Structural highlights
Function
[HEX8_ADE05] Hexon-linking protein: Structural component of the virion that lashes peripentonal hexons to the hexons situated in the facets thanks to its interaction with the capsid vertex protein. Also binds together hexons of different facets. [HEX_ADE05] 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 (By similarity). 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. [PEN3_ADE05] Major capsid protein that self-associates to form penton base pentamers, each in the shape of a pentagon, situated at the 12 verteces of the pseudo T=25 capsid. Involved in virus secondary attachment to host cell after initial attachment by the fiber protein. Binds host integrin heterodimer ITGAV-ITGB5 (alphaV-beta5) thereby triggering clathrin-mediated endocytosis of virions. Mediates initial virus attachment to CXADR-negative cells. Binding to integrins ITGAV-ITGB5 also seems to induce macropinocytosis uptake of the virus. As the virus enters the host cell, penton proteins are shedded concomitant with virion acidification in the endosome.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Construction of a complex virus may involve a hierarchy of assembly elements. Here, we report the structure of the whole human adenovirus virion at 3.6 angstroms resolution by cryo-electron microscopy (cryo-EM), revealing in situ atomic models of three minor capsid proteins (IIIa, VIII, and IX), extensions of the (penton base and hexon) major capsid proteins, and interactions within three protein-protein networks. One network is mediated by protein IIIa at the vertices, within group-of-six (GOS) tiles--a penton base and its five surrounding hexons. Another is mediated by ropes (protein IX) that lash hexons together to form group-of-nine (GON) tiles and bind GONs to GONs. The third, mediated by IIIa and VIII, binds each GOS to five surrounding GONs. Optimization of adenovirus for cancer and gene therapy could target these networks.
Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks.,Liu H, Jin L, Koh SB, Atanasov I, Schein S, Wu L, Zhou ZH Science. 2010 Aug 27;329(5995):1038-43. PMID:20798312[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lyle C, McCormick F. Integrin alphavbeta5 is a primary receptor for adenovirus in CAR-negative cells. Virol J. 2010 Jul 8;7:148. doi: 10.1186/1743-422X-7-148. PMID:20615244 doi:10.1186/1743-422X-7-148
- ↑ Liu H, Jin L, Koh SB, Atanasov I, Schein S, Wu L, Zhou ZH. Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks. Science. 2010 Aug 27;329(5995):1038-43. PMID:20798312 doi:10.1126/science.1187433
- ↑ Liu H, Jin L, Koh SB, Atanasov I, Schein S, Wu L, Zhou ZH. Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks. Science. 2010 Aug 27;329(5995):1038-43. PMID:20798312 doi:10.1126/science.1187433
