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• W2996328086 abstract "Abstract Secretory immunoglobulin A (SIgA), the most abundant antibody isotype in the body, maintains a mutual relationship with commensal bacteria and acts as a primary barrier at the mucosal surface. Colonization by commensal bacteria induces an IgA response, at least partly through a T-cell-independent process. However, the mechanism underlying the commensal-bacteria-induced T-cell-independent IgA response has yet to be fully clarified. Here, we show that commensal-bacteria-derived butyrate promotes T-cell-independent IgA class switching recombination (CSR) in the mouse colon. Notably, the butyrate concentration in human stools correlated positively with the amount of IgA. Butyrate up-regulated the production of transforming growth factor β1 and all-trans retinoic acid by CD103+CD11b+ dendritic cells, both of which are critical for T-cell-independent IgA CSR. This effect was mediated by G-protein-coupled receptor 41 (GPR41/FFA3) and GPR109a/HCA2, and the inhibition of histone deacetylase. The butyrate-induced IgA response reinforced the colonic barrier function, preventing systemic bacterial dissemination under inflammatory conditions. These observations demonstrate that commensal-bacteria-derived butyrate contributes to the maintenance of the gut immune homeostasis by facilitating the T-cell-independent IgA response in the colon." @default.
• W2996328086 created "2019-12-26" @default.
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• W2996328086 date "2019-12-20" @default.
• W2996328086 modified "2023-10-08" @default.
• W2996328086 title "Commensal-bacteria-derived butyrate promotes the T-cell-independent IgA response in the colon" @default.
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• W2996328086 doi "https://doi.org/10.1093/intimm/dxz078" @default.
• W2996328086 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31858119" @default.
• W2996328086 hasPublicationYear "2019" @default.
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