ArticleNature communications2024
A single mutation in dairy cow-associated H5N1 viruses increases receptor binding breadth.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed.
- Diminished sialoside binding in novel H5N1 influenza hemagglutinin variants identified in a human patient.Nature communications · 2026Article
- In silico analysis of pH stabilising mutations of hemagglutinin of influenza A virus H5N1 clade 2.3.4.4b.Npj viruses · 2026Review
- Acquisition of specific human respiratory tract binding by 2.3.4.4b H5N1 hemagglutinins requires multiple mutations.Journal of virology · 2026Article
- What Antibody Repertoires See: Structural and Immunogenetic Insights Into Influenza A Virus Hemagglutinin Recognition.Immunological reviews · 2026Review
- Mammary Gland Tropism and Milk-Mediated Transmission of H5N1 in Dairy Cattle: Implications for One Health Surveillance.Veterinary sciences · 2026Review
- Standing HA phenotypic breadth shapes H5N1 cross-host potential.Research square · 2026Article
- Hemagglutinin double-mutation enhances binding of human-infecting avian influenza virus clade 2.3.4.4b H5Ny to human and SLeEMBO reports · 2026Article
- Receptor basis of unusual tissue tropism of avian influenza H5N1 clade 2.3.4.4b virus in cattle.Science advances · 2026Article
- Surveillance on California dairy farms reveals multiple possible sources of H5N1 influenza virus transmission.PLoS biology · 2026Article
- Primary bovine embryonic fibroblasts demonstrate variable fitness following infection with highly pathogenic avian influenza H5N1 strains and are susceptible to a recently circulating human 2009 pandemic lineage H1N1 strain.Microbiology spectrum · 2026Article
- The emergence and molecular evolution of H5N1 influenza viruses in United States dairy cattle.bioRxiv : the preprint server for biology · 2026Article
- Increased contact transmission of contemporary Human H5N1 compared to Bovine and Mountain Lion H5N1 in a hamster model.Nature communications · 2026Article
- Stabilization of the H5 clade 2.3.4.4b hemagglutinin improves vaccine-elicited neutralizing antibody responses in mice.Science translational medicine · 2026Article
- Evolution of H5N1 Cross-Species Transmission: Adaptive Mutations Driving Avian-to-Human Infection.Advanced genetics (Hoboken, N.J.) · 2026Article
- The bovine mammary gland as a crucible for zoonotic influenza virus emergence: Receptor-mediated adaptation of HPAI H5N1 clade 2.3.4.4b.Archives of virology · 2026Review
- Polymerase mutations underlie early adaptation of H5N1 influenza virus to dairy cattle and other mammals.Nature communications · 2026Article
- The receptor binding properties of H5Ny influenza A viruses have evolved to bind to avian-type mucin-like O-glycans.PLoS pathogens · 2026Article
- Contemporary Highly Pathogenic Avian Influenza (H5N1) Viruses Retain Neurotropism in Human Cerebral Organoids.Open forum infectious diseases · 2026Article
- Evolution, spread and impact of highly pathogenic H5 avian influenza A viruses.Nature reviews. Microbiology · 2026Review
- Influenza A Virus H5N1 Subtype: Resurgent Interspecies and Intercontinental Transmission, and a New Host.Pathogens (Basel, Switzerland) · 2025Review
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7 authors.
Funding
Abstract
Clade 2.3.4.4b H5N1 is causing an unprecedented outbreak in dairy cows in the United States. To understand if recent H5N1 viruses are changing their receptor use, we screened recombinant hemagglutinin (HA) from historical and recent 2.3.4.4b H5N1 viruses for binding to distinct glycans bearing terminal sialic acids using a glycan microarray. We find that H5 from A/Texas/37/2024, an isolate from the dairy cow outbreak, has increased binding breadth to core glycans bearing terminal α2,3 sialic acids, the avian receptor, compared to historical and recent 2.3.4.4b H5N1 viruses. We do not observe any binding to α2,6 sialic acids, the receptor used by human seasonal influenza viruses. Using molecular dynamics and a cryo-EM structure of A/Texas/37/2024 H5, we show A/Texas/37/2024 H5 is more flexible within the receptor-binding site compared to a 2.3.4.4b H5 from 2022. We identify a single mutation outside of the receptor binding site, T199I, is responsible for increased binding breadth, as it increases receptor binding site flexibility. Together, these data show recent H5N1 viruses are evolving increased receptor binding breadth which could impact the host range and cell types infected with H5N1.
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