[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

TitleIdentification of Antibodies with Non-overlapping Neutralization Sites that Target Coxsackievirus A16.
Journal, issue, pagesCell Host Microbe, Vol. 27, Issue 2, Page 249-261.e5, Year 2020
Publish dateFeb 12, 2020
AuthorsMaozhou He / Longfa Xu / Qingbing Zheng / Rui Zhu / Zhichao Yin / Zhenghui Zha / Yu Lin / Lisheng Yang / Yang Huang / Xiangzhong Ye / Shuxuan Li / Wangheng Hou / Yangtao Wu / Jinle Han / Dongxiao Liu / Zekai Li / Zhenqin Chen / Hai Yu / Yuqiong Que / Yingbin Wang / Xiaodong Yan / Jun Zhang / Ying Gu / Z Hong Zhou / Tong Cheng / Shaowei Li / Ningshao Xia /
PubMed AbstractHand, foot, and mouth disease is a common childhood illness primarily caused by coxsackievirus A16 (CVA16), for which there are no current vaccines or treatments. We identify three CVA16-specific ...Hand, foot, and mouth disease is a common childhood illness primarily caused by coxsackievirus A16 (CVA16), for which there are no current vaccines or treatments. We identify three CVA16-specific neutralizing monoclonal antibodies (nAbs) with therapeutic potential: 18A7, 14B10, and NA9D7. We present atomic structures of these nAbs bound to all three viral particle forms-the mature virion, A-particle, and empty particle-and show that each Fab can simultaneously occupy the mature virion. Additionally, 14B10 or NA9D7 provide 100% protection against lethal CVA16 infection in a neonatal mouse model. 18A7 binds to a non-conserved epitope present in all three particles, whereas 14B10 and NA9D7 recognize broad protective epitopes but only bind the mature virion. NA9D7 targets an immunodominant site, which may overlap the receptor-binding site. These findings indicate that CVA16 vaccines should be based on mature virions and that these antibodies could be used to discriminate optimal virion-based immunogens.
External linksCell Host Microbe / PubMed:32027857 / PubMed Central
MethodsEM (single particle)
Resolution2.65 - 3.78 Å
Structure data

EMDB-0887, PDB-6lha:
The cryo-EM structure of coxsackievirus A16 mature virion
Method: EM (single particle) / Resolution: 3.56 Å

EMDB-0888, PDB-6lhb:
The cryo-EM structure of coxsackievirus A16 A-particle
Method: EM (single particle) / Resolution: 3.33 Å

EMDB-0889, PDB-6lhc:
The cryo-EM structure of coxsackievirus A16 empty particle
Method: EM (single particle) / Resolution: 3.43 Å

EMDB-0890, PDB-6lhk:
The cryo-EM structure of coxsackievirus A16 mature virion in complex with Fab 18A7
Method: EM (single particle) / Resolution: 2.65 Å

EMDB-0891, PDB-6lhl:
The cryo-EM structure of coxsackievirus A16 A-particle in complex with Fab 18A7
Method: EM (single particle) / Resolution: 3.07 Å

EMDB-0892, PDB-6lho:
The cryo-EM structure of coxsackievirus A16 empty particle in complex with Fab 18A7
Method: EM (single particle) / Resolution: 3.13 Å

EMDB-0894, PDB-6lhp:
The cryo-EM structure of coxsackievirus A16 mature virion in complex with Fab 14B10
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-0895, PDB-6lhq:
The cryo-EM structure of coxsackievirus A16 mature virion in complex with Fab NA9D7
Method: EM (single particle) / Resolution: 3.06 Å

EMDB-0897, PDB-6lht:
Localized reconstruction of coxsackievirus A16 mature virion in complex with Fab 18A7
Method: EM (single particle) / Resolution: 3.67 Å

EMDB-0898:
The cryo-EM structure of coxsackievirus A16 mature virion in complex with Fabs 18A7, 14B10 and NA9D7
Method: EM (single particle) / Resolution: 3.78 Å

Chemicals

ChemComp-SPH:
SPHINGOSINE / Sphingosine

Source
  • coxsackievirus a16
  • mus musculus (house mouse)
KeywordsVIRUS / VIRAL PROTEIN / localized reconstruction

+
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