[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

TitleConvergence of a common solution for broad ebolavirus neutralization by glycan cap-directed human antibodies.
Journal, issue, pagesCell Rep, Vol. 35, Issue 2, Page 108984, Year 2021
Publish dateApr 13, 2021
AuthorsCharles D Murin / Pavlo Gilchuk / Philipp A Ilinykh / Kai Huang / Natalia Kuzmina / Xiaoli Shen / Jessica F Bruhn / Aubrey L Bryan / Edgar Davidson / Benjamin J Doranz / Lauren E Williamson / Jeffrey Copps / Tanwee Alkutkar / Andrew I Flyak / Alexander Bukreyev / James E Crowe / Andrew B Ward /
PubMed AbstractAntibodies that target the glycan cap epitope on the ebolavirus glycoprotein (GP) are common in the adaptive response of survivors. A subset is known to be broadly neutralizing, but the details of ...Antibodies that target the glycan cap epitope on the ebolavirus glycoprotein (GP) are common in the adaptive response of survivors. A subset is known to be broadly neutralizing, but the details of their epitopes and basis for neutralization are not well understood. Here, we present cryoelectron microscopy (cryo-EM) structures of diverse glycan cap antibodies that variably synergize with GP base-binding antibodies. These structures describe a conserved site of vulnerability that anchors the mucin-like domains (MLDs) to the glycan cap, which we call the MLD anchor and cradle. Antibodies that bind to the MLD cradle share common features, including use of IGHV1-69 and IGHJ6 germline genes, which exploit hydrophobic residues and form β-hairpin structures to mimic the MLD anchor, disrupt MLD attachment, destabilize GP quaternary structure, and block cleavage events required for receptor binding. Our results provide a molecular basis for ebolavirus neutralization by broadly reactive glycan cap antibodies.
External linksCell Rep / PubMed:33852862 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.002 - 9.9 Å
Structure data

EMDB-22839, PDB-7kej:
BDBV-289 bound to EBOV GPdMuc Makona
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-22841: Bundibugyo virus GP (mucin deleted) bound to antibody Fab BDBV-43 and ADI-15878
PDB-7kew: Bundibugyo virus GP (mucin deleted) bound to antibody Fab BDBV-43
Method: EM (single particle) / Resolution: 4.16 Å

EMDB-22842, PDB-7kex:
Ebola virus GP (mucin deleted, Makona strain) bound to antibody Fab EBOV-293
Method: EM (single particle) / Resolution: 4.25 Å

EMDB-22847, PDB-7kf9:
Ebola virus GP (mucin deleted, Makona strain) bound to antibody Fab EBOV-296 and EBOV-515
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-22848: Ebola virus GP (mucin deleted, Makona strain) bound to antibody Fab EBOV-442 and EBOV-515
PDB-7kfb: Ebola virus GP (mucin deleted, Makona strain) bound to antibody Fab EBOV-442
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-22851: Bundibugyo virus GP (mucin deleted) bound to antibody Fab BDBV-329 and EBOV-515
PDB-7kfe: Bundibugyo virus GP (mucin deleted) bound to antibody Fab BDBV-329
Method: EM (single particle) / Resolution: 6.6 Å

EMDB-22852:
Ebola virus GP (mucin deleted, Makona strain) bound to antibody Fab EBOV-237 and EBOV-515
Method: EM (single particle) / Resolution: 9.9 Å

EMDB-22853: Ebola virus GP (mucin deleted, Makona strain) bound to antibody Fab EBOV-437 and EBOV-515
PDB-7kfh: Ebola virus GP (mucin deleted, Makona strain) bound to antibody Fab EBOV-437
Method: EM (single particle) / Resolution: 3.8 Å

PDB-7kfg:
Antibody Fab BDBV-289
Method: X-RAY DIFFRACTION / Resolution: 3.002 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER / Diethylene glycol

Source
  • homo sapiens (human)
  • ebola virus
  • zaire ebolavirus
  • bundibugyo ebolavirus
KeywordsVIRAL PROTEIN/Immune System / ebolavirus / glycan cap / antibody / broadly neutralizing / filovirus / VIRAL PROTEIN / VIRAL PROTEIN-Immune System complex / IMMUNE SYSTEM

+
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