ArticleBiochemical and biophysical research communications2011
Fine epitope mapping of monoclonal antibodies against hemagglutinin of a highly pathogenic H5N1 influenza virus using yeast surface display.
Article in Biochemical and biophysical research communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- Mapping hemagglutinin residues driving antigenic diversity in H5Nx avian influenza viruses.Journal of virology · 2026Article
- Article
- Epitope Mapping Using Yeast Display and Next Generation Sequencing.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Mammalian Antigen Display for Pandemic Countermeasures.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Hemagglutinin expressed by yeast reshapes immune microenvironment and gut microbiota to trigger diverse anti-infection response in infected birds.Frontiers in immunology · 2023Article
- Yeast Surface Display for Protein Engineering: Library Generation, Screening, and Affinity Maturation.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Effects of Size and Surface Properties of Nanodiamonds on the Immunogenicity of Plant-Based H5 Protein of A/H5N1 Virus in Mice.Nanomaterials (Basel, Switzerland) · 2021Article
- Structural and functional definition of a vulnerable site on the hemagglutinin of highly pathogenic avian influenza A virus H5N1.The Journal of biological chemistry · 2019Article
- Nanodiamond enhances immune responses in mice against recombinant HA/H7N9 protein.Journal of nanobiotechnology · 2017Article
- Article
- Yeast Surface-Displayed H5N1 Avian Influenza Vaccines.Journal of immunology research · 2016Article
- Applications of Yeast Surface Display for Protein Engineering.Methods in molecular biology (Clifton, N.J.) · 2015Review
- Malaria invasion ligand RH5 and its prime candidacy in blood-stage malaria vaccine design.Human vaccines & immunotherapeutics · 2015Review
- Article
- Review
- A unique and conserved neutralization epitope in H5N1 influenza viruses identified by an antibody against the A/Goose/Guangdong/1/96 hemagglutinin.Journal of virology · 2013Article
- Unraveling of a neutralization mechanism by two human antibodies against conserved epitopes in the globular head of H5 hemagglutinin.Journal of virology · 2013Article
- Identification and structural characterization of a broadly neutralizing antibody targeting a novel conserved epitope on the influenza virus H5N1 hemagglutinin.Journal of virology · 2013Article
- Rapid conformational epitope mapping of anti-gp120 antibodies with a designed mutant panel displayed on yeast.Journal of molecular biology · 2013Article
- A critical HA1 neutralizing domain of H5N1 influenza in an optimal conformation induces strong cross-protection.PloS one · 2013Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
Highly pathogenic H5N1 avian influenza viruses pose a debilitating pandemic threat. Thus, understanding mechanisms of antibody-mediated viral inhibition and neutralization escape is critical. Here, a robust yeast display system for fine epitope mapping of viral surface hemagglutinin (HA)-specific antibodies is demonstrated. The full-length H5 subtype HA (HA0) was expressed on the yeast surface in a correctly folded conformation, determined by binding of a panel of extensively characterized neutralizing human monoclonal antibodies (mAbs). These mAbs target conformationally-dependent epitopes of influenza A HA, which are highly conserved across H5 clades and group 1 serotypes. By separately displaying HA1 and HA2 subunits on yeast, domain mapping of two anti-H5 mAbs, NR2728 and H5-2A, localized their epitopes to HA1. These anti-H5 mAb epitopes were further fine mapped by using a library of yeast-displayed HA1 mutants and selecting for loss of binding without prior knowledge of potential contact residues. By overlaying key mutant residues that impacted binding onto a crystal structure of HA, the NR2728 mAb was found to interact with a fully surface-exposed contiguous patch of residues at the receptor binding site (RBS), giving insight into the mechanism underlying its potent inhibition of virus binding. The non-neutralizing H5-2A mAb was similarly mapped to a highly conserved H5 strain-specific but poorly accessible location on a loop at the trimer HA interface. These data further augment our toolchest for studying HA antigenicity, epitope diversity and accessibility in response to natural and experimental influenza infection 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.