ArticleProceedings of the National Academy of Sciences of the United States of America2011
Broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutinin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 343 papers.
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Who cites it
343 citing papers in PubMed.
- Antibody Fc effector functions and IgG3 associate with decreased HIV-1 risk.The Journal of clinical investigation · 2019Trial
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- What Antibody Repertoires See: Structural and Immunogenetic Insights Into Influenza A Virus Hemagglutinin Recognition.Immunological reviews · 2026Review
- Counteracting Influenza Virus Evolution Through the Full Spectrum of Broadly Protective Antibodies.Immunological reviews · 2026Review
- Optimizing an avian influenza vaccine using a novel Bacterial Enzymatic Combinatorial Chemistry (BECC) TLR4 adjuvant.mSphere · 2026Article
- Germinal center-independent memory B cells provide rapid protection from lethal influenza challenges.bioRxiv : the preprint server for biology · 2026Article
- Elicitation of stem-directed antibodies in rhesus macaques by a conventional hemagglutinin immunogen.bioRxiv : the preprint server for biology · 2026Article
- Mechanistic and antigenic boundaries of Henipavirus and Parahenipavirus glycoproteins.Nature communications · 2026Article
- Review
- Coordinated immune response distinguishes duration of SARS-CoV-2 viral particle shedding in humans.iScience · 2026Article
- DNA origami vaccine nanoparticles improve humoral and cellular immune responses to infectious diseases.Nature biomedical engineering · 2026Article
- Affinity maturation and light-chain-mediated paratope diversification anticipates viral evolution.Cell reports · 2026Article
- Presentation of hemagglutinin on adjuvant-bearing self-assembling peptide nanofibers increases heterologous responses against influenza.Acta biomaterialia · 2026Article
- A single mutation at position 214 of influenza B hemagglutinin enhances cross-neutralization.Emerging microbes & infections · 2025Article
- Structural basis for a potent human neutralizing antibody targeting a conserved epitope on the H7 hemagglutinin head.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Consensus-Guided Construction of H5N1-Specific and Universal Influenza a Multiepitope Vaccines.Biology · 2025Article
- Transient regulatory T cell manipulation is limited by anti-antibody responses in HIV-1 envelope immunized rhesus macaques.iScience · 2025Article
283 more citing papers are in PubMed but not listed here.
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Authors and funding
13 authors.
Funding
Abstract
Seasonal antigenic drift of circulating influenza virus leads to a requirement for frequent changes in vaccine composition, because exposure or vaccination elicits human antibodies with limited cross-neutralization of drifted strains. We describe a human monoclonal antibody, CH65, obtained by isolating rearranged heavy- and light-chain genes from sorted single plasma cells, coming from a subject immunized with the 2007 trivalent influenza vaccine. The crystal structure of a complex of the hemagglutinin (HA) from H1N1 strain A/Solomon Islands/3/2006 with the Fab of CH65 shows that the tip of the CH65 heavy-chain complementarity determining region 3 (CDR3) inserts into the receptor binding pocket on HA1, mimicking in many respects the interaction of the physiological receptor, sialic acid. CH65 neutralizes infectivity of 30 out of 36 H1N1 strains tested. The resistant strains have a single-residue insertion near the rim of the sialic-acid pocket. We conclude that broad neutralization of influenza virus can be achieved by antibodies with contacts that mimic those of the receptor.
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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.