Molecular determinants of sialylated IgG anti-inflammatory activity.

ABSTRACT: IgG antibodies are the basis for many successful therapeutics. A single, N-linked glycan is present on the Fc on all IgGs, and the composition of that glycan exerts marked influence over effector functions of the IgG. We and others have shown terminal sialylation of the Fc glycan confers anti-inflammatory activity to the IgG1 subclass and is thought to be responsible for the anti-inflammatory activity of high-dose intravenous immunoglobulin. However, whether sialylation results in anti-inflammatory activity for other IgG subclasses is unknown. We found that IgG1 and IgG3, but not IgG2 nor IgG4, suppressed autoantibody-mediated inflammation in vivo when sialylated. This activity was dependent upon human DC-SIGN or its murine ortholog, SIGN-R1. Fc γ receptor-binding profiles for asialylated

SUBMITTER: Sneed SL 

PROVIDER: S-EPMC12107084 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature