Jieyi Xu
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Jieyi Xu has a total of 6 co-authors. Here are the top co-authors by number of shared publications:
- Binliang Huang
Department of Clinical Laboratory Medicine, Shantou University Medical College, Shantou 515041, China
1 shared publication - Fei-Yuan Yu
Department of Cell Biology and Genetics, Shantou University Medical College, Shantou 515041, China
1 shared publication - Ganbo Liang
Shantou University Medical College, Shantou 515041, China
1 shared publication - Qian Xu
International Science and Technology Cooperation Base for Molecular Medicine, Department of Pathology, Shantou University Medical College, Shantou 515041, China
1 shared publication - Shuqi Chen
International Science and Technology Cooperation Base for Molecular Medicine, Department of Pathology, Shantou University Medical College, Shantou 515041, China
1 shared publication - Yuning Lin
Department of Cell Biology and Genetics, Shantou University Medical College, Shantou 515041, China
1 shared publication
Latest Publications
- Open Access
- 25 October 2025
- Published by MDPI AG in Biomolecules
- Vol. 15 (11) , 1508
Fab N-Glycosylation in IgG: Implications in Physiological and Pathological Immune Regulation
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.
- 25 October 2025
- Published by MDPI AG in Biomolecules
- Vol. 15 (11) , 1508
Open AccessFab N-Glycosylation in IgG: Implications in Physiological and Pathological Immune Regulation
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.