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Retrospective screening of serum IgG glycosylation biomarker for primary Sjögren’s syndrome using lectin microarray
BACKGROUND: Primary Sjögren’s syndrome (PSS) is a systemic autoimmune disease resulting in significant loss of systemic gland secretory function. IgG glycosylation abnormalities had been found to play important roles in autoimmune diseases. Here, we aim to explore the specific changes of IgG glycosy...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
PeerJ Inc.
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9961092/ https://www.ncbi.nlm.nih.gov/pubmed/36852221 http://dx.doi.org/10.7717/peerj.14853 |
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author | Li, Siting Zeng, Xiaoli Tang, Shiyi Li, Xi Zhang, Guoyuan Li, Mengtao Zeng, Xiaofeng Hu, Chaojun |
author_facet | Li, Siting Zeng, Xiaoli Tang, Shiyi Li, Xi Zhang, Guoyuan Li, Mengtao Zeng, Xiaofeng Hu, Chaojun |
author_sort | Li, Siting |
collection | PubMed |
description | BACKGROUND: Primary Sjögren’s syndrome (PSS) is a systemic autoimmune disease resulting in significant loss of systemic gland secretory function. IgG glycosylation abnormalities had been found to play important roles in autoimmune diseases. Here, we aim to explore the specific changes of IgG glycosylation in PSS patient serum that could serve as potential biomarkers for disease diagnosis and differential diagnosis. METHOD: From 2012 to 2018, patients diagnosed with PSS or primary biliary cholangitis (PBC) admitted consecutively to the department of Rheumatology at Peking Union Medical College Hospital were retrospectively included in this study. Glycan profiles of serum IgG from 40 PSS patients, 50 PBC patients, and 38 healthy controls were detected with lectin microarray containing 56 lectins. Lectins with significantly different signal intensity among groups were selected and validated by lectin blot assay. RESULTS: Lectin microarray analysis revealed that binding levels of Amaranthus Caudatus Lectin (ACL, prefers glycan Galβ3GalNAc, P = 0.011), Morniga M Lectin (MNA-M, prefers glycan mannose. P = 0.013), and Lens Culinaris Agglutinin (LCA, prefers glycan fucose) were significantly increased, while Salvia sclarea Agglutinin (SSA, prefers glycan sialylation, P = 0.001) was significantly decreased in PSS patients compared to PBC group. Compared to healthy controls, MNA-M (P = 0.001) and LCA (P = 0.028) were also significantly increased, while Phaseolus Vulgaris Erythroagglutinin and Phaseolus Vulgaris Leucoagglutinin (PHA-E and PHA-L, prefer glycan galactose, P = 0.004 and 0.006) were significantly decreased in PSS patients. The results of LCA and MNA-M were further confirmed using lectin blot assay. CONCLUSION: Changes in serum IgG glycosylation in PSS increased binding levels of LCA and MNA-M lectins using microarray techniques compared to PBC patients and healthy controls, which could provide potential diagnostic value. Increased core fucose and mannose alteration of IgG may play important roles in PSS disease. |
format | Online Article Text |
id | pubmed-9961092 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | PeerJ Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-99610922023-02-26 Retrospective screening of serum IgG glycosylation biomarker for primary Sjögren’s syndrome using lectin microarray Li, Siting Zeng, Xiaoli Tang, Shiyi Li, Xi Zhang, Guoyuan Li, Mengtao Zeng, Xiaofeng Hu, Chaojun PeerJ Molecular Biology BACKGROUND: Primary Sjögren’s syndrome (PSS) is a systemic autoimmune disease resulting in significant loss of systemic gland secretory function. IgG glycosylation abnormalities had been found to play important roles in autoimmune diseases. Here, we aim to explore the specific changes of IgG glycosylation in PSS patient serum that could serve as potential biomarkers for disease diagnosis and differential diagnosis. METHOD: From 2012 to 2018, patients diagnosed with PSS or primary biliary cholangitis (PBC) admitted consecutively to the department of Rheumatology at Peking Union Medical College Hospital were retrospectively included in this study. Glycan profiles of serum IgG from 40 PSS patients, 50 PBC patients, and 38 healthy controls were detected with lectin microarray containing 56 lectins. Lectins with significantly different signal intensity among groups were selected and validated by lectin blot assay. RESULTS: Lectin microarray analysis revealed that binding levels of Amaranthus Caudatus Lectin (ACL, prefers glycan Galβ3GalNAc, P = 0.011), Morniga M Lectin (MNA-M, prefers glycan mannose. P = 0.013), and Lens Culinaris Agglutinin (LCA, prefers glycan fucose) were significantly increased, while Salvia sclarea Agglutinin (SSA, prefers glycan sialylation, P = 0.001) was significantly decreased in PSS patients compared to PBC group. Compared to healthy controls, MNA-M (P = 0.001) and LCA (P = 0.028) were also significantly increased, while Phaseolus Vulgaris Erythroagglutinin and Phaseolus Vulgaris Leucoagglutinin (PHA-E and PHA-L, prefer glycan galactose, P = 0.004 and 0.006) were significantly decreased in PSS patients. The results of LCA and MNA-M were further confirmed using lectin blot assay. CONCLUSION: Changes in serum IgG glycosylation in PSS increased binding levels of LCA and MNA-M lectins using microarray techniques compared to PBC patients and healthy controls, which could provide potential diagnostic value. Increased core fucose and mannose alteration of IgG may play important roles in PSS disease. PeerJ Inc. 2023-02-22 /pmc/articles/PMC9961092/ /pubmed/36852221 http://dx.doi.org/10.7717/peerj.14853 Text en © 2023 Li et al. https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ) and either DOI or URL of the article must be cited. |
spellingShingle | Molecular Biology Li, Siting Zeng, Xiaoli Tang, Shiyi Li, Xi Zhang, Guoyuan Li, Mengtao Zeng, Xiaofeng Hu, Chaojun Retrospective screening of serum IgG glycosylation biomarker for primary Sjögren’s syndrome using lectin microarray |
title | Retrospective screening of serum IgG glycosylation biomarker for primary Sjögren’s syndrome using lectin microarray |
title_full | Retrospective screening of serum IgG glycosylation biomarker for primary Sjögren’s syndrome using lectin microarray |
title_fullStr | Retrospective screening of serum IgG glycosylation biomarker for primary Sjögren’s syndrome using lectin microarray |
title_full_unstemmed | Retrospective screening of serum IgG glycosylation biomarker for primary Sjögren’s syndrome using lectin microarray |
title_short | Retrospective screening of serum IgG glycosylation biomarker for primary Sjögren’s syndrome using lectin microarray |
title_sort | retrospective screening of serum igg glycosylation biomarker for primary sjögren’s syndrome using lectin microarray |
topic | Molecular Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9961092/ https://www.ncbi.nlm.nih.gov/pubmed/36852221 http://dx.doi.org/10.7717/peerj.14853 |
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