6ILN

Cryo-EM structure of full Echovirus 6 particle at PH 5.5

Summary for 6ILN

• Entry DOI: 10.2210/pdb6iln/pdb
• EMDB information: 9688
• Descriptor: Capsid protein VP1, Capsid protein VP2, Capsid protein VP3, ... (5 entities in total)
• Functional Keywords: virus
• Biological source: Echovirus E6; More
• Total number of polymer chains: 4
• Total formula weight: 93332.79

Authors

Gao, G.F.,Liu, S.,Zhao, X.,Peng, R. (deposition date: 2018-10-19, release date: 2019-05-15, Last modification date: 2024-03-27)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.4 Å)