ArticleStructure (London, England : 1993)2024
Structural basis for the broad antigenicity of the computationally optimized influenza hemagglutinin X6.
Article in Structure (London, England : 1993), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Nanoemulsion adjuvanted COBRA HA vaccine enhances protective antibody titers against H1N1 and H3N2 influenza viruses.Human vaccines & immunotherapeutics · 2026Article
- What Antibody Repertoires See: Structural and Immunogenetic Insights Into Influenza A Virus Hemagglutinin Recognition.Immunological reviews · 2026Review
- Structural vaccinology expedites rational design of next-generation vaccines for influenza and respiratory syncytial virus.Virologica Sinica · 2026Review
- Age-dependent immune landscapes affect influenza vaccine effectiveness and guide precision strategies.Frontiers in immunology · 2026Review
- Leveraging large language models to predict antibody biological activity against influenza A hemagglutinin.Computational and structural biotechnology journal · 2025Article
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Authors and funding
9 authors.
Funding
Abstract
Influenza causes significant morbidity and mortality. As an alternative approach to current seasonal vaccines, the computationally optimized broadly reactive antigen (COBRA) platform has been previously applied to hemagglutinin (HA). This approach integrates wild-type HA sequences into a single immunogen to expand the breadth of accessible antibody epitopes. Adding to previous studies of H1, H3, and H5 COBRA HAs, we define the structural features of another H1 subtype COBRA, X6, that incorporates HA sequences from before and after the 2009 H1N1 influenza pandemic. We determined structures of this antigen alone and in complex with COBRA-specific as well as broadly reactive and functional antibodies, analyzing its antigenicity. We found that X6 possesses features representing both historic and recent H1 HA strains, enabling binding to both head- and stem-reactive antibodies. Overall, these data confirm the integrity of broadly reactive antibody epitopes of X6 and contribute to design efforts for a next-generation vaccine.
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