ArticleThe Journal of clinical investigation2021
Canonical features of human antibodies recognizing the influenza hemagglutinin trimer interface.
Article in The Journal of clinical investigation, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 32 papers.
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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.
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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.
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Who cites it
32 citing papers in PubMed, 41 citations in OpenAlex.
- Some Exposure for Influenza Hemagglutinin Interface Antibodies.Immunological reviews · 2026Review
- The Influenza-Specific Immunoglobulin Repertoire - Nimble Yet Steeped in Tradition.Immunological reviews · 2026Review
- Counteracting Influenza Virus Evolution Through the Full Spectrum of Broadly Protective Antibodies.Immunological reviews · 2026Review
- MAAD: multidimensional antiviral antibody database.Protein & cell · 2026Article
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- Panzootic H5 influenza viruses acquired resistance to human head interface antibodies.PLoS pathogens · 2026Article
- Pleiotropic mutational effects on function and stability constrain the antigenic evolution of influenza haemagglutinin.Nature ecology & evolution · 2026Article
- Development of a potent monoclonal antibody for treatment of human metapneumovirus infections.Nature communications · 2026Article
- A protective and heterosubtypic antibody lineage targeting the influenza A virus neuraminidase active site.The Journal of clinical investigation · 2025Article
- Human coronavirus HKU1 neutralization by glycan receptor mimicry.bioRxiv : the preprint server for biology · 2025Article
- Iterative immunogen optimization to focus immune responses on a conserved, subdominant viral epitope.bioRxiv : the preprint server for biology · 2025Article
- Pleiotropic mutational effects on function and stability constrain the antigenic evolution of influenza hemagglutinin.bioRxiv : the preprint server for biology · 2025Article
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- Use of equine H3N8 hemagglutinin as a broadly protective influenza vaccine immunogen.NPJ vaccines · 2024Article
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- Potent HPIV3-neutralizing IGHV5-51 Antibodies Identified from Multiple Individuals Show L Chain and CDRH3 Promiscuity.Journal of immunology (Baltimore, Md. : 1950) · 2024Article
- Antigen spacing on protein nanoparticles influences antibody responses to vaccination.Cell reports · 2023Article
- Structural basis for cross-group recognition of an influenza virus hemagglutinin antibody that targets postfusion stabilized epitope.PLoS pathogens · 2023Article
Corrections and comments
- Erratum issued
Authors and funding
21 authors at 4 institutions in 1 country.
Funding
Abstract
Broadly reactive antibodies targeting the influenza A virus hemagglutinin (HA) head domain are thought to be rare and to require extensive somatic mutations or unusual structural features to achieve breadth against divergent HA subtypes. Here we describe common genetic and structural features of protective human antibodies from several individuals recognizing the trimer interface (TI) of the influenza A HA head, a recently identified site of vulnerability. We examined the sequence of TI-reactive antibodies, determined crystal structures for TI antibody-antigen complexes, and analyzed the contact residues of the antibodies on HA to discover common genetic and structural features of TI antibodies. Our data reveal that many TI antibodies are encoded by a light chain variable gene segment incorporating a shared somatic mutation. In addition, these antibodies have a shared acidic residue in the heavy chain despite originating from diverse heavy chain variable gene segments. These studies show that the TI region of influenza A HA is a major antigenic site with conserved structural features that are recognized by a common human B cell public clonotype. The canonical nature of this antibody-antigen interaction suggests that the TI epitope might serve as an important target for structure-based vaccine design.
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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.