ArticleNature communications2015
Comprehensive analysis of antibody recognition in convalescent humans from highly pathogenic avian influenza H5N1 infection.
Article in Nature communications, 2015. 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 34 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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Who cites it
34 citing papers in PubMed, 51 citations in OpenAlex.
- The DE and FG loops of the HPV major capsid protein contribute to the epitopes of vaccine-induced cross-neutralising antibodies.Scientific reports · 2016Trial
- What Antibody Repertoires See: Structural and Immunogenetic Insights Into Influenza A Virus Hemagglutinin Recognition.Immunological reviews · 2026Review
- Mapping of Phospholipase A2 Receptor Epitopes in Idiopathic Membranous Nephropathy and Clinical Relevance of Epitope Profiles.Journal of the American Society of Nephrology : JASN · 2026Article
- Dominant substitutions underlying the antigenic evolution of H5 influenza virus.Nature communications · 2025Article
- Cross-neutralizing and potent human monoclonal antibodies against historical and emerging H5Nx influenza viruses.Nature microbiology · 2025Article
- Conformational Variability Prediction of H5N1 Avian Influenza A Virus Hemagglutinins with Amino Acid Mutations Using SSSCPreds.ACS omega · 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
- Human naïve B cells recognize prepandemic influenza virus hemagglutinins.Science immunology · 2025Article
- Conformational Variability Prediction of Influenza Virus Hemagglutinins with Amino Acid Mutations Using Supersecondary Structure Code.Methods in molecular biology (Clifton, N.J.) · 2025Article
- AI-based antibody design targeting recent H5N1 avian influenza strains.Computational and structural biotechnology journal · 2025Article
- Identification of specific neutralizing antibodies for highly pathogenic avian influenza H5 2.3.4.4b clades to facilitate vaccine design and therapeutics.Emerging microbes & infections · 2024Article
- Analysis of the conserved protective epitopes of hemagglutinin on influenza A viruses.Frontiers in immunology · 2023Review
- Specific Monoclonal Antibodies Targeting Unique HA Epitopes Block H7N9 Influenza A Viral Replication.Journal of virology · 2022Article
- Identification of a cross-neutralizing antibody that targets the receptor binding site of H1N1 and H5N1 influenza viruses.Nature communications · 2022Article
- Designing a multi-epitope vaccine to provoke the robust immune response against influenza A H7N9.Scientific reports · 2021Article
- Development of molecular clamp stabilized hemagglutinin vaccines for Influenza A viruses.NPJ vaccines · 2021Article
- Polyclonal epitope mapping reveals temporal dynamics and diversity of human antibody responses to H5N1 vaccination.Cell reports · 2021Article
- Influenza Hemagglutinin Structures and Antibody Recognition.Cold Spring Harbor perspectives in medicine · 2020Review
- Article
- Structural and antigenic characterization of a computationally-optimized H5 hemagglutinin influenza vaccine.Vaccine · 2019Article
Corrections and comments
- Erratum issued
Authors and funding
17 authors at 7 institutions in 1 country.
Funding
Abstract
Understanding the mechanism of protective antibody recognition against highly pathogenic avian influenza A virus H5N1 in humans is critical for the development of effective therapies and vaccines. Here we report the crystal structure of three H5-specific human monoclonal antibodies bound to the globular head of hemagglutinin (HA) with distinct epitope specificities, neutralization potencies and breadth. A structural and functional analysis of these epitopes combined with those reported elsewhere identifies four major vulnerable sites on the globular head of H5N1 HA. Chimeric and vulnerable site-specific mutant pseudoviruses are generated to delineate broad neutralization specificities of convalescent sera from two individuals who recovered from the infection with H5N1 virus. Our results show that the four vulnerable sites on the globular head rather than the stem region are the major neutralizing targets, suggesting that during natural H5N1 infection neutralizing antibodies against the globular head work in concert to provide protective antibody-mediated immunity.
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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.