Evidence map›Paper›PMID 24049169›Full record

ArticleJournal of virology2013

A unique and conserved neutralization epitope in H5N1 influenza viruses identified by an antibody against the A/Goose/Guangdong/1/96 hemagglutinin.

Xueyong Zhu, Yong-Hui Guo, Tao Jiang, Ya-Di Wang, Kwok-Hung Chan, Xiao-Feng Li, Wenli Yu, Ryan McBride, James C Paulson, Kwok-Yung Yuen and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.7field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

52 citing papers in PubMed, 71 citations in OpenAlex.

  1. Review
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  12. AI-based antibody design targeting recent H5N1 avian influenza strains.Computational and structural biotechnology journal · 2025
    Article
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  15. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 5 institutions in 3 countries.

Xueyong ZhuDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, USA.
Yong-Hui Guo
Tao Jiang
Ya-Di Wang
Kwok-Hung Chan
Xiao-Feng Li
Wenli Yu
Ryan McBride
James C Paulson
Kwok-Yung Yuen
Cheng-Feng Qin
Xiao-Yan Che
Ian A Wilson
Scripps Research Institute · USInstitute of Microbiology · CNSouthern Medical University · CNUniversity of Hong Kong · HKZhujiang Hospital · CN

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
Viral and Host cDNA Libraries from 1918 Influenza CasesP01AI058113 · NIAID · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI GARCIA-SASTRE, ADOLFO · 2004 to 2010
$20.3M
Structural insights into pandemic and emerging influenza virusesR56AI099275 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI WILSON, IAN A · 2013 to 2013
$823k
NCI NIH HHS Y1-CO-1020NCRR NIH HHS P41 RR001209NCRR NIH HHS P41RR001209NIAID NIH HHS AI058113NIAID NIH HHS P01 AI058113NIAID NIH HHS R56 AI099275NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

Despite substantial efforts to control and contain H5N1 influenza viruses, bird flu viruses continue to spread and evolve. Neutralizing antibodies against conserved epitopes on the viral hemagglutinin (HA) could confer immunity to the diverse H5N1 virus strains and provide information for effective vaccine design. Here, we report the characterization of a broadly neutralizing murine monoclonal antibody, H5M9, to most H5N1 clades and subclades that was elicited by immunization with viral HA of A/Goose/Guangdong/1/96 (H5N1), the immediate precursor of the current dominant strains of H5N1 viruses. The crystal structures of the Fab' fragment of H5M9 in complexes with H5 HAs of A/Vietnam/1203/2004 and A/Goose/Guangdong/1/96 reveal a conserved epitope in the HA1 vestigial esterase subdomain that is some distance from the receptor binding site and partially overlaps antigenic site C of H3 HA. Further epitope characterization by selection of escape mutants and epitope mapping by flow cytometry analysis of site-directed mutagenesis of HA with a yeast cell surface display identified four residues that are critical for H5M9 binding. D53, Y274, E83a, and N276 are all conserved in H5N1 HAs and are not in H5 epitopes identified by other mouse or human antibodies. Antibody H5M9 is effective in protection of H5N1 virus both prophylactically and therapeutically and appears to neutralize by blocking both virus receptor binding and postattachment steps. Thus, the H5M9 epitope identified here should provide valuable insights into H5N1 vaccine design and improvement, as well as antibody-based therapies for treatment of H5N1 infection.

Indexed as

Amino Acid SequenceAnimalsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralConserved SequenceCrystallizationEpitope MappingEpitopesHemagglutinin Glycoproteins, Influenza VirusHumansInfluenza A Virus, H5N1 SubtypeInfluenza, HumanMiceMice, Inbred BALB CModels, MolecularAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralEpitopesHemagglutinin Glycoproteins, Influenza Virus

Identifiers

PMID24049169
PMCPMC3838140
OpenAlexW1982842737

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.