6ILO

Cryo-EM structure of empty Echovirus 6 particle at PH 7.4

6ILO の概要

• エントリーDOI: 10.2210/pdb6ilo/pdb
• EMDBエントリー: 9689
• 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: virus
• 由来する生物種: Echovirus E6; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 79846.88

構造登録者

Gao, G.F.,Liu, S.,Zhao, X.,Peng, R. (登録日: 2018-10-19, 公開日: 2019-05-15, 最終更新日: 2025-07-02)

主引用文献

Zhao, X.,Zhang, G.,Liu, S.,Chen, X.,Peng, R.,Dai, L.,Qu, X.,Li, S.,Song, H.,Gao, Z.,Yuan, P.,Liu, Z.,Li, C.,Shang, Z.,Li, Y.,Zhang, M.,Qi, J.,Wang, H.,Du, N.,Wu, Y.,Bi, Y.,Gao, S.,Shi, Y.,Yan, J.,Zhang, Y.,Xie, Z.,Wei, W.,Gao, G.F.
Human Neonatal Fc Receptor Is the Cellular Uncoating Receptor for Enterovirus B.
Cell, 177:1553-1565.e16, 2019

PubMed Abstract: Enterovirus B (EV-B), a major proportion of the genus Enterovirus in the family Picornaviridae, is the causative agent of severe human infectious diseases. Although cellular receptors for coxsackievirus B in EV-B have been identified, receptors mediating virus entry, especially the uncoating process of echovirus and other EV-B remain obscure. Here, we found that human neonatal Fc receptor (FcRn) is the uncoating receptor for major EV-B. FcRn binds to the virus particles in the "canyon" through its FCGRT subunit. By obtaining multiple cryo-electron microscopy structures at different stages of virus entry at atomic or near-atomic resolution, we deciphered the underlying mechanisms of enterovirus attachment and uncoating. These structures revealed that different from the attachment receptor CD55, binding of FcRn to the virions induces efficient release of "pocket factor" under acidic conditions and initiates the conformational changes in viral particle, providing a structural basis for understanding the mechanisms of enterovirus entry.

PubMed: 31104841
DOI: 10.1016/j.cell.2019.04.035

実験手法

ELECTRON MICROSCOPY (3.2 Å)