8E31

Purification of Enterovirus A71, strain 4643, WT capsid

8E31 の概要

• エントリーDOI: 10.2210/pdb8e31/pdb
• EMDBエントリー: 27853
• 分子名称: VP1, Genome polyprotein, VP3 (3 entities in total)
• 機能のキーワード: enterovirus, thermostability, capsid, virus
• 由来する生物種: Enterovirus A71; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 73737.83

構造登録者

Catching, A.,Capponi, S.,Andino, R. (登録日: 2022-08-16, 公開日: 2023-08-30, 最終更新日: 2023-12-06)

主引用文献

Catching, A.,Te Yeh, M.,Bianco, S.,Capponi, S.,Andino, R.
A tradeoff between enterovirus A71 particle stability and cell entry.
Nat Commun, 14:7450-7450, 2023

PubMed Abstract: A central role of viral capsids is to protect the viral genome from the harsh extracellular environment while facilitating initiation of infection when the virus encounters a target cell. Viruses are thought to have evolved an optimal equilibrium between particle stability and efficiency of cell entry. In this study, we genetically perturb this equilibrium in a non-enveloped virus, enterovirus A71 to determine its structural basis. We isolate a single-point mutation variant with increased particle thermotolerance and decreased efficiency of cell entry. Using cryo-electron microscopy and molecular dynamics simulations, we determine that the thermostable native particles have acquired an expanded conformation that results in a significant increase in protein dynamics. Examining the intermediate states of the thermostable variant reveals a potential pathway for uncoating. We propose a sequential release of the lipid pocket factor, followed by internal VP4 and ultimately the viral RNA.

PubMed: 37978288
DOI: 10.1038/s41467-023-43029-0

実験手法

ELECTRON MICROSCOPY (14 Å)