In-situ profiling of glycosylation on single cells with surface plasmon resonance imaging
Abstract Cellular glycosylation is crucial for cell recognition, signal transduction, and the development of various diseases, especially in tumor initiation, progression, and metastasis. Current glycosylation profiling methods normally involve laborious sample processing and labeling and lack in-si...
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Nature Portfolio
2025-01-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-025-56390-z |
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author | Xiaoyin Liu Jinbiao Ma Yunrui Zhang Yi Xu Yunxiao Wang Dehong Yang Di Wang Qingjun Liu Fenni Zhang |
author_facet | Xiaoyin Liu Jinbiao Ma Yunrui Zhang Yi Xu Yunxiao Wang Dehong Yang Di Wang Qingjun Liu Fenni Zhang |
author_sort | Xiaoyin Liu |
collection | DOAJ |
description | Abstract Cellular glycosylation is crucial for cell recognition, signal transduction, and the development of various diseases, especially in tumor initiation, progression, and metastasis. Current glycosylation profiling methods normally involve laborious sample processing and labeling and lack in-situ quantitative analysis. Here, we present a direct optical method to investigate and quantify the glycan expression on single cells based on lectin-glycan kinetic quantification with plasmonic imaging. Three unlabeled lectins (WGA, SBA, ConA) are employed as probes to bind with specific glycans, and binding kinetics are assessed to determine glycosylation profiles. The result reveals cell-to-cell heterogeneity in glycosylation patterns. To demonstrate the capability of our method, the glycosylation profiling of four distinct cell lines is explored, showing obvious alterations in glycan expression related to tumor initiation, progression, and metastasis. This approach enables direct quantification of glycosylation and binding kinetics, providing insights into tumor cell glycosylation mechanisms and potential applications in disease diagnosis and treatment. |
format | Article |
id | doaj-art-11b10e639fa24866aa5ec6809b7ba7b1 |
institution | Kabale University |
issn | 2041-1723 |
language | English |
publishDate | 2025-01-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
spelling | doaj-art-11b10e639fa24866aa5ec6809b7ba7b12025-01-26T12:41:48ZengNature PortfolioNature Communications2041-17232025-01-0116111410.1038/s41467-025-56390-zIn-situ profiling of glycosylation on single cells with surface plasmon resonance imagingXiaoyin Liu0Jinbiao Ma1Yunrui Zhang2Yi Xu3Yunxiao Wang4Dehong Yang5Di Wang6Qingjun Liu7Fenni Zhang8Biosensor National Special Laboratory, Department of Biomedical Engineering, Zhejiang UniversityBiosensor National Special Laboratory, Department of Biomedical Engineering, Zhejiang UniversityBiosensor National Special Laboratory, Department of Biomedical Engineering, Zhejiang UniversityStomatology Hospital, School of Stomatology, Zhejiang University School of MedicineBiosensor National Special Laboratory, Department of Biomedical Engineering, Zhejiang UniversityBiosensor National Special Laboratory, Department of Biomedical Engineering, Zhejiang UniversityBiosensor National Special Laboratory, Department of Biomedical Engineering, Zhejiang UniversityBiosensor National Special Laboratory, Department of Biomedical Engineering, Zhejiang UniversityBiosensor National Special Laboratory, Department of Biomedical Engineering, Zhejiang UniversityAbstract Cellular glycosylation is crucial for cell recognition, signal transduction, and the development of various diseases, especially in tumor initiation, progression, and metastasis. Current glycosylation profiling methods normally involve laborious sample processing and labeling and lack in-situ quantitative analysis. Here, we present a direct optical method to investigate and quantify the glycan expression on single cells based on lectin-glycan kinetic quantification with plasmonic imaging. Three unlabeled lectins (WGA, SBA, ConA) are employed as probes to bind with specific glycans, and binding kinetics are assessed to determine glycosylation profiles. The result reveals cell-to-cell heterogeneity in glycosylation patterns. To demonstrate the capability of our method, the glycosylation profiling of four distinct cell lines is explored, showing obvious alterations in glycan expression related to tumor initiation, progression, and metastasis. This approach enables direct quantification of glycosylation and binding kinetics, providing insights into tumor cell glycosylation mechanisms and potential applications in disease diagnosis and treatment.https://doi.org/10.1038/s41467-025-56390-z |
spellingShingle | Xiaoyin Liu Jinbiao Ma Yunrui Zhang Yi Xu Yunxiao Wang Dehong Yang Di Wang Qingjun Liu Fenni Zhang In-situ profiling of glycosylation on single cells with surface plasmon resonance imaging Nature Communications |
title | In-situ profiling of glycosylation on single cells with surface plasmon resonance imaging |
title_full | In-situ profiling of glycosylation on single cells with surface plasmon resonance imaging |
title_fullStr | In-situ profiling of glycosylation on single cells with surface plasmon resonance imaging |
title_full_unstemmed | In-situ profiling of glycosylation on single cells with surface plasmon resonance imaging |
title_short | In-situ profiling of glycosylation on single cells with surface plasmon resonance imaging |
title_sort | in situ profiling of glycosylation on single cells with surface plasmon resonance imaging |
url | https://doi.org/10.1038/s41467-025-56390-z |
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