7dpg
Cryo-EM structure of Coxsackievirus B1 empty particle
Structural highlights
FunctionA0A7T7KAA0_9ENTO Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation (By similarity). Allows the capsid to remain inactive before the maturation step.[ARBA:ARBA00025202] Publication Abstract from PubMedEnterovirus uncoating receptors bind at the surface depression ("canyon") that encircles each capsid vertex causing the release of a host-derived lipid called "pocket factor" that is buried in a hydrophobic pocket formed by the major viral capsid protein, VP1. Coxsackievirus and adenovirus receptor (CAR) is a universal uncoating receptor of group B coxsackieviruses (CVB). Here, we present five high-resolution cryoEM structures of CVB representing different stages of virus infection. Structural comparisons show that the CAR penetrates deeper into the canyon than other uncoating receptors, leading to a cascade of events: collapse of the VP1 hydrophobic pocket, high-efficiency release of the pocket factor and viral uncoating and genome release under neutral pH, as compared with low pH. Furthermore, we identified a potent therapeutic antibody that can neutralize viral infection by interfering with virion-CAR interactions, destabilizing the capsid and inducing virion disruption. Together, these results define the structural basis of CVB cell entry and antibody neutralization. Cryo-EM structures reveal the molecular basis of receptor-initiated coxsackievirus uncoating.,Xu L, Zheng Q, Zhu R, Yin Z, Yu H, Lin Y, Wu Y, He M, Huang Y, Jiang Y, Sun H, Zha Z, Yang H, Huang Q, Zhang D, Chen Z, Ye X, Han J, Yang L, Liu C, Que Y, Fang M, Gu Y, Zhang J, Luo W, Zhou ZH, Li S, Cheng T, Xia N Cell Host Microbe. 2021 Mar 10;29(3):448-462.e5. doi: 10.1016/j.chom.2021.01.001. , Epub 2021 Feb 3. PMID:33539764[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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