| Literature DB >> 31104841 |
Xin Zhao1, Guigen Zhang2, Sheng Liu3, Xiangpeng Chen4, Ruchao Peng5, Lianpan Dai6, Xiao Qu5, Shihua Li5, Hao Song6, Zhengrong Gao7, Pengfei Yuan8, Zhiheng Liu9, Changyao Li5, Zifang Shang6, Yan Li5, Meifan Zhang5, Jianxun Qi5, Han Wang6, Ning Du6, Yan Wu6, Yuhai Bi1, Shan Gao10, Yi Shi1, Jinghua Yan11, Yong Zhang12, Zhengde Xie13, Wensheng Wei14, George F Gao15.
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.Entities:
Keywords: FcRn; attachment; cryo-EM; echovirus; enterovirus; human neonatal Fc receptor; receptor; uncoating
Year: 2019 PMID: 31104841 DOI: 10.1016/j.cell.2019.04.035
Source DB: PubMed Journal: Cell ISSN: 0092-8674 Impact factor: 41.582