6HBJ

Echovirus 18 empty particle

6HBJ の概要

• エントリーDOI: 10.2210/pdb6hbj/pdb
• EMDBエントリー: 0183
• 分子名称: Viral protein 1, Viral protein 2, Viral protein 3 (3 entities in total)
• 機能のキーワード: echovirus, echovirus 18, empty particle, b-particle, enterovirus, picornavirus, virus
• 由来する生物種: Echovirus E18; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 87510.56

構造登録者

Buchta, D.,Fuzik, T.,Hrebik, D.,Levdansky, Y.,Moravcova, J.,Plevka, P. (登録日: 2018-08-10, 公開日: 2019-03-20, 最終更新日: 2024-11-20)

主引用文献

Buchta, D.,Fuzik, T.,Hrebik, D.,Levdansky, Y.,Sukenik, L.,Mukhamedova, L.,Moravcova, J.,Vacha, R.,Plevka, P.
Enterovirus particles expel capsid pentamers to enable genome release.
Nat Commun, 10:1138-1138, 2019

PubMed Abstract: Viruses from the genus Enterovirus are important human pathogens. Receptor binding or exposure to acidic pH in endosomes converts enterovirus particles to an activated state that is required for genome release. However, the mechanism of enterovirus uncoating is not well understood. Here, we use cryo-electron microscopy to visualize virions of human echovirus 18 in the process of genome release. We discover that the exit of the RNA from the particle of echovirus 18 results in a loss of one, two, or three adjacent capsid-protein pentamers. The opening in the capsid, which is more than 120 Å in diameter, enables the release of the genome without the need to unwind its putative double-stranded RNA segments. We also detect capsids lacking pentamers during genome release from echovirus 30. Thus, our findings uncover a mechanism of enterovirus genome release that could become target for antiviral drugs.

PubMed: 30850609
DOI: 10.1038/s41467-019-09132-x

実験手法

ELECTRON MICROSCOPY (3.16 Å)