7DPZ

Cryo-EM structure of Coxsackievirus B1 virion in complex with CAR

7DPZ の概要

• エントリーDOI: 10.2210/pdb7dpz/pdb
• EMDBエントリー: 30812
• 分子名称: Virion protein 1, VP2, VP3, ... (5 entities in total)
• 機能のキーワード: coxsackievirus b1, car, cryo-em, virus
• 由来する生物種: Coxsackievirus B1; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 107614.23

構造登録者

Li, S.,Zhu, R.,Xu, L.,Cheng, T.,Zheng, Q. (登録日: 2020-12-22, 公開日: 2021-05-05, 最終更新日: 2025-07-02)

主引用文献

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, Z.H.,Li, S.,Cheng, T.,Xia, N.
Cryo-EM structures reveal the molecular basis of receptor-initiated coxsackievirus uncoating.
Cell Host Microbe, 29:448-462.e5, 2021

PubMed 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.

PubMed: 33539764
DOI: 10.1016/j.chom.2021.01.001

実験手法

ELECTRON MICROSCOPY (3.8 Å)