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TitleDistinct binding modes drive the broad neutralization profile of two persistent influenza hemagglutinin stem-specific antibody lineages.
Journal, issue, pagesStructure, Vol. 33, Issue 5, Page 869-877.e7, Year 2025
Publish dateMay 1, 2025
AuthorsGrace E Mantus / Gabriele Cerutti / Michael Chambers / Rebecca A Gillespie / Geoffrey D Shimberg / Abby Spangler / Jason Gorman / Tongqing Zhou / Chen-Hsiang Shen / Masaru Kanekiyo / Peter D Kwong / Lawrence Shapiro / Sarah F Andrews /
PubMed AbstractElicitation of antibodies to the influenza hemagglutinin stem is a critical part of universal influenza vaccine strategies. While numerous broadly reactive stem antibodies have been isolated, our ...Elicitation of antibodies to the influenza hemagglutinin stem is a critical part of universal influenza vaccine strategies. While numerous broadly reactive stem antibodies have been isolated, our understanding of how these antibodies mature within the human B cell repertoire is limited. Here, we isolated and tracked two stem-specific antibody lineages over a decade in a single participant that received multiple seasonal and pandemic influenza vaccinations. Despite similar binding and neutralization profiles, antibodies from these lineages utilized fundamentally different interactions to engage the central epitope on the influenza stem. Structural analysis of an unmutated common ancestor from one lineage identified critical residues that were the main drivers of increased affinity and breadth to group 1 influenza subtypes. These observations demonstrate the heterogeneous pathways by which stem-specific antibodies can mature within the human B cell repertoire.
External linksStructure / PubMed:40112805 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.97 - 3.5 Å
Structure data

43169

8veb

EMDB-43169, PDB-8veb:
Cryo-EM structure of antibody T5-1E08 in complex with stabilized H1N1 Influenza Hemagglutinin Trimer (A/Kiev/1/57)
Method: EM (single particle) / Resolution: 2.97 Å

43170

8ved

EMDB-43170, PDB-8ved:
Cryo-EM structure of antibody T5-1E11 in complex with stabilized H1N1 Influenza Hemagglutinin Trimer (A/Kiev/1/57)
Method: EM (single particle) / Resolution: 2.98 Å

43171

8vee

EMDB-43171, PDB-8vee:
Cryo-EM structure of antibody T5-1E08 in complex with H7N9 Influenza Hemagglutinin Trimer (A/Shanghai/2/13)
Method: EM (single particle) / Resolution: 3.18 Å

43172

8vef

EMDB-43172, PDB-8vef:
Cryo-EM structure of antibody T5-1E08 UCA (unmutated common ancestor) in complex with stabilized H1N1 Influenza Hemagglutinin Trimer (A/Kiev/1/57)
Method: EM (single particle) / Resolution: 3.04 Å

PDB-8t1g:
The crystal structure of hemagglutinin form a h7n9 influenza virus (a/shanghai/1/2013) in complex with antibody 1E11
Method: X-RAY DIFFRACTION / Resolution: 3.5 Å

Chemicals

ChemComp-CA:
Unknown entry

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

Source
  • influenza a virus
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM/VIRAL PROTEIN / hemagglutinin / influenza / virus / antibody / H7N9 / IMMUNE SYSTEM / IMMUNE SYSTEM-VIRAL PROTEIN complex / Broadly neutralizing antibody / group 1 / antibody maturation / cryo-EM / Fab / trimer / spike / viral protein / Group 2 / unmutated common ancestor / UCA

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