ArticleBiomarker research2026
Interleukin-10 enhances IgG galactosylation and sialylation.
Article in Biomarker research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
IgG antibodies contain a conserved N-linked glycosylation site at Asn297 in the Fc region, and variations in Fc glycosylation critically influence antibody effector functions. While inflammatory signals during immunization are known to reduce IgG Fc galactosylation and sialylation, the counter-regulatory pathways that enhance these modifications remain poorly understood. Here, we investigated the association of the anti-inflammatory cytokine IL-10 with germinal center (GC) responses and IgG Fc glycosylation following protein immunization in mice. Blockade of IL-10 receptor signaling after immunization with a model protein and the adjuvant Alum reduced Fc galactosylation and sialylation of antigen-specific IgG1 and was associated with decreased expression of the sialyltransferase St6gal1 in antigen-specific GC B cells and plasma cells. Although IFNγ is known to suppress IgG Fc galactosylation and sialylation, Alum immunization paradoxically induced both high levels of Fc galactosylation and sialylation as well as a high frequency of IFNγ-producing CD4
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