7C4Z

Cryo-EM structure of empty Coxsackievirus A10 at pH 5.5

7C4Z の概要

• エントリーDOI: 10.2210/pdb7c4z/pdb
• EMDBエントリー: 30292
• 分子名称: Capsid protein VP1, Capsid protein VP2, Capsid protein VP3 (3 entities in total)
• 機能のキーワード: picornavirus, coxsackievirus a10, ph 5.5, empty particle, virus
• 由来する生物種: Coxsackievirus A10; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 87175.06

構造登録者

Cui, Y.,Peng, R.,Song, H.,Tong, Z.,Gao, G.F.,Qi, J. (登録日: 2020-05-18, 公開日: 2020-07-22, 最終更新日: 2024-03-27)

主引用文献

Cui, Y.,Peng, R.,Song, H.,Tong, Z.,Qu, X.,Liu, S.,Zhao, X.,Chai, Y.,Wang, P.,Gao, G.F.,Qi, J.
Molecular basis of Coxsackievirus A10 entry using the two-in-one attachment and uncoating receptor KRM1.
Proc.Natl.Acad.Sci.USA, 117:18711-18718, 2020

PubMed Abstract: KREMEN1 (KRM1) has been identified as a functional receptor for Coxsackievirus A10 (CV-A10), a causative agent of hand-foot-and-mouth disease (HFMD), which poses a great threat to infants globally. However, the underlying mechanisms for the viral entry process are not well understood. Here we determined the atomic structures of different forms of CV-A10 viral particles and its complex with KRM1 in both neutral and acidic conditions. These structures reveal that KRM1 selectively binds to the mature viral particle above the canyon of the viral protein 1 (VP1) subunit and contacts across two adjacent asymmetry units. The key residues for receptor binding are conserved among most KRM1-dependent enteroviruses, suggesting a uniform mechanism for receptor binding. Moreover, the binding of KRM1 induces the release of pocket factor, a process accelerated under acidic conditions. Further biochemical studies confirmed that receptor binding at acidic pH enabled CV-A10 virion uncoating in vitro. Taken together, these findings provide high-resolution snapshots of CV-A10 entry and identify KRM1 as a two-in-one receptor for enterovirus infection.

PubMed: 32690697
DOI: 10.1073/pnas.2005341117

実験手法

ELECTRON MICROSCOPY (3.3 Å)