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Updated: Mar 15, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
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Regulation of antibody effector functions through IgG Fc N-glycosylation

Isaak Quast1, Benjamin Peschke1, Jan D Lünemann2

  • 1Laboratory of Neuroinflammation, Department of Neuroinflammation, Institute of Experimental Immunology, University of Zürich, Winterthurerstrasse 190, 8057, Zurich, Switzerland.

Cellular and Molecular Life Sciences : CMLS
|September 19, 2016
PubMed

Immunoglobulin gamma (IgG) antibodies are key effector proteins of the immune system. They recognize antigens with high specificity and are indispensable for immunological memory following pathogen exposure or vaccination. The constant, crystallizable fragment (Fc) of IgG molecules mediates antibody effector functions such as complement-dependent cytotoxicity, antibody-mediated cellular cytotoxicity, and antibody-dependent cell-mediated phagocytosis. These functions are regulated by a single N-linked, biantennary glycan of the heavy chain, which resides just below the hinge region, and the presence of specific sugar moieties on the glycan has profound implications on IgG effector functions. Emerging knowledge of how Fc glycans contribute to IgG structure and functions has opened new avenues for the therapeutic exploitation of defined antibody glycoforms in the treatment of cancer and autoimmune diseases. Here, we review recent advances in understanding proinflammatory IgG effector functions and their regulation by Fc glycans.

Keywords:
AntibodyGlycanGlycobiologyImmunoglobulinImmunologyImmunotherapy

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