Sialylation of N-Linked Glycans Influences the Immunomodulatory Effects of IgM on T Cells

Internalization Immunoglobulin M
DOI: 10.4049/jimmunol.1402025 Publication Date: 2014-11-25T04:29:05Z
ABSTRACT
Human serum IgM Abs are composed of heavily glycosylated polymers with five glycosylation sites on the μ (heavy) chain and one site J chain. In contrast to IgG glycans, which vital for a number biological functions, virtually nothing is known about structure-function relationships glycans. Natural earliest Ig produced recognizes multiple Ags low affinity, whereas immune induced by Ag exposure characterized higher specificity. anti-lymphocyte present in healthy individuals increases inflammatory conditions. It able inhibit T cell activation, but underlying molecular mechanism not understood. this study, our knowledge, we show first time that sialylated N-linked glycans induce internalization cells, turn causes severe inhibition responses. The absence sialic acid residues abolishes these inhibitory activities, showing key role N-glycans inducing IgM-mediated suppression.
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