Fab N-Glycosylation in IgG: Implications in Physiological and Pathological Immune Regulation

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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.
Funding Information
  • Basic and Applied Basic Research Foundation of Guangdong Province (2021A1515010751, 2024A1515013142)
  • Special Fund Project for Science and Technology Innovation Strategy of Guangdong Province (STKJ2021206)
  • SUMC Scientific Research Initiation Grant

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