Structural highlights
FunctionG9G853_9ADEN 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.[HAMAP-Rule:MF_04048] 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.[HAMAP-Rule:MF_04048] Protease cofactor: Cofactor that activates the viral protease. Binds to viral protease in a 1:1 ratio.[HAMAP-Rule:MF_04048] Publication Abstract from PubMed[Figure: see text]. ChAdOx1 interacts with CAR and PF4 with implications for thrombosis with thrombocytopenia syndrome.,Baker AT, Boyd RJ, Sarkar D, Teijeira-Crespo A, Chan CK, Bates E, Waraich K, Vant J, Wilson E, Truong CD, Lipka-Lloyd M, Fromme P, Vermaas J, Williams D, Machiesky L, Heurich M, Nagalo BM, Coughlan L, Umlauf S, Chiu PL, Rizkallah PJ, Cohen TS, Parker AL, Singharoy A, Borad MJ Sci Adv. 2021 Dec 3;7(49):eabl8213. doi: 10.1126/sciadv.abl8213. Epub 2021 Dec 1. PMID:34851659[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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