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Unknown,Transcriptomics,Genomics,Proteomics

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Sialylation of N-linked glycans influences the immunomodulatory effects of IgM on T cells

ABSTRACT: Human serum IgM antibodies are composed of heavily glycosylated polymers with five glycosylation sites on the μ (heavy) chain and one glycosylation site on the J chain. In contrast to IgG glycans, which are vital for a number of biological functions, virtually nothing is known about structure-function relationships of IgM glycans. Natural IgM is the earliest immunoglobulin produced and recognizes multiple antigens with low affinity, whilst immune IgM is induced by antigen exposure and is characterized by a higher antigen specificity. Natural anti-lymphocyte IgM is present in the serum of healthy individuals and increases in inflammatory conditions. It is able to inhibit T cell activation, but the underlying molecular mechanism is not understood. Here we show, for the first time, that sialylated N-linked glycans induce the internalization of IgM by T cells, which in turn causes severe inhibition of T cell responses. The absence of sialic acid residues abolishes these inhibitory activities, showing a key role of sialylated N-glycans in inducing the IgM-mediated immune suppression.

ORGANISM(S): Homo sapiens

SUBMITTER: Andrea Masotti

PROVIDER: E-MTAB-3030 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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