All late proteins expressed from the major late promoter are produced by alternative splicing and alternative polyadenylation of the same gene giving rise to non-overlapping ORFs. A leader sequence is present in the N-terminus of all these mRNAs and is recognized by the viral shutoff protein to provide expression although conventional translation via ribosome scanning from the cap has been shut off in the host cell.
Belongs to the adenoviridae core-capsid bridging protein family.
Belongs to the adenoviridae histone-like nucleoprotein family.
Belongs to the adenoviridae penton family.
Cleaved near the N-terminus by the viral protease during virion maturation to form the mature protein.
Expressed in the late phase of the viral replicative cycle.
Interacts with the core-capsid bridging protein; this interaction bridges the virus core to the capsid. Interacts with host NPM1; this interaction might play a role in placing the pre-histone-like nucleoprotein on the viral DNA or regulating viral gene expression. Interacts with host HMGB1; this interaction inhibits host immune response.
Interacts with the fiber protein (via N-terminal tail region). Interacts with the capsid vertex protein; this interaction binds the penton base to neighboring peripentonal hexons.
Lacks conserved residue(s) required for the propagation of feature annotation.
Major capsid protein that self-associates to form penton base pentamers, each in the shape of a pentagon, situated at the 12 vertices of the pseudo T=25 capsid. Involved in virus secondary attachment to host cell after initial attachment by the fiber protein, and in endocytosis of virions. As the virus enters the host cell, penton proteins are shed concomitant with virion acidification in the endosome.
Plays a role in the inhibition of host immune response within the nucleus. Interacts with cellular nucleosomes and immobilizes the host immune danger signal HMGB1 on chromatin. In turn, prevents HMGB1 release out of the cell and thus decreases inflammation. Plays also a role in the wrapping and condensation of the viral DNA. May also promote viral genome import into the nucleus.
Belongs to the adenoviridae hexon-linking protein family.
Cleaved by the viral protease during virion maturation. May cause the middle segment to be shed from the capsid.
Hexon-linking protein-C: Structural component of the virion that acts as a cement protein on the capsid interior and which glue the peripentonal hexons and group-of-nine hexons together.
Hexon-linking protein-N: Structural component of the virion that acts as a cement protein on the capsid interior and which glue the peripentonal hexons and group-of-nine hexons together.
Interacts with the peripentonal hexons as well as the hexons in the facets. Part of a complex composed of the core-capsid bridging protein, the endosome lysis protein VI and the hexon-linking protein VIII; these interactions bridge the virus core to the capsid.
Belongs to the adenoviridae fiber family.
Belongs to the adenoviridae E4 30 to 34 kDa protein family.
Belongs to the adenoviridae E1B 55 kDa protein family.
Plays a major role to prevent cellular inhibition of viral genome replication. Assembles an SCF-like E3 ubiquitin ligase complex based on the cellular proteins ELOB, ELOC, CUL5 and RBX1, in cooperation with viral E4orf6. This viral RING-type ligase ubiquitinates cellular substrates and targets them to proteasomal degradation: TP53/p53, LIG4, MRE11-RAD50-NBS1 (MRN) complex, ITGA3, DAXX and BLM. Degradation of host TP53/p53 activity is essential for preventing E1A-induced TP53 accumulation that would otherwise lead to cell apoptosis and growth arrest. E1B-55K also inactivates TP53 transcription-factor activity by binding its transactivation domain. E1B-55K also functions as a SUMO1 E3 ligase for TP53 which causes the latter to be sequestered in promyelocytic leukemia (PML) nuclear bodies thereby contributing to maximal inhibition of TP53 function.
Belongs to the adenoviridae E3_20 family.
Binds and retains class I heavy chains in the endoplasmic reticulum during the early period of virus infection, thereby impairing their transport to the cell surface. Also delays the expression of class I alleles that it cannot affect by direct retention. Binds transporters associated with antigen processing (TAP) and acts as a tapasin inhibitor, preventing class I/TAP association. In consequence, infected cells are masked for immune recognition by cytotoxic T-lymphocytes.
Belongs to the adenoviridae hexon-interlacing protein family.
Expressed in the intermediate phase of the viral replicative cycle.
Homotrimer. Interacts with hexon protein; this interaction tethers the hexons together. Self-interacts with adjacent proteins. Interacts with kinesin light chain KLC1; this interaction leads to capsid disruption at the nuclear pore complex during virus entry into host cell.
Structural component of the virion that acts as a cement protein on the capsid exterior and forms triskelion structures consisting of three molecules that stabilize three hexon trimers at the center of each icosahedral facet and fixes the peripentonal hexons. Dispensable for assembly. During virus entry, recruits the anterograde motor kinesin-1 to the capsid docked at the nuclear pore complex thereby subjecting the docked capsid to a pulling force. The resulting tension leads to capsid disruption, dispersion of capsid fragments toward cell periphery and eventually viral DNA entry into the host nucleus.
This protein is only encoded by mastadenoviruses, and may therefore play a role in mammals tropism.
Three N-terminal domains of hexon-interlacing protein form triskelions between hexon capsomers.
Belongs to the adenoviridae E1A protein family.
Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle.
Belongs to the adenoviridae shutoff protein family.
Belongs to the adenoviridae splicing factor family.
Methylated. Asymmetric dimethylation by host PRMT1 of the Arg/Gly-rich region may regulate shutoff protein binding to hexon and promote the capsid assembly in the nucleus.
Monomer. Interacts with hexon protein; this interaction allows chaperoning and trimerization of hexon proteins. Interacts (via N-terminus) with host initiation factor EIF4G (via C-terminus). Interacts (via RRM domain) with viral mRNAs that contain the tripartite leader; this interaction allows ribosome shunting and expression of viral late mRNAs.
Phosphorylated. Tyrosine phosphorylation enhances preferential binding to tripartite leader mRNAs and allows ribosome shunting.
Protein that inhibits host translation while promoting late viral translation by ribosome shunting. Blocks host cap-dependent translation by binding to eIF4G, displacing MKNK1 from cap initiation complexes and preventing EIF4E phosphorylation. Binds to the tripartite leader sequence of viral late mRNAs and recruits host eIF4G, PABPC1/poly-A binding protein and 40S ribosomes subunits on viral mRNAs, allowing ribosome shunting and efficient translation of late viral mRNAs even though conventional translation via ribosome scanning from the cap has been shut off in the host cell. During assembly, acts as a chaperone protein that helps hexon proteins assembly into trimers.
Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, pVIII, and pX) inside newly assembled particles giving rise to mature virions. Protease complexed to its cofactor slides along the viral DNA to specifically locate and cleave the viral precursors. Mature virions have a weakened organization compared to the unmature virions, thereby facilitating subsequent uncoating. Without maturation, the particle lacks infectivity and is unable to uncoat. Late in adenovirus infection, in the cytoplasm, may participate in the cytoskeleton destruction. Cleaves host cell cytoskeletal keratins K7 and K18.
Interacts with protease cofactor pVI-C; this interaction is necessary for protease activation.
Requires DNA and protease cofactor for maximal activation. Inside nascent virions, becomes partially activated by binding to the viral DNA, allowing it to cleave the cofactor that binds to the protease and fully activates it. Actin, like the viral protease cofactor, seems to act as a cofactor in the cleavage of cytokeratin 18 and of actin itself.
Belongs to the adenoviridae E2A DNA-binding protein family.
Homomultimerizes on viral ssDNA bound to pTP. Forms a initiation complex with viral polymerase, pTP and hosts NFIA and POU2F1/OCT1. Interacts with host SRCAP.
Plays a role in the elongation phase of viral strand displacement replication by unwinding the template in an ATP-independent fashion, employing its capacity to form multimers. Also enhances the rate of initiation. Released from template upon second strand synthesis. Assembles in complex with viral pTP, viral pol, host NFIA and host POU2F1/OCT1 on viral origin of replication. Covers the whole ssDNA genome during synthesis. The complementary strand synthesis induces its relese from DNA template. May inhibit cellular transcription mediated by the interaction between host SRCAP and CBP.
The C-terminal arm bridges DBP molecules together, thereby creating a chain.
Belongs to the adenoviridae hexon protein family.
Belongs to the adenoviridae protein VI family.
Endosome lysis protein: Structural component of the virion that provides increased stability to the particle shell through its interaction with the core-capsid bridging protein and the hexon-linking protein VIII. Fibers shedding during virus entry into host cell allows the endosome lysis protein to be exposed as a membrane-lytic peptide. Exhibits pH-independent membrane fragmentation activity and probably mediates viral rapid escape from host endosome via organellar membrane lysis. It is not clear if it then remains partially associated with the capsid and involved in the intracellular microtubule-dependent transport of capsid to the nucleus, or if it is lost during endosomal penetration.
Heterodimer with the viral protease; disulfide-linked. Interacts with the viral protease.
Homotrimer. Interacts with the capsid vertex protein; this interaction binds the peripentonal hexons to the neighboring penton base. Interacts with the hexon-linking protein; this interaction tethers the hexons surrounding the penton to those situated in the central plate of the facet. Interacts with the hexon-interlacing protein; this interaction lashes the hexons together. Interacts with host dyneins DYNC1LI1 and DYNC1I2; this interaction might be involved in intracellular microtubule-dependent transport of incoming viral capsid. Interacts with the shutoff protein; this interaction allows folding and formation of hexons trimers. Interacts with pre-protein VI; this interaction probably allows nuclear import of hexon trimers and possibly pre-capsid assembly.
Interacts (via PPxY motif) with host NEDD4 ubiquitine ligase; this interaction might play a role in virus intracellular transport during entry. Part of a complex composed of the core-capsid bridging protein, the endosome lysis protein VI and the hexon-linking protein VIII; these interactions bridge the virus core to the capsid. Interacts with peripentonal hexons; this interaction stabilizes the capsid by gluing two peripentonal hexons together and joining them with an adjacent group-of-nine hexon.
Interacts with hexon protein; this interaction allows nuclear import of hexon trimers and possibly pre-capsid assembly. Interacts (via C-terminal NLS) with importin alpha/beta.
Late-budding domains (L domains) are short sequence motifs essential for viral particle release. They can occur individually or in close proximity within structural proteins. They interacts with sorting cellular proteins of the multivesicular body (MVB) pathway. Most of these proteins are class E vacuolar protein sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes. Minor capsid protein 6 contains one L domain: a PPXY motif which binds to the WW domains of HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases, like NEDD4. In adenoviruses, this motif seems to play a role in microtubule-dependent intracellular trafficking toward the nucleus during virus entry into host cell and in suppression of DAXX-mediated repression of the immediate early E1A promoter.
Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein. Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus.
N-terminal amphipathic alpha-helix domain is essential for the membrane lytic activity.
Pre-protein VI: During virus assembly, promotes hexon trimers nuclear import through nuclear pore complexes via an importin alpha/beta-dependent mechanism. By analogy to herpesviruses capsid assembly, might act as a chaperone to promote the formation of the icosahedral capsid.
Protease cofactor: Cofactor that activates the viral protease. Binds to viral protease in a 1:1 ratio.
Protease cofactor: Contains the major nuclear import and export signals. Proteolytically removed during virion maturation. The processing of the C-terminus turns the precursor into a mature viral structural protein and abrogates its ability to promote hexon import and act as a potential chaperone protein.
Ubiquitinated by Nedd4 following partial capsid disassembly; which might play a role in intracellular virus movement during entry.
Belongs to the adenoviridae hexon-linking protein IIIa family.
Belongs to the adenoviridae packaging protein 3 family.
Cleaved at different sites by the viral protease during virion maturation.
Cleaved near the C-terminus by the viral protease during virion maturation to form the mature protein.
Expressed in the early phase and late phase of the viral replicative cycle.
Interacts with hexon proteins; this interaction tethers the peripentonal hexons to hexons situated in the facet. Interacts with the penton protein (via N-terminus). Interacts with packaging protein 3; this interaction is required to promote correct genome packaging.
Involved in viral genome packaging through its interaction with packaging proteins 1 and 2. After proteolyic cleavage by adenovirus protease, L1 52/55k protein is removed from the capsid during viral maturation.
Part of the genome packaging complex composed of packaging proteins 1, 2 and 3; this complex specifically binds to the packaging sequence on the left end of viral genomic DNA and performs packaging of the viral genome. Interacts with hexon-linking protein IIIa; this interaction is required to promote correct genome packaging.
Structural component of the virion that acts as a cement protein on the capsid exterior which mediates the interactions between the hexons, including the peripentonal hexons, and reaches all the way to the penton vertices. Two hexon linking proteins IIIa, one from each facet, stabilize the unique edge interface between a pair of facets. As the virus enters the host cell, hexon linking proteins IIIa are shed concomitant with virion acidification in the endosome. During virus assembly, seems to play a role in the serotype specificity of the packaging of viral DNA via its interaction with packaging protein 3.
Belongs to the adenoviridae packaging protein 1 family.
Component of the packaging machinery which encapsidates the viral DNA into preformed capsids and transcriptional activator of the viral major late promoter (MLP). Binds, along with packaging proteins 2 and 3, to the specific packaging sequence on the left end of viral genomic DNA and displays ATPase activity thereby providing the power stroke of the packaging machinery. The activity of packaging protein IVa2 is stimulated by protein 33K which acts as a terminase. May be the protein that pumps DNA into the capsid powered by ATP hydrolysis. Specifically binds to the 5'-CG-3' nucleotides of the repeats making up the packaging sequence. Component of the DEF-A and DEF-B transcription factors that bind downstream elements of the major late promoter (MLP), and stimulate transcription from the MLP after initiation of viral DNA replication. DEF-A is a heterodimer packaging proteins 1 and 2 and DEF-B is a homodimer of packaging protein 1.
Homodimer. Part of a genome packaging complex composed of packaging proteins 1, 2 and 3; this complex specifically binds to the packaging sequence on the left end of viral genomic DNA and performs packaging of the viral genome. Interacts with protein 33K.