ArticleNature structural & molecular biology2013
A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin.
Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.
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Who cites it
105 citing papers in PubMed, 144 citations in OpenAlex.
- H7N9 influenza virus neutralizing antibodies that possess few somatic mutations.The Journal of clinical investigation · 2016Trial
- What Antibody Repertoires See: Structural and Immunogenetic Insights Into Influenza A Virus Hemagglutinin Recognition.Immunological reviews · 2026Review
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- Identification and characterization of a broadly neutralizing and protective nanobody against the HA1 domain of H5 avian influenza virus hemagglutinin.Journal of virology · 2025Article
- Structural basis of different neutralization capabilities of monoclonal antibodies against H7N9 virus.Journal of virology · 2025Article
- Clade 2.3.4.4b but not historical clade 1 HA replicating RNA vaccine protects against bovine H5N1 challenge in mice.Nature communications · 2025Article
- Functional and structural basis of human parainfluenza virus type 3 neutralization with human monoclonal antibodies.Nature microbiology · 2024Article
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- Antigen spacing on protein nanoparticles influences antibody responses to vaccination.Cell reports · 2023Article
- Characterization of non-neutralizing human monoclonal antibodies that target the M1 and NP of influenza A viruses.Journal of virology · 2023Article
- Stringent and complex sequence constraints of an IGHV1-69 broadly neutralizing antibody to influenza HA stem.Cell reports · 2023Article
- Highly Cross-Reactive and Protective Influenza A Virus H3N2 Hemagglutinin- and Neuraminidase-Specific Human Monoclonal Antibodies.Microbiology spectrum · 2023Article
- Signatures of VNature communications · 2023Article
- Mechanistic dissection of antibody inhibition of influenza entry yields unexpected heterogeneity.Biophysical journal · 2023Article
- Antigen spacing on protein nanoparticles influences antibody responses to vaccination.bioRxiv : the preprint server for biology · 2023Article
- Structural insights into the broad protection against H1 influenza viruses by a computationally optimized hemagglutinin vaccine.Communications biology · 2023Article
- The Trypanosoma cruzi Antigen and Epitope Atlas: antibody specificities in Chagas disease patients across the Americas.Nature communications · 2023Article
- Analysis of the conserved protective epitopes of hemagglutinin on influenza A viruses.Frontiers in immunology · 2023Review
- An epitope-enriched immunogen expands responses to a conserved viral site.Cell reports · 2022Article
45 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Influenza virus hemagglutinin (HA) mediates receptor binding and viral entry during influenza infection. The development of receptor analogs as viral-entry blockers has not been successful, which suggests that sialic acid may not be an ideal scaffold to obtain broad, potent HA inhibitors. Here, we report crystal structures of Fab fragments from three human antibodies that neutralize the 1957 pandemic H2N2 influenza virus in complex with H2 HA. All three antibodies use an aromatic residue to plug a conserved cavity in the HA receptor-binding site. Each antibody interacts with the absolutely conserved HA1 Trp153 at the cavity base through π-π stacking with the signature Phe54 of two VH1-69-encoded antibodies or a tyrosine from HCDR3 in the other antibody. This highly conserved interaction can be used as a starting point to design inhibitors targeting this conserved hydrophobic pocket in influenza 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.