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Science. 2006 Aug 4;313(5787):670-3.

Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation.

Author information

1
Laboratory of Molecular Genetics and Immunology, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.

Abstract

Immunoglobulin G (IgG) mediates pro- and anti-inflammatory activities through the engagement of its Fc fragment (Fc) with distinct Fcg receptors (FcgRs). One class of Fc-FcgR interactions generates pro-inflammatory effects of immune complexes and cytotoxic antibodies. In contrast, therapeutic intravenous gamma globulin and its Fc fragments are anti-inflammatory. We show here that these distinct properties of the IgG Fc result from differential sialylation of the Fc core polysaccharide. IgG acquires anti-inflammatory properties upon Fc sialylation, which is reduced upon the induction of an antigen-specific immune response. This differential sialylation may provide a switch from innate anti-inflammatory activity in the steady state to generating adaptive pro-inflammatory effects upon antigenic challenge.

PMID:
16888140
DOI:
10.1126/science.1129594
[Indexed for MEDLINE]
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