Novel roles for the IgG Fc glycan.

Autor: Anthony RM; Leonard Wagner Laboratory of Molecular Genetics and Immunology, The Rockefeller University, New York, New York 10065, USA. ranthony01@rockefeller.edu, Wermeling F, Ravetch JV
Jazyk: angličtina
Zdroj: Annals of the New York Academy of Sciences [Ann N Y Acad Sci] 2012 Apr; Vol. 1253, pp. 170-80. Date of Electronic Publication: 2012 Jan 30.
DOI: 10.1111/j.1749-6632.2011.06305.x
Abstrakt: IgG antibodies trigger leukocyte activation and inflammation by forming immune complexes that crosslink activating Fcγ receptors (FcγRs). This is essential to combat infection, but detrimental if antibodies target or cross-react with autoantigens. The high specificity and long serum half-life of IgG antibodies confers tremendous therapeutic potential. Indeed, antibodies have been successfully employed to target cancers, autoreactive B cells, and pro-inflammatory cytokines. Conversely, IgG antibodies can also initiate anti-inflammatory responses. In the form of intravenous immunoglobulin (IVIG), IgGs are routinely administered to treat inflammatory autoimmune diseases. Importantly, the N-linked glycans on the IgG Fc are absolutely required for initiating these IgG effector functions. In fact, the Fc glycan composition dictates IgG affinity to individual FcγRs, and in a broader sense, binding to different FcγRs classes: activating, inhibitory, and anti-inflammatory (dendritic cell-specific ICAM-3 grabbing nonintegrin, DC-SIGN). The Fc glycan requirements to initiate and suppress inflammation will be discussed herein.
(© 2012 New York Academy of Sciences.)
Databáze: MEDLINE
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