Quantitative N-glycoproteomic analysis reveals glycosylation signatures of plasma immunoglobulin G in systemic sclerosis
Systemic sclerosis (SSc) is a perplexing autoimmune disorder, characterized by mysterious causes, high mortality rates, and a lack of effective treatments. The role of abnormal glycosylation in the onset of autoimmune diseases has been recognized for some time. Nonetheless, the intricate details of...
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Frontiers Media S.A.
2025-02-01
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| Series: | Frontiers in Immunology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fimmu.2025.1531191/full |
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| author | Lu Cheng Lu Cheng Yanhong Li Yu Zhou Yingying Ling Tong Wu Zongan Liang Yinlan Wu Chunyu Tan Yi Liu Yong Zhang |
| author_facet | Lu Cheng Lu Cheng Yanhong Li Yu Zhou Yingying Ling Tong Wu Zongan Liang Yinlan Wu Chunyu Tan Yi Liu Yong Zhang |
| author_sort | Lu Cheng |
| collection | DOAJ |
| description | Systemic sclerosis (SSc) is a perplexing autoimmune disorder, characterized by mysterious causes, high mortality rates, and a lack of effective treatments. The role of abnormal glycosylation in the onset of autoimmune diseases has been recognized for some time. Nonetheless, the intricate details of intact glycopeptides in SSc remain elusive owing to challenges in their detection. In this study, we characterized plasma immunoglobulin G (IgG) intact N-glycopeptides from 30 SSc patients and 30 healthy controls (HCs) via our recently developed intact glycopeptide analysis method GlycoQuant. Through this approach, twelve differentially expressed intact N-glycopeptides were identified. The correlation of specific intact N-glycopeptides with the clinical features of SSc patients was analyzed. The results revealed a notable increase in the levels of 6 intact N-glycopeptides (IgG2-N3H3F1, IgG2-N3H4F1, IgG2-N4H4F1, IgG2-N4H5F1, IgG2-N5H4F1, and IgG2-N5H5F1) and a decrease in the levels of another set of 6 intact N-glycopeptides (IgG1-N4H3F1, IgG2-N3H6F1A1, IgG2-N4H4F1A1, IgG2-N5H3F1, IgG3-N4H3F1, and IgG3-N4H4F1). These changes in the levels of intact N-glycopeptides are associated with various aspects of SSc, including diffuse SSc (dSSc), interstitial lung disease (ILD), disease progression, cardiovascular involvement and C-reactive protein in the peripheral blood. In summary, this study offers a detailed overview of the intact N-glycopeptide profile in the peripheral blood of patients with SSc, providing valuable insights that could propel further research into SSc. |
| format | Article |
| id | doaj-art-c1ac99498f78443fa605e1d9bf43977b |
| institution | Kabale University |
| issn | 1664-3224 |
| language | English |
| publishDate | 2025-02-01 |
| publisher | Frontiers Media S.A. |
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| series | Frontiers in Immunology |
| spelling | doaj-art-c1ac99498f78443fa605e1d9bf43977b2025-02-07T06:49:52ZengFrontiers Media S.A.Frontiers in Immunology1664-32242025-02-011610.3389/fimmu.2025.15311911531191Quantitative N-glycoproteomic analysis reveals glycosylation signatures of plasma immunoglobulin G in systemic sclerosisLu Cheng0Lu Cheng1Yanhong Li2Yu Zhou3Yingying Ling4Tong Wu5Zongan Liang6Yinlan Wu7Chunyu Tan8Yi Liu9Yong Zhang10Department of Pulmonary and Critical Care Medicine, State Key Laboratory of Respiratory Health and Multimorbidity, Institutes for Systems Genetics, West China Hospital, Sichuan University, Chengdu, ChinaDepartment of Rheumatology and Immunology, Laboratory of Rheumatology and Immunology, West China Hospital, Sichuan University, Chengdu, ChinaDepartment of Rheumatology and Immunology, Laboratory of Rheumatology and Immunology, West China Hospital, Sichuan University, Chengdu, ChinaDepartment of Respiratory and Critical Care Medicine, Chengdu First People’s Hospital, Chengdu, ChinaDepartment of Pulmonary and Critical Care Medicine, State Key Laboratory of Respiratory Health and Multimorbidity, Institutes for Systems Genetics, West China Hospital, Sichuan University, Chengdu, ChinaDepartment of Rheumatology and Immunology, Laboratory of Rheumatology and Immunology, West China Hospital, Sichuan University, Chengdu, ChinaDepartment of Rheumatology and Immunology, Laboratory of Rheumatology and Immunology, West China Hospital, Sichuan University, Chengdu, ChinaDepartment of Rheumatology and Immunology, Laboratory of Rheumatology and Immunology, West China Hospital, Sichuan University, Chengdu, ChinaDepartment of Rheumatology and Immunology, Laboratory of Rheumatology and Immunology, West China Hospital, Sichuan University, Chengdu, ChinaDepartment of Rheumatology and Immunology, Laboratory of Rheumatology and Immunology, West China Hospital, Sichuan University, Chengdu, ChinaDepartment of Pulmonary and Critical Care Medicine, State Key Laboratory of Respiratory Health and Multimorbidity, Institutes for Systems Genetics, West China Hospital, Sichuan University, Chengdu, ChinaSystemic sclerosis (SSc) is a perplexing autoimmune disorder, characterized by mysterious causes, high mortality rates, and a lack of effective treatments. The role of abnormal glycosylation in the onset of autoimmune diseases has been recognized for some time. Nonetheless, the intricate details of intact glycopeptides in SSc remain elusive owing to challenges in their detection. In this study, we characterized plasma immunoglobulin G (IgG) intact N-glycopeptides from 30 SSc patients and 30 healthy controls (HCs) via our recently developed intact glycopeptide analysis method GlycoQuant. Through this approach, twelve differentially expressed intact N-glycopeptides were identified. The correlation of specific intact N-glycopeptides with the clinical features of SSc patients was analyzed. The results revealed a notable increase in the levels of 6 intact N-glycopeptides (IgG2-N3H3F1, IgG2-N3H4F1, IgG2-N4H4F1, IgG2-N4H5F1, IgG2-N5H4F1, and IgG2-N5H5F1) and a decrease in the levels of another set of 6 intact N-glycopeptides (IgG1-N4H3F1, IgG2-N3H6F1A1, IgG2-N4H4F1A1, IgG2-N5H3F1, IgG3-N4H3F1, and IgG3-N4H4F1). These changes in the levels of intact N-glycopeptides are associated with various aspects of SSc, including diffuse SSc (dSSc), interstitial lung disease (ILD), disease progression, cardiovascular involvement and C-reactive protein in the peripheral blood. In summary, this study offers a detailed overview of the intact N-glycopeptide profile in the peripheral blood of patients with SSc, providing valuable insights that could propel further research into SSc.https://www.frontiersin.org/articles/10.3389/fimmu.2025.1531191/fullsystemic sclerosis (SSc)N-glycosylationglycopeptideimmunoglobulin g (IgG)glycoproteomics |
| spellingShingle | Lu Cheng Lu Cheng Yanhong Li Yu Zhou Yingying Ling Tong Wu Zongan Liang Yinlan Wu Chunyu Tan Yi Liu Yong Zhang Quantitative N-glycoproteomic analysis reveals glycosylation signatures of plasma immunoglobulin G in systemic sclerosis Frontiers in Immunology systemic sclerosis (SSc) N-glycosylation glycopeptide immunoglobulin g (IgG) glycoproteomics |
| title | Quantitative N-glycoproteomic analysis reveals glycosylation signatures of plasma immunoglobulin G in systemic sclerosis |
| title_full | Quantitative N-glycoproteomic analysis reveals glycosylation signatures of plasma immunoglobulin G in systemic sclerosis |
| title_fullStr | Quantitative N-glycoproteomic analysis reveals glycosylation signatures of plasma immunoglobulin G in systemic sclerosis |
| title_full_unstemmed | Quantitative N-glycoproteomic analysis reveals glycosylation signatures of plasma immunoglobulin G in systemic sclerosis |
| title_short | Quantitative N-glycoproteomic analysis reveals glycosylation signatures of plasma immunoglobulin G in systemic sclerosis |
| title_sort | quantitative n glycoproteomic analysis reveals glycosylation signatures of plasma immunoglobulin g in systemic sclerosis |
| topic | systemic sclerosis (SSc) N-glycosylation glycopeptide immunoglobulin g (IgG) glycoproteomics |
| url | https://www.frontiersin.org/articles/10.3389/fimmu.2025.1531191/full |
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