[English] 日本語
Yorodumi Papers
- Database of articles cited by EMDB/PDB/SASBDB data -

+
Search query

Keywords
Structure methods
Author
Journal
IF

-
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 / 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

+
About Yorodumi Papers

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi Papers

Database of articles cited by EMDB/PDB/SASBDB data

  • Database of articles cited by EMDB, PDB, and SASBDB entries
  • Using PubMed data

Related info.:EMDB / PDB / SASBDB / Yorodumi / EMN Papers / Changes in new EM Navigator and Yorodumi

Read more