ArticleNature communications2024
Epistasis mediates the evolution of the receptor binding mode in recent human H3N2 hemagglutinin.
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 22 papers.
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Who cites it
22 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
- Epistasis facilitates the long-term antigenic evolution of the influenza B virus hemagglutinin.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
- Isolation and characterization of a novel reassortant H3N8 avian influenza virus from chickens in Eastern China.Virus genes · 2026Article
- Molecular Characterization of an H3N2 Canine Influenza Virus Isolated from a Dog in Jiangsu, China, in 2025.Veterinary sciences · 2025Article
- Construction and Research Progress of Animal Models and Mouse Adapted Strains of Seasonal Influenza Virus.Vaccines · 2025Review
- Pleiotropic mutational effects on function and stability constrain the antigenic evolution of influenza hemagglutinin.bioRxiv : the preprint server for biology · 2025Article
- Neutralizing Antibodies vs. Viruses: Interacting Mechanisms and Escape Tactics.Microorganisms · 2025Review
- Review
- Epistasis in the receptor-binding domain of contemporary H3N2 viruses that reverted to bind sialylated di-LacNAc repeats.Cell reports · 2025Article
- Structural and functional insights into the evolution of SARS-CoV-2 KP.3.1.1 spike protein.Cell reports · 2025Article
- Deep mutational scanning of rabies glycoprotein defines mutational constraint and antibody-escape mutations.Cell host & microbe · 2025Article
- Strategies and efforts in circumventing the emergence of antiviral resistance against conventional antivirals.npj antimicrobials and resistance · 2025Review
- Analysis of Epidemiological and Evolutionary Characteristics of Seasonal Influenza Viruses in Shenzhen City from 2018 to 2024.Viruses · 2025Article
- Article
- Structural and Functional Insights into the Evolution of SARS-CoV-2 KP.3.1.1 Spike Protein.bioRxiv : the preprint server for biology · 2024Article
- A single mutation in bovine influenza H5N1 hemagglutinin switches specificity to human receptors.Science (New York, N.Y.) · 2024Article
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Authors and funding
19 authors.
Funding
Abstract
The receptor-binding site of influenza A virus hemagglutinin partially overlaps with major antigenic sites and constantly evolves. In this study, we observe that mutations G186D and D190N in the hemagglutinin receptor-binding site have coevolved in two recent human H3N2 clades. X-ray crystallography results show that these mutations coordinately drive the evolution of the hemagglutinin receptor binding mode. Epistasis between G186D and D190N is further demonstrated by glycan binding and thermostability analyses. Immunization and neutralization experiments using mouse and human samples indicate that the evolution of receptor binding mode is accompanied by a change in antigenicity. Besides, combinatorial mutagenesis reveals that G186D and D190N, along with other natural mutations in recent H3N2 strains, alter the compatibility with a common egg-adaptive mutation in seasonal influenza vaccines. Overall, our findings elucidate the role of epistasis in shaping the recent evolution of human H3N2 hemagglutinin and substantiate the high evolvability of its receptor-binding mode.
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