6ILM
Cryo-EM structure of Echovirus 6 complexed with its uncoating receptor FcRn at PH 7.4
6ILM の概要
エントリーDOI | 10.2210/pdb6ilm/pdb |
EMDBエントリー | 9687 |
分子名称 | Capsid protein VP1, Capsid protein VP2, Capsid protein VP3, ... (9 entities in total) |
機能のキーワード | echovirus 6, fcrn, cryo-em, virus-receptor complex, virus |
由来する生物種 | Homo sapiens (Human) 詳細 |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 136154.83 |
構造登録者 | |
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 Cited by 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: 31104841DOI: 10.1016/j.cell.2019.04.035 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.4 Å) |
構造検証レポート
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