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Updated: May 17, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
[Glycosylation-dependent effector function of IgG antibodies]
1Labor für Toleranz und Autoimmunität, Institut für Systemische Entzündungsforschung, Universität zu Lübeck, Ratzeburger Allee 160, 23538, Lübeck, Deutschland. Marc.Ehlers@uk-sh.de
The Fc fragments of pathogenic IgG autoantibodies in patients with rheumatoid arthritis are low-galactosylated and low-sialylated. In contrast, high-galactosylated and high-sialylated antigen-specific IgG antibodies are sufficient to inhibit a pro-inflammatory immune response in an antigen-specific manner and might be a promising therapeutic tool to re-establish tolerance against defined self-antigens in autoimmune patients.
The Fc fragments of pathogenic IgG autoantibodies in patients with rheumatoid arthritis are low-galactosylated and low-sialylated. In contrast, high-galactosylated and high-sialylated antigen-specific IgG antibodies are sufficient to inhibit a pro-inflammatory immune response in an antigen-specific manner and might be a promising therapeutic tool to re-establish tolerance against defined self-antigens in autoimmune patients.
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