[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

TitleBroadly neutralizing antibodies target a haemagglutinin anchor epitope.
Journal, issue, pagesNature, Vol. 602, Issue 7896, Page 314-320, Year 2022
Publish dateDec 23, 2021
AuthorsJenna J Guthmiller / Julianna Han / Henry A Utset / Lei Li / Linda Yu-Ling Lan / Carole Henry / Christopher T Stamper / Meagan McMahon / George O'Dell / Monica L Fernández-Quintero / Alec W Freyn / Fatima Amanat / Olivia Stovicek / Lauren Gentles / Sara T Richey / Alba Torrents de la Peña / Victoria Rosado / Haley L Dugan / Nai-Ying Zheng / Micah E Tepora / Dalia J Bitar / Siriruk Changrob / Shirin Strohmeier / Min Huang / Adolfo García-Sastre / Klaus R Liedl / Jesse D Bloom / Raffael Nachbagauer / Peter Palese / Florian Krammer / Lynda Coughlan / Andrew B Ward / Patrick C Wilson /
PubMed AbstractBroadly neutralizing antibodies that target epitopes of haemagglutinin on the influenza virus have the potential to provide near universal protection against influenza virus infection. However, viral ...Broadly neutralizing antibodies that target epitopes of haemagglutinin on the influenza virus have the potential to provide near universal protection against influenza virus infection. However, viral mutants that escape broadly neutralizing antibodies have been reported. The identification of broadly neutralizing antibody classes that can neutralize viral escape mutants is critical for universal influenza virus vaccine design. Here we report a distinct class of broadly neutralizing antibodies that target a discrete membrane-proximal anchor epitope of the haemagglutinin stalk domain. Anchor epitope-targeting antibodies are broadly neutralizing across H1 viruses and can cross-react with H2 and H5 viruses that are a pandemic threat. Antibodies that target this anchor epitope utilize a highly restricted repertoire, which encodes two public binding motifs that make extensive contacts with conserved residues in the fusion peptide. Moreover, anchor epitope-targeting B cells are common in the human memory B cell repertoire and were recalled in humans by an oil-in-water adjuvanted chimeric haemagglutinin vaccine, which is a potential universal influenza virus vaccine. To maximize protection against seasonal and pandemic influenza viruses, vaccines should aim to boost this previously untapped source of broadly neutralizing antibodies that are widespread in the human memory B cell pool.
External linksNature / PubMed:34942633 / PubMed Central
MethodsEM (single particle)
Resolution3.38 - 20.0 Å
Structure data

EMDB-25634:
Negative stain map of monoclonal Fab 047-09 4F04 binding the anchor epitope of H1 HA
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-25635:
Negative stain map of monoclonal Fab 241 IgA 2F04 binding the anchor epitope of H1 HA
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-25636:
Negative stain map of polyclonal Fab 236.7 binding the anchor and esterase epitopes of H1 HA
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-25637:
Negative stain map of polyclonal Fab 236.7 binding the RBS epitope of H1 HA
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-25638:
Negative stain map of polyclonal Fab 236.14 binding an epitope on the top of the head of H1 HA
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-25639:
Negative stain map of polyclonal Fab 236.14 binding the esterase epitope of H1 HA
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-25640:
Negative stain map of polycolonal Fab 236.14 binding the RBS epitope of H1 HA
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-25641:
Negative stain map of polyclonal Fab 236.14 binding the anchor epitope of H1 HA
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-25642:
Negative stain map of polyclonal Fab 241.7 binding the esterase epitope of H1 HA
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-25643:
Negative stain map of polyclonal Fab 241.14 binding the anchor epitope of H1 HA
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-25644:
Negative stain map of polyclonal Fab 241.14 binding the esterase epitope of H1 HA
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-25645:
Negative stain map of polyclonal Fab 241.14 binding an epitope on the top of the head of H1 HA
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-25646:
Negative stain map of polyclonal Fab 241.14 binding the RBS epitope of H1 HA
Method: EM (single particle) / Resolution: 20.0 Å

25655

7t3d

EMDB-25655, PDB-7t3d:
CryoEM map of anchor 222-1C06 Fab and lateral patch 2B05 Fab binding H1 HA
Method: EM (single particle) / Resolution: 3.38 Å

Chemicals

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

Source
  • homo sapiens (human)
  • influenza a virus (a/california/04/2009(h1n1))
KeywordsViral Protein/IMMUNE SYSTEM / anchor / antibodies / influenza A virus / hemagglutinin / IMMUNE SYSTEM / Viral Protein-IMMUNE SYSTEM complex

+
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