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- W3128781611 abstract "Enterovirus 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." @default.
- W3128781611 created "2021-02-15" @default.
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- W3128781611 date "2021-03-01" @default.
- W3128781611 modified "2023-10-16" @default.
- W3128781611 title "Cryo-EM structures reveal the molecular basis of receptor-initiated coxsackievirus uncoating" @default.
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