ArticleProceedings of the National Academy of Sciences of the United States of America2014
A common solution to group 2 influenza virus neutralization.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers.
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Who cites it
126 citing papers in PubMed.
- What Antibody Repertoires See: Structural and Immunogenetic Insights Into Influenza A Virus Hemagglutinin Recognition.Immunological reviews · 2026Review
- Structural basis for distinct protective mechanisms of IGHV3-23 antibodies targeting influenza hemagglutinin stem.Nature communications · 2026Article
- Article
- Characterization of two non-competing antibodies to influenza H3N2 hemagglutinin stem reveals its evolving antigenicity.Nature communications · 2025Article
- Molecular divergence and convergence of mammalian antibody responses to the influenza virus hemagglutinin stem.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Assessing the structural boundaries of broadly reactive antibody interactions with diverse H3 influenza hemagglutinin proteins.Journal of virology · 2025Article
- Passive Immunization in the Prevention and Treatment of Viral Infections.European journal of immunology · 2025Review
- Conserved sites on the influenza H1 and H3 hemagglutinin recognized by human antibodies.Science advances · 2025Article
- Disease diagnostics using machine learning of B cell and T cell receptor sequences.Science (New York, N.Y.) · 2025Article
- How Broadly Neutralising Antibodies Are Redefining Immunity to Influenza.Antibodies (Basel, Switzerland) · 2025Review
- An explainable language model for antibody specificity prediction using curated influenza hemagglutinin antibodies.Immunity · 2024Article
- Human neutralizing antibodies target a conserved lateral patch on H7N9 hemagglutinin head.Nature communications · 2024Article
- VarEPS-Influ:an risk evaluation system of occurred and virtual variations of influenza virus genomes.Nucleic acids research · 2024Article
- Protective human antibodies against a conserved epitope in pre- and postfusion influenza hemagglutinin.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- An explainable language model for antibody specificity prediction using curated influenza hemagglutinin antibodies.bioRxiv : the preprint server for biology · 2023Article
- Antigenic Landscape Analysis of Individuals Vaccinated with a Universal Influenza Virus Vaccine Candidate Reveals Induction of Cross-Subtype Immunity.Journal of virology · 2023Article
- Analysis of the conserved protective epitopes of hemagglutinin on influenza A viruses.Frontiers in immunology · 2023Review
- Article
- Structural basis for a human broadly neutralizing influenza A hemagglutinin stem-specific antibody including H17/18 subtypes.Nature communications · 2022Article
- Universal antibody targeting the highly conserved fusion peptide provides cross-protection in mice.Human vaccines & immunotherapeutics · 2022Article
66 more citing papers are in PubMed but not listed here.
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Authors and funding
23 authors.
Funding
Abstract
The discovery and characterization of broadly neutralizing antibodies (bnAbs) against influenza viruses have raised hopes for the development of monoclonal antibody (mAb)-based immunotherapy and the design of universal influenza vaccines. Only one human bnAb (CR8020) specifically recognizing group 2 influenza A viruses has been previously characterized that binds to a highly conserved epitope at the base of the hemagglutinin (HA) stem and has neutralizing activity against H3, H7, and H10 viruses. Here, we report a second group 2 bnAb, CR8043, which was derived from a different germ-line gene encoding a highly divergent amino acid sequence. CR8043 has in vitro neutralizing activity against H3 and H10 viruses and protects mice against challenge with a lethal dose of H3N2 and H7N7 viruses. The crystal structure and EM reconstructions of the CR8043-H3 HA complex revealed that CR8043 binds to a site similar to the CR8020 epitope but uses an alternative angle of approach and a distinct set of interactions. The identification of another antibody against the group 2 stem epitope suggests that this conserved site of vulnerability has great potential for design of therapeutics and vaccines.
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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.