StrucGP: de novo structural sequencing of site-specific N-glycan on glycoproteins using a modularization strategy
Precision mapping of glycans at structural and site-specific level is still one of the most challenging tasks in the glycobiology field. Here, we describe a modularization strategy for de novo interpretation of N-glycan structures on intact glycopeptides using tandem mass spectrometry. An algorithm...
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| Veröffentlicht in: | Nature methods 2021-08, Vol.18 (8), p.921-929 |
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| creator | Shen, Jiechen Jia, Li Dang, Liuyi Su, Yuanjie Zhang, Jie Xu, Yintai Zhu, Bojing Chen, Zexuan Wu, Jingyu Lan, Rongxia Hao, Zhifang Ma, Chen Zhao, Ting Gao, Ni Bai, Jieyun Zhi, Yuan Li, Jun Zhang, Junying Sun, Shisheng |
| description | Precision mapping of glycans at structural and site-specific level is still one of the most challenging tasks in the glycobiology field. Here, we describe a modularization strategy for de novo interpretation of N-glycan structures on intact glycopeptides using tandem mass spectrometry. An algorithm named StrucGP is also developed to automate the interpretation process for large-scale analysis. By dividing an N-glycan into three modules and identifying each module using distinct patterns of Y ions or a combination of distinguishable B/Y ions, the method enables determination of detailed glycan structures on thousands of glycosites in mouse brain, which comprise four types of core structure and 17 branch structures with three glycan subtypes. Owing to the database-independent glycan mapping strategy, StrucGP also facilitates the identification of rare/new glycan structures. The approach will be greatly beneficial for in-depth structural and functional study of glycoproteins in the biomedical research.
StrucGP offers a de novo glycan mapping method to determine detailed N-glycan structures at the site-specific level. |
| doi_str_mv | 10.1038/s41592-021-01209-0 |
| format | Article |
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StrucGP offers a de novo glycan mapping method to determine detailed N-glycan structures at the site-specific level.</description><identifier>ISSN: 1548-7091</identifier><identifier>EISSN: 1548-7105</identifier><identifier>DOI: 10.1038/s41592-021-01209-0</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>631/1647/2067 ; 631/1647/514/2255 ; 631/1647/794 ; 631/45/1268 ; Algorithms ; Bioinformatics ; Biological Microscopy ; Biological Techniques ; Biomedical and Life Sciences ; Biomedical Engineering/Biotechnology ; Glycan ; Glycopeptides ; Glycoproteins ; Ions ; Life Sciences ; Mapping ; Mass spectrometry ; Mass spectroscopy ; Medical research ; Modularization ; Modules ; Physiological aspects ; Polysaccharides ; Proteomics ; Structure ; Structure-function relationships</subject><ispartof>Nature methods, 2021-08, Vol.18 (8), p.921-929</ispartof><rights>The Author(s), under exclusive licence to Springer Nature America, Inc. 2021</rights><rights>COPYRIGHT 2021 Nature Publishing Group</rights><rights>The Author(s), under exclusive licence to Springer Nature America, Inc. 2021.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c419t-c55cd02c2b18dfb319a3334460f4455a556821307d750848e4ee2223a9dd388f3</citedby><cites>FETCH-LOGICAL-c419t-c55cd02c2b18dfb319a3334460f4455a556821307d750848e4ee2223a9dd388f3</cites><orcidid>0000-0002-8170-0169 ; 0000-0002-7242-7164 ; 0000-0002-3722-3991</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/s41592-021-01209-0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/s41592-021-01209-0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids></links><search><creatorcontrib>Shen, Jiechen</creatorcontrib><creatorcontrib>Jia, Li</creatorcontrib><creatorcontrib>Dang, Liuyi</creatorcontrib><creatorcontrib>Su, Yuanjie</creatorcontrib><creatorcontrib>Zhang, Jie</creatorcontrib><creatorcontrib>Xu, Yintai</creatorcontrib><creatorcontrib>Zhu, Bojing</creatorcontrib><creatorcontrib>Chen, Zexuan</creatorcontrib><creatorcontrib>Wu, Jingyu</creatorcontrib><creatorcontrib>Lan, Rongxia</creatorcontrib><creatorcontrib>Hao, Zhifang</creatorcontrib><creatorcontrib>Ma, Chen</creatorcontrib><creatorcontrib>Zhao, Ting</creatorcontrib><creatorcontrib>Gao, Ni</creatorcontrib><creatorcontrib>Bai, Jieyun</creatorcontrib><creatorcontrib>Zhi, Yuan</creatorcontrib><creatorcontrib>Li, Jun</creatorcontrib><creatorcontrib>Zhang, Junying</creatorcontrib><creatorcontrib>Sun, Shisheng</creatorcontrib><title>StrucGP: de novo structural sequencing of site-specific N-glycan on glycoproteins using a modularization strategy</title><title>Nature methods</title><addtitle>Nat Methods</addtitle><description>Precision mapping of glycans at structural and site-specific level is still one of the most challenging tasks in the glycobiology field. Here, we describe a modularization strategy for de novo interpretation of N-glycan structures on intact glycopeptides using tandem mass spectrometry. An algorithm named StrucGP is also developed to automate the interpretation process for large-scale analysis. By dividing an N-glycan into three modules and identifying each module using distinct patterns of Y ions or a combination of distinguishable B/Y ions, the method enables determination of detailed glycan structures on thousands of glycosites in mouse brain, which comprise four types of core structure and 17 branch structures with three glycan subtypes. Owing to the database-independent glycan mapping strategy, StrucGP also facilitates the identification of rare/new glycan structures. The approach will be greatly beneficial for in-depth structural and functional study of glycoproteins in the biomedical research.
StrucGP offers a de novo glycan mapping method to determine detailed N-glycan structures at the site-specific level.</description><subject>631/1647/2067</subject><subject>631/1647/514/2255</subject><subject>631/1647/794</subject><subject>631/45/1268</subject><subject>Algorithms</subject><subject>Bioinformatics</subject><subject>Biological Microscopy</subject><subject>Biological Techniques</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedical Engineering/Biotechnology</subject><subject>Glycan</subject><subject>Glycopeptides</subject><subject>Glycoproteins</subject><subject>Ions</subject><subject>Life Sciences</subject><subject>Mapping</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Medical research</subject><subject>Modularization</subject><subject>Modules</subject><subject>Physiological aspects</subject><subject>Polysaccharides</subject><subject>Proteomics</subject><subject>Structure</subject><subject>Structure-function 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| subjects | 631/1647/2067 631/1647/514/2255 631/1647/794 631/45/1268 Algorithms Bioinformatics Biological Microscopy Biological Techniques Biomedical and Life Sciences Biomedical Engineering/Biotechnology Glycan Glycopeptides Glycoproteins Ions Life Sciences Mapping Mass spectrometry Mass spectroscopy Medical research Modularization Modules Physiological aspects Polysaccharides Proteomics Structure Structure-function relationships |
| title | StrucGP: de novo structural sequencing of site-specific N-glycan on glycoproteins using a modularization strategy |
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