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TitleStructural and immunological characterization of the H3 influenza hemagglutinin during antigenic drift.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 11452, Year 2025
Publish dateDec 11, 2025
AuthorsRebeca de Paiva Froes Rocha / Ilhan Tomris / Charles A Bowman / Emma Stevens / Jason Kantorow / Corinna M Plitt / Weiwei Peng / Svearike Oeverdieck / Thales Galdino Andrade / James A Ferguson / Diana D Jung / Rafael Elias Marques / Sander Herfst / Joost Snijder / Srirupa Chakraborty / Alba Torrents de la Peña / Zachary T Berndsen / Robert P de Vries / Andrew B Ward /
PubMed AbstractThe 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 ...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.
External linksNat Commun / PubMed:41381528 / PubMed Central
MethodsEM (single particle)
Resolution2.3 - 3.8 Å
Structure data

45997

9cxt

EMDB-45997, PDB-9cxt:
Hemagglutinin A/Hong Kong/1/68 produced in GnTI- cells
Method: EM (single particle) / Resolution: 3.4 Å

45998

9cxu

EMDB-45998, PDB-9cxu:
Endo H-treated hemagglutinin A/Hong Kong/1/68
Method: EM (single particle) / Resolution: 2.3 Å

46466

9d0y

EMDB-46466, PDB-9d0y:
Map of endoH-treated hemagglutinin A/Sing/INFIMH/16
Method: EM (single particle) / Resolution: 3.1 Å

46477

9d1u

EMDB-46477, PDB-9d1u:
Map of influenza hemagglutinin A/Sing/INFIMH/16 expressed in GntI- cells
Method: EM (single particle) / Resolution: 3.7 Å

46500

9d2m

EMDB-46500, PDB-9d2m:
Map of hemagglutinin A/Sing/INFIMH/16 expressed in 293F cells
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • influenza a virus
  • influenza a virus (strain a/hong kong/1/1968 h3n2)
  • aequorea victoria (jellyfish)
KeywordsVIRAL PROTEIN / hemagglutinin / glycoprotein / H3 / influenza / evolution / Sing16

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