ArticleJournal of virology2018
Structural Basis for the Broad, Antibody-Mediated Neutralization of H5N1 Influenza Virus.
Article in Journal of virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 20 citations in OpenAlex.
- Advances and challenges in avian influenza vaccines: From conventional approaches to next-generation strategies.Veterinary and animal science · 2026Review
- Molecular detection of coronavirus in wild birds from Lima, Peru.Veterinary research communications · 2026Article
- Coronaviruses in diarrheic pigeons and the first determination of the complete genome of a new pigeon gammacoronavirus.Scientific reports · 2025Article
- Identification and characterization of a broadly neutralizing and protective nanobody against the HA1 domain of H5 avian influenza virus hemagglutinin.Journal of virology · 2025Article
- Structure-based Design of Chimeric Influenza Hemagglutinins to Elicit Cross-group Immunity.bioRxiv : the preprint server for biology · 2025Article
- Human naïve B cells recognize prepandemic influenza virus hemagglutinins.Science immunology · 2025Article
- How Broadly Neutralising Antibodies Are Redefining Immunity to Influenza.Antibodies (Basel, Switzerland) · 2025Review
- AI-based antibody design targeting recent H5N1 avian influenza strains.Computational and structural biotechnology journal · 2025Article
- Gulls as a host for both gamma and deltacoronaviruses.Scientific reports · 2023Article
- Analysis of the conserved protective epitopes of hemagglutinin on influenza A viruses.Frontiers in immunology · 2023Review
- Identification of a cross-neutralizing antibody that targets the receptor binding site of H1N1 and H5N1 influenza viruses.Nature communications · 2022Article
- Review
- A stepwise docking molecular dynamics approach for simulating antibody recognition with substantial conformational changes.Computational and structural biotechnology journal · 2022Article
- Identification of Hemagglutinin Mutations Caused by Neuraminidase Antibody Pressure.Microbiology spectrum · 2021Article
- An expanded benchmark for antibody-antigen docking and affinity prediction reveals insights into antibody recognition determinants.Structure (London, England : 1993) · 2021Article
- An IgM antibody targeting the receptor binding site of influenza B blocks viral infection with great breadth and potency.Theranostics · 2019Article
Corrections and comments
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Authors and funding
18 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human infection with highly pathogenic avian influenza A viruses causes severe disease and fatalities. We previously identified a potent and broadly neutralizing antibody (bnAb), 13D4, against the H5N1 virus. Here, we report the co-crystal structure of 13D4 in complex with the hemagglutinin (HA) of A/Vietnam/1194/2004 (H5N1). We show that heavy-chain complementarity-determining region 3 (HCDR3) of 13D4 confers broad yet specific neutralization against H5N1, undergoing conformational rearrangement to bind to the receptor binding site (RBS). Further, we show that mutating four critical residues within the RBS-Trp153, Lys156, Lys193, and Leu194-disrupts the binding between 13D4 and HA. Viruses bearing Asn193 instead of Lys/Arg can evade 13D4 neutralization, indicating that Lys193 polymorphism might be, at least in part, involved in the antigenicity of recent H5 genotypes (such as H5N6 and H5N8) as distinguished from H5N1. BnAb 13D4 may offers a template for therapeutic RBS inhibitor design and serve as an indicator of antigenic change for current H5 viruses.
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Registered trials
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.