ArticleProceedings of the National Academy of Sciences of the United States of America2015
Structures of complexes formed by H5 influenza hemagglutinin with a potent broadly neutralizing human monoclonal antibody.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 53 citations in OpenAlex.
- 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
- Dairy cattle herds mount a characteristic antibody response to highly pathogenic H5N1 avian influenza viruses.Journal of virology · 2025Article
- A replicating recombinant vesicular stomatitis virus model for dairy cattle H5N1 influenza virus glycoprotein evolution.Journal of virology · 2025Article
- Pan-H7 influenza human antibody virus neutralization depends on avidity and steric hindrance.JCI insight · 2025Article
- Identification and characterization of a broadly neutralizing and protective nanobody against the HA1 domain of H5 avian influenza virus hemagglutinin.Journal of virology · 2025Article
- A replicating recombinant vesicular stomatitis virus model for dairy cattle H5N1 influenza virus glycoprotein evolution.bioRxiv : the preprint server for biology · 2025Article
- Structural basis of different neutralization capabilities of monoclonal antibodies against H7N9 virus.Journal of virology · 2025Article
- AI-based antibody design targeting recent H5N1 avian influenza strains.Computational and structural biotechnology journal · 2025Article
- Epitopes in the HA and NA of H5 and H7 avian influenza viruses that are important for antigenic drift.FEMS microbiology reviews · 2024Review
- Antibody inhibition of influenza A virus assembly and release.Journal of virology · 2024Article
- Structure of an influenza group 2-neutralizing antibody targeting the hemagglutinin stem supersite.Structure (London, England : 1993) · 2022Article
- Hemagglutinin Structure and Activities.Cold Spring Harbor perspectives in medicine · 2021Review
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- Antibody heavy chain CDR3 length-dependent usage of human IGHJ4 and IGHJ6 germline genes.Antibody therapeutics · 2021Article
- Characterization of Novel Cross-Reactive Influenza B Virus Hemagglutinin Head Specific Antibodies That Lack Hemagglutination Inhibition Activity.Journal of virology · 2020Article
- Structural intermediates in the low pH-induced transition of influenza hemagglutinin.PLoS pathogens · 2020Article
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- Article
- Structural and antigenic characterization of a computationally-optimized H5 hemagglutinin influenza vaccine.Vaccine · 2019Article
- Article
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Authors and funding
18 authors at 6 institutions in 4 countries.
Funding
Abstract
H5N1 avian influenza viruses remain a threat to public health mainly because they can cause severe infections in humans. These viruses are widespread in birds, and they vary in antigenicity forming three major clades and numerous antigenic variants. The most important features of the human monoclonal antibody FLD194 studied here are its broad specificity for all major clades of H5 influenza HAs, its high affinity, and its ability to block virus infection, in vitro and in vivo. As a consequence, this antibody may be suitable for anti-H5 therapy and as a component of stockpiles, together with other antiviral agents, for health authorities to use if an appropriate vaccine was not available. Our mutation and structural analyses indicate that the antibody recognizes a relatively conserved site near the membrane distal tip of HA, near to, but distinct from, the receptor-binding site. Our analyses also suggest that the mechanism of infectivity neutralization involves prevention of receptor recognition as a result of steric hindrance by the Fc part of the antibody. Structural analyses by EM indicate that three Fab fragments are bound to each HA trimer. The structure revealed by X-ray crystallography is of an HA monomer bound by one Fab. The monomer has some similarities to HA in the fusion pH conformation, and the monomer's formation, which results from the presence of isopropanol in the crystallization solvent, contributes to considerations of the process of change in conformation required for membrane fusion.
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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.