ArticleCell reports2015
Structural Basis for a Switch in Receptor Binding Specificity of Two H5N1 Hemagglutinin Mutants.
Article in Cell reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 34 citations in OpenAlex.
- Acquisition of specific human respiratory tract binding by 2.3.4.4b H5N1 hemagglutinins requires multiple mutations.Journal of virology · 2026Article
- Intra-patient neuraminidase mutations in avian H5N1 influenza virus reduce sialidase activity to complement weaker hemagglutinin binding and facilitate human infection.PLoS pathogens · 2026Article
- The receptor binding properties of H5Ny influenza A viruses have evolved to bind to avian-type mucin-like O-glycans.PLoS pathogens · 2026Article
- Host switching mutations in H5N1 influenza hemagglutinin suppress site-specific activation dynamics.Nature communications · 2025Article
- Reassortment of newly emergent clade 2.3.4.4b A(H5N1) highly pathogenic avian influenza A viruses in Bangladesh.Emerging microbes & infections · 2025Article
- Host Switching Mutations in H5N1 Influenza Hemagglutinin Suppress Site-specific Activation Dynamics.bioRxiv : the preprint server for biology · 2025Article
- The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.bioRxiv : the preprint server for biology · 2025Article
- A single mutation in bovine influenza H5N1 hemagglutinin switches specificity to human receptors.Science (New York, N.Y.) · 2024Article
- Multivalent interactions between fully glycosylated influenza virus hemagglutinins mediated by glycans at distinct N-glycosylation sites.Npj viruses · 2024Article
- Molecular Markers and Mechanisms of Influenza A Virus Cross-Species Transmission and New Host Adaptation.Viruses · 2024Review
- Pathogenicity and virulence of influenza.Virulence · 2023Review
- Molecular epidemiology and pathogenicity of H5N1 and H9N2 avian influenza viruses in clinically affected chickens on farms in Bangladesh.Emerging microbes & infections · 2021Article
- Amino acid substitutions in the H5N1 avian influenza haemagglutinin alter pH of fusion and receptor binding to promote a highly pathogenic phenotype in chickens.The Journal of general virology · 2021Article
- Review
- Glycomics and glycoproteomics of viruses: Mass spectrometry applications and insights toward structure-function relationships.Mass spectrometry reviews · 2020Review
- Phenotypic Effects of Substitutions within the Receptor Binding Site of Highly Pathogenic Avian Influenza H5N1 Virus Observed during Human Infection.Journal of virology · 2020Article
- Molecular Docking of Broad-Spectrum Antibodies on Hemagglutinins of Influenza A Virus.Evolutionary bioinformatics online · 2019Article
- The structural variability of the influenza A hemagglutinin receptor-binding site.Briefings in functional genomics · 2018Review
- Direct Visualization of the Conformational Dynamics of Single Influenza Hemagglutinin Trimers.Cell · 2018Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Avian H5N1 influenza viruses continue to spread in wild birds and domestic poultry with sporadic infection in humans. Receptor binding specificity changes are a prerequisite for H5N1 viruses and other zoonotic viruses to be transmitted among humans. Previous reported hemagglutinin (HA) mutants from ferret-transmissible H5N1 viruses of A/Vietnam/1203/2004 and A/Indonesia/5/2005 showed slightly increased, but still very weak, binding to human receptors. From mutagenesis and glycan array studies, we previously identified two H5N1 HA mutants that could more effectively switch receptor specificity to human-like α2-6-linked sialosides with avidity comparable to wild-type H5 HA binding to avian-like α2-3-linked sialosides. Here, crystal structures of these two H5 HA mutants free and in complex with human and avian glycan receptor analogs reveal the structural basis for their preferential binding to human receptors. These findings suggest continuous surveillance should be maintained to monitor and assess human-to-human transmission potential of H5N1 viruses.
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