EMD-30805

Single-particle
3.2 Å
EMD-30805 Deposition: 18/12/2020
Map released: 05/05/2021
Last modified: 27/03/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-30805

Cryo-EM structure of Coxsackievirus B1 mature virion

EMD-30805

Single-particle
3.2 Å
EMD-30805 Deposition: 18/12/2020
Map released: 05/05/2021
Last modified: 27/03/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Coxsackievirus B1
Sample: Coxsackievirus B1
Fitted models: 7dpf (Avg. Q-score: 0.601)

Deposition Authors: Zheng Q, Li S
Cryo-EM structures reveal the molecular basis of receptor-initiated coxsackievirus uncoating.
PUBMED: 33539764
DOI: doi:10.1016/j.chom.2021.01.001
ISSN: 1934-6069
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.