattt tctgaagtgc 1080

aaattgcccg tcgtattaaa gaggggcgtg gccaagggca tgtaaagact atattcgcgg 1140

cgttgtgaca atttaccgaa caactccgcg gccgggaagc cgatctcggc ttgaacgaat 1200

tgttaggtgg cggtacttgg gtcgatatca aagtgcatca cttcttcccg tatgcccaac 1260

tttgtataga gagccactgc gggatcgtca ccgtaatctg cttgcacgta gatcacataa 1320

gcaccaagcg cgttggcctc atgcttgagg agattgatga gcgcggtggc aatgccctgc 1380

ctccggtgct cgccggagac tgcgagatca tagatataga tctcactacg cggctgctca 1440

aacttgggca gaacgtaagc cgcgagagcg ccaacaaccg cttcttggtc gaaggcagca 1500

agcgcgatga atgtcttact acggagcaag ttcccgaggt aatcggagtc cggctgatgt 1560

tgggagtagg tggctacgtc tccgaactca cgaccgaaaa gatcaagagc agcccgcatg 1620

gatttgactt ggtcagggcc gagcctacat gtgcgaatga tgcccatact tgagccacct 1680

aactttgttt tagggcgact gccctgctgc gtaacatcgt tgctgctgcg taacatcgtt 1740

gctgctccat aacatcaaac atcgacccac ggcgtaacgc gcttgctgct tggatgcccg 1800

aggcatagac tgtacaaaaa aacagtcata acaagccatg aaaaccgcca ctgcgccgtt 1860

accaccgctg cgttcggtca aggttctgga ccagttgcgt gagcgcatac gctacttgca 1920

ttacagttta cgaaccgaac aggcttatgt caactgggtt cgtgccttca tccgtttcca 1980

cggtgtgcgt cacccggcaa ccttgggcag cagcgaagtc gccataactt cgtatagcat 2040

acattatacg aagttatctg taactataac ggtcctaagg tagcgagttt aaacactagt 2100

atcgattcgc gacctactcc ggaatattaa tagatcatgg agataattaa aatgataacc 2160

atctcgcaaa taaataagta ttttactgtt ttcgtaacag ttttgtaata aaaaaaccta 2220

taaatattcc ggattattca taccgtccca ccatcgggcg cggatccatg aggagacgag 2280

ccgtgctagg cggagcggtg gtgtatccgg agggtcctcc tccttcttac gagagcgtga 2340

tgcagcaaca ggcggcgatg atacagcccc cactggaggc tcccttcgta cccccacggt 2400

acctggcgcc tacggaaggg agaaacagca ttcgttactc ggagctgtcg cccctgtacg 2460

ataccaccaa gttgtatctg gtggacaaca agtcggcgga catcgcctcc ctgaactatc 2520

agaacgacca cagcaacttc ctgaccacgg tggtgcagaa caatgacttt acccccacgg 2580

aggctagcac cgaccacatc aactttgacg agcggtcgcg atggggcggt cagctgaaga 2640

ccatcatgca caccaacatg cccggaggtg aaaacctgta ttttcagagc accaaagata 2700

actttaacgt gtataaagcg acccgcccgt atctggcgca tggaggtgca gagcaggtct 2760

actggtcgct ccctgacatg atgcaagacc cagtcacctt ccgctccaca agacaagtca 2820

acaactaccc agtggtgggt gcagagctta tgcccggtgg aagcggaggt agcgttcctg 2880

ctctcacaga tcacgggacc ctgccgttac gcagcagtat ccggggagtc cagcgcgtga 2940

ccgttactga cgccagacgc cgcacctgtc cctacgttta caaggccctg ggcatagtcg 3000

cgccgcgcgt tctttcaagc cgcactttct gataagcttc catcaacttt gacgagcggt 3060

cgcgatgggg cggtcagctg aagaccatca tgcacaccaa catgcccaac gtgaacgagt 3120

acatgttcag caacaagttc aaggcgaggg agcttgtcga gaagtactag aggatcataa 3180

tcagccatac cacatttgta gaggttttac ttgctttaaa aaacctccca cacctccccc 3240

tgaacctgaa acataaaatg aatgcaattg ttgttgttaa cttgtttatt gcagcttata 3300

atggttacaa ataaagcaat agcatcacaa atttcacaaa taaagcattt ttttcactgc 3360

attctagttg tggtttgtcc aaactcatca atgtatctta tcatgtctgg atctgatcac 3420

tgcttgagcc tagaagatcc ggctgctaac aaagcccgaa aggaagctga gttggctgct 3480

gccaccgctg agcaataact atcataaccc ctagggtata cccatctaat tggaaccaga 3540

taagtgaaat ctagttccaa actattttgt catttttaat tttcgtatta gcttacgacg 3600

ctacacccag ttcccatcta ttttgtcact cttccctaaa taatccttaa aaactccatt 3660

tccacccctc ccagttccca actattttgt ccgcccaca 3699

<210> 28

<211> 254

<212> PRT

<213> Artificial sequence

<220>

<223> VAJB-CHIK protein

<400> 28

Met Arg Arg Arg Ala Val Leu Gly Gly Ala Val Val Tyr Pro Glu Gly

1 5 10 15

Pro Pro Pro Ser Tyr Glu Ser Val Met Gln Gln Gln Ala Ala Met Ile

20 25 30

Gln Pro Pro Leu Glu Ala Pro Phe Val Pro Pro Arg Tyr Leu Ala Pro

35 40 45

Thr Glu Gly Arg Asn Ser Ile Arg Tyr Ser Glu Leu Ser Pro Leu Tyr

50 55 60

Asp Thr Thr Lys Leu Tyr Leu Val Asp Asn Lys Ser Ala Asp Ile Ala

65 70 75 80

Ser Leu Asn Tyr Gln Asn Asp His Ser Asn Phe Leu Thr Thr Val Val

85 90 95

Gln Asn Asn Asp Phe Thr Pro Thr Glu Ala Ser Thr Gln Thr Ile Asn

100 105 110

Phe Asp Glu Arg Ser Arg Trp Gly Gly Gln Leu Lys Thr Ile Met His

115 120 125

Thr Asn Met Pro Gly Gly Glu Asn Leu Tyr Phe Gln Ser Thr Lys Asp

130 135 140

Asn Phe Asn Val Tyr Lys Ala Thr Arg Pro Tyr Leu Ala His Gly Gly

145 150 155 160

Ala Glu Gln Val Tyr Trp Ser Leu Pro Asp Met Met Gln Asp Pro Val

165 170 175

Thr Phe Arg Ser Thr Arg Gln Val Asn Asn Tyr Pro Val Val Gly Ala

180 185 190

Glu Leu Met Pro Gly Gly Ser Gly Gly Ser Val Pro Ala Leu Thr Asp

195 200 205

His Gly Thr Leu Pro Leu Arg Ser Ser Ile Arg Gly Val Gln Arg Val

210 215 220

Thr Val Thr Asp Ala Arg Arg Arg Thr Cys Pro Tyr Val Tyr Lys Ala

225 230 235 240

Leu Gly Ile Val Ala Pro Arg Val Leu Ser Ser Arg Thr Phe

245 250

<210> 29

<211> 18

<212> PRT

<213> Chikungunya virus

<400> 29

Ser Thr Lys Asp Asn Phe Asn Val Tyr Lys Ala Thr Arg Pro Tyr Leu

1 5 10 15

Ala His

<---

Claims (185)

1. A polypeptide for presenting an oligopeptide, polypeptide, protein and/or protein complex having the structure of formula (I) Where A is the N-terminal amino acid region of the adenovirus penton base protein, B is the amino acid region of the adenovirus penton base protein, C represents the C-terminal amino acid region of the adenovirus penton base, where B represents the amino acid region located between A and C in the sequence of the indicated adenovirus penton base, where A, B and C form a jelly roll fold domain of the specified adenovirus penton base protein, L ₁ and L ₂ are independently selected from the group consisting of an oligopeptide, a polypeptide, a protein and a protein complex, wherein said oligopeptide, polypeptide, protein and protein complex, respectively, are either substantially non-adenoviral or, if adenoviral, AL ₁ -BL ₂ -C forms a penton base chimera, wherein A, B and C form a base roll domain an adenovirus penton of one adenovirus subtype, and L ₁ and L ₂ form the crown domain of the adenovirus penton base of an adenovirus subtype different from the adenovirus subtype of the roll fold domain. 2. The polypeptide according to claim 1, where amino acid region A contains beta sheets 1, 2 and 3 of the domain with a roll-type fold of the specified adenovirus. 3. The polypeptide according to claim 1 or 2, where amino acid region B contains beta sheets 4 and 5 of the domain with a roll-type fold of the specified adenovirus. 4. Polypeptide according to any one of paragraphs. 1-3, where amino acid region C contains beta sheets 6, 7 and 8 of the adenovirus roll-type folding domain. 5. Polypeptide according to any one of paragraphs. 1-4, wherein amino acid regions A, B and C have an amino acid sequence, each independently selected from the group consisting of the penton bases of human adenovirus serotype 2, human adenovirus serotype 3, human adenovirus serotype 4, human adenovirus serotype 5, human adenovirus 7 serotype, human adenovirus 11 serotype, human adenovirus 12 serotype, human adenovirus 17 serotype, human adenovirus serotype 25, human adenovirus 35 serotype, human adenovirus 37 serotype, human adenovirus 41 serotype, gorilla adenovirus, chimpanzee adenovirus, simian adenovirus serotype 18, simian adenovirus s 20 serotype, simian adenovirus 49 serotype, rhesus macaque adenovirus 51 serotype, rhesus macaque adenovirus 52 serotype and rhesus macaque adenovirus 53 serotype. 6. The polypeptide of claim 5, wherein amino acid region A has the following consensus sequence (SEQ ID NO: 21): (U) _1-47 PTX ₁ GRNSIRY SX ₂ X ₃ x ₄ PX ₅ X ₆ DTT X ₇ X ₃ YLVDNKSA DIASLNYQND HSNFX ₅ TTVX ₉ Q NNDX ₁₀ X ₁₁ PX ₁₂ EAX ₁₃ TQTINX ₁₄ DX ₁₅ RS RWGX ₁₆ X ₁₇ LKTIX ₁₈ X ₁₉ TZ ₁ Z ₂ Z ₃ Z ₄ Z ₅ Z ₆ Z ₇ Z ₈ Z ₉ Z ₁₀ Z ₁₁ Z ₁₂ Z ₁₃ Z ₁₄ Z _15, where: amino acid region A ends at the C-terminus before Z ₁ at residue T or at amino acids Z ₁ to Z _15, U represents any amino acid or is absent, X ₁ represents E or G, X ₂ represents E or S, X ₃ represents L or V, X ₄ represents A or S, X ₅ represents L or Q, X ₆ represents Y or E, X ₇ represents R or K, X ₈ represents V or L, X ₉ represents V or I, X ₁₀ represents F or Y, X ₁₁ represents T or S, X ₁₂ represents A, or T, or I, or G, X ₁₃ represents S or G, X ₁₄ represents F or L, X ₁₅ represents E or D, X ₁₆ represents A or G, X ₁₇ represents D or Q, X ₁₈ represents L or M, X ₁₉ represents H or R, Z ₁ , if present, represents N, Z ₂ , if present, represents M, Z ₃ , if present, represents P, Z ₄ , if present, is N, Z ₅ , if present, is V or I, Z ₆ , if present, is N, Z ₇ , if present, is E or D, Z ₈ , if present, is Y or F, Z ₉ , if present, represents M, Z ₁₀ , if present, is F or S or Y, Z ₁₁ , if present, is T or S, Z ₁₂ , if present, is S or N, Z ₁₃ , if present, represents K, Z ₁₄ , if present, is F, Z ₁₆ , if present, represents K. 7. The polypeptide according to claim 6, where amino acid region A is selected from the group consisting of the following sequences: from an amino acid selected from positions 1 to 48 to an amino acid selected from positions 129 to 144, UniProtAcc. No. Q2Y0H9, from an amino acid selected from positions 1 to 48 to an amino acid selected from positions 129 to 144, UniProtAcc. No. P03276, from an amino acid selected from positions 1 to 44 to an amino acid selected from positions 125 to 140, UniProtAcc. No. Q2KSF3, from an amino acid selected from positions 1 to 48 to an amino acid selected from positions 129 to 144, UniProtAcc. No. P12538, from an amino acid selected from positions 1 to 48 to an amino acid selected from positions 129 to 144, UniProtAcc. No. Q9JFT6, from an amino acid selected from positions 1 to 48 to an amino acid selected from positions 129 to 144, UniProtAcc. No. D2DM93, from an amino acid selected from positions 1 to 38 to an amino acid selected from positions 119 to 134, UniProtAcc. No. P36716, from an amino acid selected from positions 1 to 35 to an amino acid selected from positions 116 to 131, UniProtAcc. No. F1DT65, from an amino acid selected from positions 1 to 43 to an amino acid selected from positions 124 to 139, UniProtAcc. No. M0QUK0, from an amino acid selected from positions 1 to 49 to an amino acid selected from positions 130 to 145, UniProtAcc. No. Q7T941, from an amino acid selected from positions 1 to 35 to an amino acid selected from positions 116 to 131, UniProtAcc. No. Q912J1, from an amino acid selected from positions 1 to 46 to an amino acid selected from positions 127 to 142, UniProtAcc. No. F8WQN4, from an amino acid selected from positions 1 to 49 to an amino acid selected from positions 130 to 145, UniProtAcc. No. E5L3Q9, from an amino acid selected from positions 1 to 44 to an amino acid selected from positions 125 to 140, UniProtAcc. No. G9G849, from an amino acid selected from positions 1 to 46 to an amino acid selected from positions 127 to 142, UniProtAcc. No. H8PFZ9, from an amino acid selected from positions 1 to 45 to an amino acid selected from positions 126 to 141, UniProtAcc. No. F6KSU4, from an amino acid selected from positions 1 to 46 to an amino acid selected from positions 127 to 142, UniProtAcc. No. F2WTK5, from an amino acid selected from positions 1 to 43 to an amino acid selected from positions 124 to 139, UniProtAcc. No. A0A0A1EWW1, from an amino acid selected from positions 1 to 43 to an amino acid selected from positions 124 to 139, UniProtAcc. No. A0A0A1EWX7, and from an amino acid selected from positions 1 to 44 to an amino acid selected from positions 125 to 140, UniProtAcc. No. A0A0A1EWZ7. 8. Polypeptide according to any one of paragraphs. 5-7, wherein amino acid region B of the above general formula (I) has the following sequence (SEQ ID NO: 22): Z ₁₇ Z ₁₈ Z ₁₉ Z ₂₀ Z ₂₁ Z ₂₂ Z ₂₃ Z ₂₄ Z ₂₅ Z ₂₆ Z ₂₇ QVYWSLPDX ₂₀ MX ₂₁ DPVTFRST X ₂₂ QX ₂₃ X ₂₄ NX ₂₅ PVVGX ₂₆ ELZ ₂₈ Z ₂₉ Z ₃₀ , where: amino acid section B begins at the N-terminus of amino acids Z ₁₇ to Z ₂₇ or amino acid Q after Z ₂₇ , amino acid section B ends at the C-terminus before Z ₂₈ of amino acid L or amino acids Z ₂₈ to Z ₃₀ , Z ₁₇ , if present, is L or S, Z ₁₈ , if present, is T or P or C, Z ₁₉ , if present, is T or P, Z ₂₀ , if present, is P or S or A or R, Z ₂₁ , if present, is N or D, Z ₂₂ , if present, is G or V, Z ₂₃ , if present, is H or T, Z ₂₄ , if present, is C, Z ₂₅ , if present, represents G, Z ₂₆ , if present, is A or V or S, Z ₂₇ , if present, is E or Q, X ₂₀ represents L or M, X ₂₁ represents Q or K, X ₂₂ represents Q, or R, or S, X ₂₃ represents V or I, X ₂₄ represents S or N, X ₂₅ represents Y or F, X ₂₆ represents A or V, Z ₂₈ , if present, is M or L, Z ₂₉ , if present, represents P, Z ₃₀ , if present, is V or F. 9. The polypeptide according to claim 8, where the amino acid region B is selected from the group consisting of the following sequences: from an amino acid selected from positions 398 to 409 to an amino acid selected from positions 440 to 443, UniProtAcc. No. Q2Y0H9, from an amino acid selected from positions 425 to 436 to an amino acid selected from positions 467 to 470, UniProtAcc. No. P03276, from an amino acid selected from positions 379 to 390 to an amino acid selected from positions 421 to 444, UniProtAcc. No. Q2KSF3, from an amino acid selected from positions 425 to 436 to an amino acid selected from positions 467 to 470, UniProtAcc. No. P12538, from an amino acid selected from positions 398 to 409 to an amino acid selected from positions 440 to 443, UniProtAcc. No. Q9JFT6, from an amino acid selected from positions 415 to 426 to an amino acid selected from positions 457 to 460, UniProtAcc. No. D2DM93, from an amino acid selected from positions 351 to 362 to an amino acid selected from positions 393 to 397, UniProtAcc. No. P36716, from an amino acid selected from positions 370 to 381 to an amino acid selected from positions 413 to 416, UniProtAcc. No. F1DT65, from an amino acid selected from positions 388 to 399 to an amino acid selected from positions 440 to 443, UniProtAcc. No. M0QUK0, from an amino acid selected from positions 445 to 456 to an amino acid selected from positions 497 to 500, UniProtAcc. No. Q7T941, from an amino acid selected from positions 372 to 383 to an amino acid selected from positions 414 to 417, UniProtAcc. No. Q912J1, from an amino acid selected from positions 362 to 373 to an amino acid selected from positions 404 to 407, UniProtAcc. No. F8WQN4, from an amino acid selected from positions 416 to 427 to an amino acid selected from positions 458 to 461, UniProtAcc. No. E5L3Q9, from an amino acid selected from positions 372 to 383 to an amino acid selected from positions 420 to 423, UniProtAcc. No. G9G849, from an amino acid selected from positions 353 to 364 to an amino acid selected from positions 395 to 398, UniProtAcc. No. H8PFZ9, from an amino acid selected from positions 358 to 369 to an amino acid selected from positions 400 to 403, UniProtAcc. No. F6KSU4, from an amino acid selected from positions 356 to 367 to an amino acid selected from positions 398 to 401, UniProtAcc. No. F2WTK5, from an amino acid selected from positions 352 to 363 to an amino acid selected from positions 394 to 397, UniProtAcc. No. A0A0A1EWW1, from an amino acid selected from positions 350 to 361 to an amino acid selected from positions 392 to 395, UniProtAcc. No. A0A0A1EWX7, and from an amino acid selected from positions 351 to 362 to an amino acid selected from positions 393 to 396, UniProtAcc. No. A0A0A1EWZ7. 10. Polypeptide according to any one of paragraphs. 5-9, wherein amino acid region C of the above general formula (I) has the following sequence (SEQ ID NO: 23): Z ₃₁ Z ₃₂ Z ₃₃ ALTDHGT LPLRSSIX ₂₇ GV QRVTX ₂₈ TDARR RTCPYVYKA LGIVX ₃₀ PX ₃₁ VLS SRTF, where: amino acid region C begins at the N-terminus of amino acids Z ₃₁ to Z ₃₃ or amino acid A after Z ₃₃ , Z ₃₁ , if present, is N, Z ₃₂ , if present, represents V, Z ₃₃ , if present, is P, X ₂₇ represents R, or S, or G, X ₂₈ represents V or I, X ₂₉ represents Y or H, X ₃₀ represents A or S, X ₃₁ represents R or K. 11. The polypeptide according to claim 10, where amino acid region C is selected from the group consisting of the following sequences: from an amino acid selected from positions 492 to 495 to the C-terminal amino acid of UniProtAcc. No. Q2Y0H9, from an amino acid selected from positions 519 to 522 to the C-terminal amino acid of UniProtAcc. No. P03276, from an amino acid selected from positions 466 to 469 to the C-terminal amino acid of UniProtAcc. No. Q2KSF3, from an amino acid selected from positions 492 to 495 to the C-terminal amino acid of UniProtAcc. No. P12538, from an amino acid selected from positions 465 to 468 to the C-terminal amino acid of UniProtAcc. No. Q9JFT6, from an amino acid selected from positions 482 to 485 to the C-terminal amino acid of UniProtAcc. No. D2DM93, from an amino acid selected from positions 419 to 422 to the C-terminal amino acid of UniProtAcc. No. P36716, from an amino acid selected from positions 438 to 441 to the C-terminal amino acid of UniProtAcc. No. F1DT65, from an amino acid selected from positions 455 to 458 to the C-terminal amino acid of UniProtAcc. No. M0QUK0, from an amino acid selected from positions 522 to 525 to the C-terminal amino acid of UniProtAcc. No. Q7T941, from an amino acid selected from positions 439 to 442 to the C-terminal amino acid of UniProtAcc. No. Q912J1, from an amino acid selected from positions 429 to 432 to the C-terminal amino acid of UniProtAcc. No. F8WQN4, from an amino acid selected from positions 483 to 486 to the C-terminal amino acid of UniProtAcc. No. E5L3Q9, from an amino acid selected from positions 445 to 448 to the C-terminal amino acid of UniProtAcc. No. G9G849, from an amino acid selected from positions 420 to 423 to the C-terminal amino acid of UniProtAcc. No. H8PFZ9, from an amino acid selected from positions 425 to 428 to the C-terminal amino acid of UniProtAcc. No. F6KSU4, from an amino acid selected from positions 423 to 426 to the C-terminal amino acid of UniProtAcc. No. F2WTK5, from an amino acid selected from positions 419 to 422 to the C-terminal amino acid of UniProtAcc. No. A0A0A1EWW1, from an amino acid selected from positions 417 to 420 to the C-terminal amino acid of UniProtAcc. No. A0A0A1EWX7, and from an amino acid selected from positions 418 to 421 to the C-terminal amino acid of UniProtAcc. No. A0A0A1EWZ7. 12. Polypeptide according to any one of paragraphs. 1-11, where amino acid region A has the sequence of positions 1 to 132 UniProtAcc. No. Q2Y0H9, amino acid region B has the sequence of positions 407 to 442 UniProtAcc. No. Q2Y0H9, and amino acid region C has the sequence of positions 493 to 544 of UniProtAcc. No. Q2Y0H9. 13. Polypeptide according to any one of paragraphs. 1-12, where L ₁ and/or L ₂ is an oligopeptide having a sequence of from 4 to 40 amino acids selected from amino acids G and S. 14. The polypeptide of claim 13, wherein L ₁ and/or L ₂ are independently selected from the group consisting of GGGS (SEQ ID NO: 24) and GGSGGS (SEQ ID NO: 25). 15. Polypeptide according to any one of paragraphs. 1-12, where L ₁ is an adenoviral sequence containing the RGD loop of a penton base of an adenovirus having a serotype different from the serotype of the adenovirus(es) from which the specified amino acid regions A, B and C are derived, and/or L ₂ is an adenoviral sequence , containing a penton base variable loop of an adenovirus having a serotype different from the serotype of the adenovirus from which the indicated amino acid regions A, B and C are derived. 16. The polypeptide of claim 15, wherein L ₁ is a large fragment of the crown domain of a penton base of an adenovirus having a serotype different from the serotype of the adenovirus(es) from which said amino acid regions A, B and C are derived, and L ₂ is a small fragment of the crown domain of the penton base of an adenovirus having a serotype different from the serotype of the adenovirus(es) from which the indicated amino acid regions A, B and C are derived. 17. The polypeptide according to claim 16, where the large and small fragments come from the penton base protein of the same adenovirus. 18. The polypeptide according to claim 16, where the large and small fragments are derived from the penton base protein of various adenoviruses. 19. Polypeptide according to any one of paragraphs. 15-18, where one or more non-adenoviral sequences are inserted into the RGD loop and/or the variable loop. 20. Polypeptide according to any one of paragraphs. 1-19, where L ₁ and/or L ₂ contain an antigen. 21. The polypeptide according to claim 20, where the antigen is selected from the group consisting of an infectious agent antigen and a tumor antigen. 22. Polypeptide according to any one of paragraphs. 1-21, where L ₁ and/or L ₂ is/are attached to a nucleic acid, drug, label and/or binding partner of a biologically binding pair. 23. Nucleic acid encoding a polypeptide according to any one of paragraphs. 1-22. 24. Nucleic acid for obtaining a nucleic acid according to claim 23 by inserting nucleotide sequences encoding L ₁ and L ₂ of the general formula (I), containing a sequence having the following general formula (II) Where a is a nucleotide sequence encoding A of general formula (I), b is a nucleotide sequence encoding B of general formula (I), c is a nucleotide sequence encoding C of general formula (I), and l ₁ , l ₂ each represents a nucleotide sequence, is ₁ to is ₄ each independently represent a nucleotide sequence containing at least one insertion site. 25. The nucleic acid according to claim 24, where the values is ₁ to is ₄ are selected from the group consisting of restriction enzyme recognition sequences and homing endonuclease recognition sequences. 26. The nucleic acid according to claim 25, where is ₁ contains an EcoRI site, is ₂ contains a RsrII site, is ₃ contains a SacI site, and is ₄ contains an XbaI site. 27. Vector for producing a polypeptide according to any one of claims. 1-22, containing the nucleic acid according to claim 23. 28. The vector of claim 27, containing the nucleic acid of claim 23 in an expression cassette. 29. Recombinant host cell for producing a polypeptide according to any one of paragraphs. 1-22, containing the nucleic acid according to claim 23 or the vector according to claim 27 or 28. 30. Pentamer polypeptide complex according to any one of paragraphs. 1-12 and 15-22 for the presentation of an oligopeptide, polypeptide, protein and/or protein complex, wherein AL ₁ -BL ₂ -C forms a penton base chimera, and wherein A, B and C form a penton base roll domain of adenovirus one adenovirus subtype, and L ₁ and L ₂ form the crown domain of the penton base of an adenovirus subtype of an adenovirus different from the adenovirus subtype of the roll fold domain. 31. Virus-like particle (VLP) for the presentation of an oligopeptide, polypeptide, protein and/or protein complex, containing 12 pentameric complexes according to claim 30. 32. Polypeptide according to any one of paragraphs. 1-22, nucleic acid according to claim 23, vector according to claim 27 or 28, host cell according to claim 29 or HPV according to claim 31 for use as a medicine. 33. Pharmaceutical composition for the presentation of an oligopeptide, polypeptide, protein and/or protein complex, containing a polypeptide according to any one of paragraphs. 1-22, the nucleic acid of claim 23, the vector of claim 27 or 28, the host cell of claim 29, or the HPV of claim 31, together with at least one pharmaceutically acceptable carrier, excipient and/or diluent. 34. A method for producing a polypeptide according to any one of claims. 1-22, including the step of culturing a recombinant host cell according to claim 29, where the host cell contains the vector according to claim 28 under conditions that ensure expression of the specified polypeptide. 35. A method for producing HPV according to claim 31, including the step of incubating a polypeptide solution according to any one of claims. 1-22 under conditions that ensure the assembly of the polypeptide into HPV. 36. Polypeptide according to any one of paragraphs. 1-22, the nucleic acid of claim 23, the vector of claim 27 or 28, the host cell of claim 29, or the HPV of claim 31 for use in the treatment and/or prevention of an infectious disease, immune disease, tumor or cancer.