ArticleNature communications2025
Characterization of two non-competing antibodies to influenza H3N2 hemagglutinin stem reveals its evolving antigenicity.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- What Antibody Repertoires See: Structural and Immunogenetic Insights Into Influenza A Virus Hemagglutinin Recognition.Immunological reviews · 2026Review
- The Influenza-Specific Immunoglobulin Repertoire - Nimble Yet Steeped in Tradition.Immunological reviews · 2026Review
- From Phage Display to Yeast Secretion: Developing Fc-Fused Nanobodies Against Influenza Virus.Cells · 2026Article
- Structural insights into antibody responses against influenza A virus in its natural reservoir.bioRxiv : the preprint server for biology · 2026Article
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10 authors.
Funding
Abstract
The conserved stem domain of influenza hemagglutinin (HA), which is classified into group 1 and group 2, is a target of broadly neutralizing antibodies. While many group 1 HA stem antibodies have been described, much less is known about group 2 HA stem antibodies. This study structurally characterizes two group 2 HA stem antibodies, 2F02 and AG2-G02, targeting the central stem epitope and the lower stem epitope, respectively. Unlike prototypic antibodies to group 2 HA stem, 2F02 and AG2-G02 do not compete for binding. Both antibodies offer protection in a female mouse model via neutralization activity and Fc-mediated effector functions. We further demonstrate that the natural evolution of HA2 position 32 restricts the binding of AG2-G02 to recent human H3N2 HAs and influences the binding of human plasma samples. Overall, these findings advance our understanding of the antigenicity of HA stem, which has important implications for the development of broadly protective influenza vaccines.
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