ArticleCell2019
A Site of Vulnerability on the Influenza Virus Hemagglutinin Head Domain Trimer Interface.
Article in Cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 194 papers.
What it found
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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
194 citing papers in PubMed, 260 citations in OpenAlex.
- A chimeric hemagglutinin-based universal influenza virus vaccine approach induces broad and long-lasting immunity in a randomized, placebo-controlled phase I trial.Nature medicine · 2021Trial
- Some Exposure for Influenza Hemagglutinin Interface Antibodies.Immunological reviews · 2026Review
- What Antibody Repertoires See: Structural and Immunogenetic Insights Into Influenza A Virus Hemagglutinin Recognition.Immunological reviews · 2026Review
- An In Vitro Screen Identifies H1 Influenza Hemagglutinin Substitutions That Alter mRNA-LNP Vaccine Responses Against the Stalk Domain.Vaccines · 2026Article
- Single-component self-assembling protein nanoparticles displaying stabilized prefusion-closed hemagglutinin trimers for influenza vaccine development.Nature communications · 2026Article
- The Influenza-Specific Immunoglobulin Repertoire - Nimble Yet Steeped in Tradition.Immunological reviews · 2026Review
- Article
- Counteracting Influenza Virus Evolution Through the Full Spectrum of Broadly Protective Antibodies.Immunological reviews · 2026Review
- Pre-existing hemagglutinin-specific antibody levels are associated with B-cell repertoire maturation and antibody breadth after influenza vaccination.Virologica Sinica · 2026Article
- A neutralizing nanobody targeting a conserved lateral patch on HA1 confers protection against multiple H7 avian influenza viruses.Journal of virology · 2026Article
- Stabilized mosaic hemagglutinin immunogens as novel universal influenza virus vaccines.Molecular therapy : the journal of the American Society of Gene Therapy · 2026Article
- Preexisting IgG forms immune complexes and links local thermal reactogenicity with immunogenicity in influenza vaccination.NPJ vaccines · 2026Article
- Article
- Structural vaccinology expedites rational design of next-generation vaccines for influenza and respiratory syncytial virus.Virologica Sinica · 2026Review
- Impact of cellular proteases on the function of antiviral antibodies.Journal of virology · 2026Review
- Stabilization of the H5 clade 2.3.4.4b hemagglutinin improves vaccine-elicited neutralizing antibody responses in mice.Science translational medicine · 2026Article
- 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
- Probing the role of membrane in neutralizing activity of antibodies against influenza virus.Structure (London, England : 1993) · 2026Article
134 more citing papers are in PubMed but not listed here.
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Authors and funding
17 authors at 6 institutions in 2 countries.
Funding
Abstract
Here, we describe the discovery of a naturally occurring human antibody (Ab), FluA-20, that recognizes a new site of vulnerability on the hemagglutinin (HA) head domain and reacts with most influenza A viruses. Structural characterization of FluA-20 with H1 and H3 head domains revealed a novel epitope in the HA trimer interface, suggesting previously unrecognized dynamic features of the trimeric HA protein. The critical HA residues recognized by FluA-20 remain conserved across most subtypes of influenza A viruses, which explains the Ab's extraordinary breadth. The Ab rapidly disrupted the integrity of HA protein trimers, inhibited cell-to-cell spread of virus in culture, and protected mice against challenge with viruses of H1N1, H3N2, H5N1, or H7N9 subtypes when used as prophylaxis or therapy. The FluA-20 Ab has uncovered an exceedingly conserved protective determinant in the influenza HA head domain trimer interface that is an unexpected new target for anti-influenza therapeutics and vaccines.
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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.