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Structure paper

TitleHuman Neonatal Fc Receptor Is the Cellular Uncoating Receptor for Enterovirus B.
Journal, issue, pagesCell, Vol. 177, Issue 6, Page 1553-1565.e16, Year 2019
Publish dateMay 30, 2019
AuthorsXin Zhao / Guigen Zhang / Sheng Liu / Xiangpeng Chen / Ruchao Peng / Lianpan Dai / Xiao Qu / Shihua Li / Hao Song / Zhengrong Gao / Pengfei Yuan / Zhiheng Liu / Changyao Li / Zifang Shang / Yan Li / Meifan Zhang / Jianxun Qi / Han Wang / Ning Du / Yan Wu / Yuhai Bi / Shan Gao / Yi Shi / Jinghua Yan / Yong Zhang / Zhengde Xie / Wensheng Wei / George F Gao /
PubMed AbstractEnterovirus 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 ...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.
External linksCell / PubMed:31104841 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 3.8 Å
Structure data

9684

6ilj

EMDB-9684, PDB-6ilj:
Cryo-EM structure of Echovirus 6 complexed with its attachment receptor CD55 at PH 5.5
Method: EM (single particle) / Resolution: 3.6 Å

9685

6ilk

EMDB-9685, PDB-6ilk:
Cryo-EM structure of Echovirus 6 complexed with its attachment receptor CD55 at PH 7.4
Method: EM (single particle) / Resolution: 3.0 Å

9686

6ill

EMDB-9686, PDB-6ill:
Cryo-EM structure of Echovirus 6 complexed with its uncoating receptor FcRn at PH 5.5
Method: EM (single particle) / Resolution: 3.8 Å

9687

6ilm

EMDB-9687, PDB-6ilm:
Cryo-EM structure of Echovirus 6 complexed with its uncoating receptor FcRn at PH 7.4
Method: EM (single particle) / Resolution: 3.4 Å

9688

6iln

EMDB-9688, PDB-6iln:
Cryo-EM structure of full Echovirus 6 particle at PH 5.5
Method: EM (single particle) / Resolution: 3.4 Å

9689

6ilo

EMDB-9689, PDB-6ilo:
Cryo-EM structure of empty Echovirus 6 particle at PH 7.4
Method: EM (single particle) / Resolution: 3.2 Å

9690

6ilp

EMDB-9690, PDB-6ilp:
Cryo-EM structure of full Echovirus 6 particle at PH 7.4
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-SPH:
SPHINGOSINE

ChemComp-K:
Unknown entry

ChemComp-NA:
Unknown entry

Source
  • echovirus e6
  • homo sapiens (human)
KeywordsVIRUS / Echovirus 6 / CD55 / Cryo-EM / virus-receptor complex / FcRn

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