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Updated: Sep 17, 2025

Immunoglobulin G N-Glycan Analysis by Ultra-Performance Liquid Chromatography
Published on: January 18, 2020
N-glycosylation patterns of plasma immunoglobulin G in anti-synthetase syndrome disease
Jing Zhao1, Yanhong Li1, Yingying Ling1
1Department of Rheumatology and Immunology, Laboratory of Rheumatology and Immunology, Institutes for Systems Genetics, West China Hospital, Sichuan University, Chengdu, China.
Introduction:
Anti-synthetase syndrome (ASS) is a subtype of idiopathic inflammatory myopathy (IIM) characterized by characteristic rash, myositis, and interstitial lung disease (ILD). The etiology of ASS is unknown, and patients have a poor quality of life and are prone to pulmonary infection. Recent studies have elucidated the potential role of abnormal glycosylation of immunoglobulin G (IgG) in the pathogenesis of autoimmune diseases. However, the pattern of patient-specific IgG N-glycosylation in ASS has not been fully elucidated.
Methods:
the GlycoQuant method was used to quantify the intact N-glycopeptides of IgG from 30 ASS patients and 30 healthy controls (HCs).
Results And Discussion:
Thirteen differentially expressed intact N-glycopeptides were identified (p<0.05). Notably, we observed increased fucosylation (p<0.0001) and decreased N-acetylneuraminic acid (p<0.05) in ASS patients. In addition, specific glycosylation patterns correlated with lung function parameters. Our study revealed the IgG glycosylation profile in ASS patients and provided a valuable reference for further investigation of its potential diagnostic and prognostic applications.
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