[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

TitleBroad neutralization of influenza B hemagglutinin antibodies via receptor mimicry and glycan engagement.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 123, Issue 18, Page e2532989123, Year 2026
Publish dateMay 5, 2026
AuthorsKuan-Ying A Huang / Hong Thuy Vy Nguyen / Yi-Yin Chen / Kai-Jung Wu / Po-Hsien Hsu / Yo-Min Liu / Tzou-Yien Lin / Che Ma /
PubMed AbstractInfluenza B virus contributes to seasonal influenza epidemics and causes global morbidity and mortality. The two antigenically distinct lineages, Victoria and Yamagata, cocirculate within the ...Influenza B virus contributes to seasonal influenza epidemics and causes global morbidity and mortality. The two antigenically distinct lineages, Victoria and Yamagata, cocirculate within the population and are subject to ongoing antigenic drift. In this study, we report the isolation of cross-lineage neutralizing anti-influenza B hemagglutinin (HA) monoclonal antibodies, exhibiting hemagglutination-inhibition activities, from vaccinated adult donors. While some antibodies exhibit reduced activities against recently emerged antigenic variants, BP-1A and BO-6B demonstrate broad neutralization across influenza B viruses isolated over the past two decades and confer protection in mice against lethal challenge from both lineages. Structural analysis of the antibody Fab domains in complex with HA reveals two distinct molecular binding modes: BP-1A uses a long heavy chain CDR3 loop that mimics the ligand to target the receptor-binding site, while BO-6B engages a conserved cleft on the surface of vestigial esterase subdomain through key interactions with glycan moieties. These findings elucidate the molecular basis for broad neutralization by human anti-influenza B HA antibodies and provide insights that may guide the development of immunotherapeutics and rational vaccine design.
External linksProc Natl Acad Sci U S A / PubMed:42060718 / PubMed Central
MethodsEM (single particle)
Resolution2.59 - 3.09 Å
Structure data

66599

9x5w

EMDB-66599, PDB-9x5w:
B/Brisbane/60/2008 HA in complex with BP-1A
Method: EM (single particle) / Resolution: 2.76 Å

66600

9x5x

EMDB-66600, PDB-9x5x:
B/Brisbane/60/2008 HA in complex with FV2DP1-1B
Method: EM (single particle) / Resolution: 2.76 Å

66601

9x5y

EMDB-66601, PDB-9x5y:
B/Brisbane/60/2008 HA in complex with BO-6B
Method: EM (single particle) / Resolution: 2.65 Å

66602

9x5z

EMDB-66602, PDB-9x5z:
B/Phuket/3073/2013-like HA in complex with BP-1A
Method: EM (single particle) / Resolution: 2.59 Å

66603

9x60

EMDB-66603, PDB-9x60:
B/Hubei-Wujiagang/158/2009 HA in complex with FV2DP1-1B
Method: EM (single particle) / Resolution: 3.09 Å

66604

9x61

EMDB-66604, PDB-9x61:
B/Hubei-Wujiagang/158/2009 HA in complex with BO-6B
Method: EM (single particle) / Resolution: 2.99 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • homo sapiens (human)
  • influenza b virus (b/brisbane/60/2008)
  • influenza b virus
  • influenza b virus (b/hubei-wujiagang/158/2009)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / Hemagglutinin / HA / antibody / influenza B virus / BP-1A / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex / FV2DP1-1B / BO-6B

+
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