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Updated: Jan 10, 2026

Immunoglobulin G N-Glycan Analysis by Ultra-Performance Liquid Chromatography
Published on: January 18, 2020
Fab N-Glycosylation in IgG: Implications in Physiological and Pathological Immune Regulation
Shuqi Chen1, Feiyuan Yu2, Binliang Huang3
1International Science and Technology Cooperation Base for Molecular Medicine, Department of Pathology, Shantou University Medical College, Shantou 515041, China.
Abstract:
Compared with classical Fc N-glycosylation, Fab N-glycosylation displays site heterogeneity and structural diversity. It contributes to immune regulation by modulating antibody stability, half-life, and antigen-binding activity, as well as by mediating blocking antibody effects. This review highlights the expression patterns and potential mechanisms of Fab N-glycosylated IgG in autoimmune diseases, pregnancy-induced immune tolerance, and tumor immune evasion, and discusses its structural and functional similarities to IgG4. Although Fab N-glycosylation plays an important role in both physiological and pathological conditions, the complexity of its glycan structures and variability in glycosylation sites hinder a precise understanding of its functional impacts. Clarifying these aspects is expected to emerge as a major focus in glycomics and antibody engineering research.
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