Anti-Inflammatory Activity of Immunoglobulin G Resulting from Fc Sialylation

American Association for the Advancement of Science (AAAS) - Tập 313 Số 5787 - Trang 670-673 - 2006
Yoshikatsu Kaneko1, Falk Nimmerjahn1, Jeffrey V. Ravetch1
1Laboratory of Molecular Genetics and Immunology, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.

Tóm tắt

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.

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We thank M. Madaio for providing the NTS; C. Bertozzi for helpful discussions and suggestions; A. Datta for glycan analysis; and P. Smith J. Clowney A. Kim and J. Pagan for technical assistance. These studies were supported by grants from NIH (J.V.R.). Y.K. was supported by fellowships from the Naito Foundation the Kanae Foundation for Life & Social-Medical Science and the Uehara Memorial Foundation. F.N. is a fellow of the Cancer Research Institute.

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American Association for the Advancement of Science (AAAS)

Tập 313 Số 5787

670-673

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