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Updated: Jan 28, 2026

Analysis of SCAP N-glycosylation and Trafficking in Human Cells
Published on: November 8, 2016
IgG Fc Glycosylation in Human Immunity
Taia T Wang1,2
1Department of Medicine, Division of Infectious Diseases, Department of Microbiology and Immunology, Program in Immunology, Stanford University School of Medicine, Stanford University, Stanford, CA, 94305, USA. taiawang@stanford.edu.
Abstract:
Glycosylation of IgG Fc domains is a central mechanism in the diversification of antibody function. Modifications to the core Fc glycan impact antibody function by shifting the balance of Type I and Type II Fc gamma receptors (FcγR) that will be engaged by immune complexes. This, in turn, modulates the effector cells and functions that can be recruited during immune activation. Critically, humans have evolved to regulate Fc glycan modifications for immune homeostasis. Dysregulation in Fc glycan modifications can lead to loss of immune tolerance, symptomatic autoimmunity, and susceptibility to infectious diseases. Here, we discuss IgG Fc glycosylation and its role in human health and disease.
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