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TitleMaturation of germinal center B cells after influenza virus vaccination in humans.
Journal, issue, pagesJ Exp Med, Vol. 221, Issue 8, Year 2024
Publish dateAug 5, 2024
AuthorsKatherine M McIntire / Hailong Meng / Ting-Hui Lin / Wooseob Kim / Nina E Moore / Julianna Han / Meagan McMahon / Meng Wang / Sameer Kumar Malladi / Bassem M Mohammed / Julian Q Zhou / Aaron J Schmitz / Kenneth B Hoehn / Juan Manuel Carreño / Temima Yellin / Teresa Suessen / William D Middleton / Sharlene A Teefey / Rachel M Presti / Florian Krammer / Jackson S Turner / Andrew B Ward / Ian A Wilson / Steven H Kleinstein / Ali H Ellebedy /
PubMed AbstractGerminal centers (GC) are microanatomical lymphoid structures where affinity-matured memory B cells and long-lived bone marrow plasma cells are primarily generated. It is unclear how the maturation ...Germinal centers (GC) are microanatomical lymphoid structures where affinity-matured memory B cells and long-lived bone marrow plasma cells are primarily generated. It is unclear how the maturation of B cells within the GC impacts the breadth and durability of B cell responses to influenza vaccination in humans. We used fine needle aspiration of draining lymph nodes to longitudinally track antigen-specific GC B cell responses to seasonal influenza vaccination. Antigen-specific GC B cells persisted for at least 13 wk after vaccination in two out of seven individuals. Monoclonal antibodies (mAbs) derived from persisting GC B cell clones exhibit enhanced binding affinity and breadth to influenza hemagglutinin (HA) antigens compared with related GC clonotypes isolated earlier in the response. Structural studies of early and late GC-derived mAbs from one clonal lineage in complex with H1 and H5 HAs revealed an altered binding footprint. Our study shows that inducing sustained GC reactions after influenza vaccination in humans supports the maturation of responding B cells.
External linksJ Exp Med / PubMed:38935072 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.75 - 3.41 Å
Structure data

41874

8u44

EMDB-41874, PDB-8u44:
CryoEM structure of A/Solomon Islands/3/2006 H1 HA in complex with 05.GC.w2.3C10-H1_SI06
Method: EM (single particle) / Resolution: 3.41 Å

PDB-8txm:
Crystal structure of 05.GC.w13.02 Fab in complex with H1 HA from A/California/04/2009(H1N1)
Method: X-RAY DIFFRACTION / Resolution: 3.25 Å

PDB-8txp:
Crystal structure of 05.GC.w13.01 Fab in complex with H1 HA from A/California/04/2009(H1N1)
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

PDB-8txt:
Crystal structure of 05.GC.w13.02 Fab in complex with H5 HA from A/Viet Nam/1203/2004(H5N1)
Method: X-RAY DIFFRACTION / Resolution: 3.19 Å

PDB-8ty7:
Crystal structure of 05.GC.w2.3C10 Fab in complex with H1 HA from A/California/04/2009(H1N1)
Method: X-RAY DIFFRACTION / Resolution: 3.21 Å

Chemicals

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

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
  • influenza a virus
  • influenza a virus (strain swl a/california/04/2009 h1n1)
  • influenza a virus (a/viet nam/1203/2004(h5n1))
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / H1N1 / Antibody / Hemagglutinin / VIRAL PROTEIN-IMMUNE SYSTEM complex / Influenza virus / H1 / monoclonal antibody / virus

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