6z7n
From Proteopedia
The atomic structure of HAdV-F41 at pH 7.4
Structural highlights
FunctionCAP6_ADE41 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.[HAMAP-Rule:MF_04048] 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.[HAMAP-Rule:MF_04048] Cofactor that activates the viral protease. Binds to viral protease in a 1:1 ratio.[HAMAP-Rule:MF_04048] Publication Abstract from PubMedHuman adenovirus (HAdV) types F40 and F41 are a prominent cause of diarrhea and diarrhea-associated mortality in young children worldwide. These enteric HAdVs differ notably in tissue tropism and pathogenicity from respiratory and ocular adenoviruses, but the structural basis for this divergence has been unknown. Here, we present the first structure of an enteric HAdV-HAdV-F41-determined by cryo-electron microscopy to a resolution of 3.8 A. The structure reveals extensive alterations to the virion exterior as compared to nonenteric HAdVs, including a unique arrangement of capsid protein IX. The structure also provides new insights into conserved aspects of HAdV architecture such as a proposed location of core protein V, which links the viral DNA to the capsid, and assembly-induced conformational changes in the penton base protein. Our findings provide the structural basis for adaptation of enteric HAdVs to a fundamentally different tissue tropism. The structure of enteric human adenovirus 41-A leading cause of diarrhea in children.,Rafie K, Lenman A, Fuchs J, Rajan A, Arnberg N, Carlson LA Sci Adv. 2021 Jan 8;7(2):eabe0974. doi: 10.1126/sciadv.abe0974. Print 2021 Jan. PMID:33523995[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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