Dataset Information

N-glycosylation patterns of plasma immunoglobulin G in anti-synthetase syndrome disease

ABSTRACT: Anti-synthetase syndrome (ASS), a subtype of idiopathic inflammatory myopathy (IMM), is characterized by distinctive skin rashes, proximal muscle weakness, and interstitial lung disease (ILD). The etiology of ASS remains largely unknown, and patients endure a poor quality of life and are prone to pulmonary infection. Recent studies have highlighted the potential role of aberrant glycosylation of immunoglobulin G (IgG) in the development of autoimmune diseases. However, the specific N-glycosylation patterns of IgG in ASS have not yet been fully elucidated. In this study, we employed GlycoQuant, a method for intact glycopeptide analysis, to investigate the intact N-glycopeptides of IgG from 30 ASS patients and 30 healthy controls (HC). Our analysis revealed 13 differentially expressed intact N-glycopeptides in ASS. Furthermore, we observed a significant increase in fucose alongside a marked decrease in N-acetylneuraminic acid levels among ASS patients. Crucially, alterations in IgG N-glycosylation correlated with the disease severity. In conclusion, this study provides a thorough overview of IgG N-glycosylation patterns in ASS, laying a solid foundation for future research in this area.

ORGANISM(S): Homo Sapiens

SUBMITTER: Yong Zhang

PROVIDER: PXD058077 | iProX | Wed Nov 20 00:00:00 GMT 2024

REPOSITORIES: iProX

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N-glycosylation patterns of plasma immunoglobulin G in anti-synthetase syndrome disease.

Zhao Jing J Li Yanhong Y Ling Yingying Y Wu Tong T Wu Yinlan Y Tan Chunyu C Cheng Lu L Huang Deying D Liu Yi Y Zhang Yong Y

Frontiers in immunology 20250618

<h4>Introduction</h4>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-glyc ...[more]

PMID: 40607430

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Project description:Changes in IgG glycosylation have been reported to be associated with colorectal cancer (CRC), but the alteration in specific subclass of IgG is unknown. Herein, we optimized five common IgG glycopeptides enrichment methods to acquire comprehensive profiling of IgG glycoproteomics in CRC. Notably, incomplete tryptic digestion of IgG occurred when using ordinary ratio of protease to protein, which significantly impacted the final statistical analysis of association between IgG glycosylation and CRC. We introduced a method based on two-step enzymatic digestion, enabling the complete digestion of IgG glycopeptides and further improving the detection intensity of the target glycopeptides. By this approach, total 47 IgG glycopeptides can be identified by nanoLC-ESI-MS/MS. Following rapid and automatic data processing through the self-developed program, we observed that IgG1_H3N4F1 and IgG1_H3N4 were substantially increased in CRC, while IgG1_H5N5F1, IgG1_H5N4F1S1and IgG2_H5N4F1 were markedly decreased. Strikingly, these four glycopeptides were continually significantly changed in early and late stages of CRC. Further evaluation of the diagnostic performance showed they all obtained a fair performance in discriminating the patients from the normal. In terms of the glycan features, it demonstrated that CRC progression associates with the increased agalactosylation, and the decreased digalactosylation and galactosylation per antenna on diantennay glycans of IgG1 and IgG2. Concurrently, the decreased sialylation of IgG1 was strongly correlated with CRC. Moreover, tumor-specific glycosylation analysis showed that the alterations of subclass-specific IgG glycosylation were more significant in colon cancer, and no obvious difference between colon and rectal cancer was found. More importantly, all these findings were validated in an independent cohort. This two-step enzymatic approach is crucial to explore the relationship between the disease progression and IgG glycosylation.

Dataset Information

N-glycosylation patterns of plasma immunoglobulin G in anti-synthetase syndrome disease

Publications

N-glycosylation patterns of plasma immunoglobulin G in anti-synthetase syndrome disease.

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