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

Manuela Colucci, Henning Stöckmann, Alessia Butera, Andrea Masotti, Antonella Baldassarre, Ezio Giorda, Stefania Petrini, Pauline M. Rudd, Roberto Sitia, Francesco Emma, Marina Vivarelli

Research output: Contribution to journalArticlepeer-review


Human serum IgM Abs are composed of heavily glycosylated polymers with five glycosylation sites on the m (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 Ig produced and recognizes multiple Ags with low affinity, whereas immune IgM is induced by Ag exposure and is characterized by a higher Ag 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. In this study, to our knowledge, 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.

Original languageEnglish
Pages (from-to)151-157
Number of pages7
JournalJournal of Immunology
Issue number1
Publication statusPublished - Jan 1 2015

ASJC Scopus subject areas

  • Immunology


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