ArticleCell reports2025
Epistasis in the receptor-binding domain of contemporary H3N2 viruses that reverted to bind sialylated di-LacNAc repeats.
Article in Cell reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Diminished sialoside binding in novel H5N1 influenza hemagglutinin variants identified in a human patient.Nature communications · 2026Article
- Acquisition of specific human respiratory tract binding by 2.3.4.4b H5N1 hemagglutinins requires multiple mutations.Journal of virology · 2026Article
- Targeting virus-glycan recognition in influenza viruses and coronaviruses: from the molecular principles to glycomimetic antivirals strategies.RSC chemical biology · 2026Review
- Molecular Characterization of Influenza A(H3N2) Hemagglutinin Variants Circulating in Western Mexico, 2022.International journal of molecular sciences · 2026Article
- Loss of hemagglutination ability by H3N2 influenza A virus, subclade K.bioRxiv : the preprint server for biology · 2026Article
- Predicting the antigenic evolution of seasonal influenza viruses using phylogenetic convergence.bioRxiv : the preprint server for biology · 2026Article
- Pleiotropic mutational effects on function and stability constrain the antigenic evolution of influenza haemagglutinin.Nature ecology & evolution · 2026Article
- Learning a viral protein's vocabulary.Nature ecology & evolution · 2026Article
- The receptor binding properties of H5Ny influenza A viruses have evolved to bind to avian-type mucin-like O-glycans.PLoS pathogens · 2026Article
- Pleiotropic mutational effects on function and stability constrain the antigenic evolution of influenza hemagglutinin.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
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Abstract
Since their introduction into humans, H3N2 influenza A viruses have evolved continuously to escape immunity through antigenic drift, driven by mutations in and around the receptor-binding site. Recently, these changes resulted in viruses that recognize elongated glycans, which are less abundant in the human respiratory tract, complicating vaccine strain propagation. This study employed ELISA, glycan arrays, tissue staining, flow cytometry, and hemagglutinin (HA) assays to demonstrate the molecular determinants of recent H3N2 viruses that regained recognition of shorter glycans. Mutations Y159N/T160I in contemporary strains replace Y159/T160, weakening receptor binding. However, this is compensated by Y195F in the 190-helix. These findings highlight epistasis across critical residues in the HA receptor-binding site, including the 130-loop, 150-loop, and 190-helix. Interestingly, a positive correlation exists between binding to an asymmetrical N-glycan and binding to human and ferret respiratory tract tissues. These results elucidate the epistatic nature of receptor-binding specificity during influenza A virus H3N2 evolution.
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