Structural highlights
FunctionQ9QAH8_ADE41 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.[HAMAP-Rule:MF_04052] 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. See AlsoReferences
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