ArticleNature communications2025
Structural and immunological characterization of the H3 influenza hemagglutinin during antigenic drift.
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 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed.
- Comparative Immunogenicity of Inactivated H7N9 Avian Influenza Vaccines with Different Internal Gene Backbones.Microorganisms · 2026Article
- Towards spatial lipid profiling by using mass spectrometry: analytical challenges and applications.Analytical and bioanalytical chemistry · 2026Review
- Structural insights into antibody responses against influenza A virus in its natural reservoir.bioRxiv : the preprint server for biology · 2026Article
- Mapping the specificity of H3N2 strain-specific and cross-reactive human neutralizing antibodies elicited by the 2025-2026 influenza vaccine.medRxiv : the preprint server for health sciences · 2026Article
- First detection and transatlantic introduction of Influenza A(H3N2) subclade K (J.2.4.1) into Ecuador: insights from genomic sentinel surveillance.Frontiers in public health · 2026Article
Corrections and comments
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Authors and funding
19 authors.
Funding
Abstract
The quest for a universal influenza vaccine holds great promise for mitigating the global burden of influenza-related morbidity and mortality. However, challenges persist in identifying conserved epitopes capable of eliciting robust and durable immune responses. In this study, we explore the influence of glycan evolution on H3 hemagglutinin from 1968 to present day and its impacts on protein structure, antigenicity and immunogenicity by using computational, biochemical and biophysical techniques. Structural characterization of HK/68 and Sing/16 by cryo-electron microscopy shows that while HK/68 is resistant to enzymatic deglycosylation, removal of glycans destabilizes the hyperglycosylated head and membrane-proximal region in Sing/16. Furthermore, the appearance of glycans in Sing/16 hemagglutinin head domain shifts the polyclonal immune response upon vaccination to target the esterase and stem. These insights expand our understanding of glycans beyond their role in protein folding and highlight the interplay among glycan integration and immune recognition to design a universal influenza vaccine.
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Registered trials
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