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TitleSerum IgA proteomics reveals clonal composition and neutralization of dimeric and monomeric IgA repertoires against human norovirus.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 123, Issue 34, Page e2603905123, Year 2026
Publish dateAug 25, 2026
AuthorsJuyeon Park / Gyunghee Jo / Yaoska Reyes / Whitney Pickens / Dae Sung Kim / Alexandra Beaver / Verónica P Costantini / Chang Liu / Daeun Kim / Daechan Park / Victoria Longo / Paul D Brewer-Jensen / Michael L Mallory / Ed Satterwhite / Rocio Zapata-Bustos / Jeffrey Marchioni / Mark R Zweigart / Becca A Flitter / Jan Vinjé / Julianna Han / Ted M Ross / Jiwon Lee / Jason J Lavinder / Sean N Tucker / Zunlong Ke / Andrew B Ward / Lisa C Lindesmith / Ralph S Baric / George Georgiou /
PubMed AbstractProtection against human norovirus correlates with attachment ligand blockade antibody titers, fecal IgA titers, and serum IgA titers. IgA responses in serum comprise approximately 80 to 95% of ...Protection against human norovirus correlates with attachment ligand blockade antibody titers, fecal IgA titers, and serum IgA titers. IgA responses in serum comprise approximately 80 to 95% of monomeric IgA (mIgA) and 5 to 20% of dimeric IgA (dIgA). Using serum LC-MS/MS proteomics, we established clonal relationships between circulating IgG and IgA, as well as between dIgA and mIgA. We observed a modest degree of clonal overlap between circulating IgG and IgA at steady state and found that more than 80% of antigen-specific mIgA was also detectable as dIgA. We biochemically characterized neutralizing epitopes on norovirus GII.4 virus-like particles (VLPs) targeted by serum IgA clonotypes and demonstrated that dIgA markedly enhances neutralization potency relative to mIgA and IgG in an epitope-specific manner. Cryoelectron microscopy and cryoelectron tomography revealed that whether IgA dimerization enhances viral neutralization depends on epitope accessibility on the VLP and antibody binding orientation. Together, these findings provide molecular-level resolution of the serum IgA response and define the structural basis by which dIgA enhances neutralization potency in an epitope-specific manner.
External linksProc Natl Acad Sci U S A / PubMed:42607213 / PubMed Central
MethodsEM (single particle)
Resolution2.93 - 7.68 Å
Structure data

71602

9pfj

EMDB-71602, PDB-9pfj:
Cryo-EM structure of VX77 Fab in complex with GII.4 Norovirus P domain
Method: EM (single particle) / Resolution: 3.08 Å

71603

9pfk

EMDB-71603, PDB-9pfk:
Cryo-EM structure of VX93 Fab in complex with GII.4 Norovirus P domain
Method: EM (single particle) / Resolution: 2.93 Å

EMDB-72540: Cryo-EM map of norovirus GII.4 SY 2012 VLP in complex with VX77 Fab
Method: EM (single particle) / Resolution: 3.43 Å

EMDB-72541: Cryo-EM map of norovirus GII.4 SY 2012 VLP in complex with VX93 Fab
Method: EM (single particle) / Resolution: 3.34 Å

EMDB-72542: Cryo-EM map of norovirus GII.4 SY 2012 VLP in complex with VX93 Fab - fivefold axis local map (4 Fabs)
Method: EM (single particle) / Resolution: 6.97 Å

EMDB-72543: Cryo-EM map of norovirus GII.4 SY 2012 VLP in complex with VX93 Fab - fivefold axis local map (5 Fabs-1)
Method: EM (single particle) / Resolution: 6.5 Å

EMDB-72544: Cryo-EM map of norovirus GII.4 SY 2012 VLP in complex with VX93 Fab - fivefold axis local map (5 Fabs-2)
Method: EM (single particle) / Resolution: 7.53 Å

EMDB-72545: Cryo-EM map of norovirus GII.4 SY 2012 VLP in complex with VX93 Fab - fivefold axis local map (3 Fabs-1)
Method: EM (single particle) / Resolution: 7.42 Å

EMDB-72546: Cryo-EM map of norovirus GII.4 SY 2012 VLP in complex with VX93 Fab - fivefold axis local map (3 Fabs-2)
Method: EM (single particle) / Resolution: 6.66 Å

EMDB-72547: Cryo-EM map of norovirus GII.4 SY 2012 VLP in complex with VX93 Fab - threefold axis local map (1 Fab)
Method: EM (single particle) / Resolution: 7.68 Å

EMDB-72548: Cryo-EM map of norovirus GII.4 SY 2012 VLP in complex with VX93 Fab - threefold axis local map (2 Fabs-1)
Method: EM (single particle) / Resolution: 7.39 Å

EMDB-72549: Cryo-EM map of norovirus GII.4 SY 2012 VLP in complex with VX93 Fab - threefold axis local map (2 Fabs-2)
Method: EM (single particle) / Resolution: 7.46 Å

EMDB-72550: Cryo-EM map of norovirus GII.4 SY 2012 VLP in complex with VX93 Fab - threefold axis local map (2 Fabs-3)
Method: EM (single particle) / Resolution: 6.59 Å

EMDB-72551: Cryo-EM map of norovirus GII.4 SY 2012 VLP in complex with VX93 Fab - threefold axis local map (3 Fabs)
Method: EM (single particle) / Resolution: 6.65 Å

Source
  • homo sapiens (human)
  • norovirus hu/gii.4/sydney/nsw0514/2012/au
  • Norovirus GII.4 Sydney 2012
KeywordsVIRAL PROTEIN/Immune System / Norovirus / Antibody complex / VIRAL PROTEIN / VIRAL PROTEIN-Immune System complex

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