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Article

Epistasis mediates the evolution of the receptor binding mode in recent human H3N2 hemagglutinin.

Nature communications - 18 Jun 2024

Lei Ruipeng, Liang Weiwen, Ouyang Wenhao O, Hernandez Garcia Andrea, Kikuchi Chika, Wang Shengyang, McBride Ryan, Tan Timothy J C, Sun Yuanxin, Chen Chunke, Graham Claire S, Rodriguez Lucia A, Shen Ivana R, Choi Danbi, Bruzzone Roberto, Paulson James C, Nair Satish K, Mok Chris K P, Wu Nicholas C

Abstract excerpt

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....

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Share to Crystallography, X-Ray
Share to Epistasis, Genetic

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Evolution, Molecular

Share to Hemagglutinin Glycoproteins, Influenza Virus

Share to Influenza A Virus, H3N2 Subtype

Share to Influenza, Human

Share to Influenza Vaccines

Share to Receptors, Virus

Source

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Identifiers

PMID: 38890325
DOI: 10.1038/s41467-024-49487-4
PMCID: PMC11189414

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

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