Click‐iG: Simultaneous Enrichment and Profiling of Intact N‐linked, O‐GalNAc, and O‐GlcNAcylated Glycopeptides

Author:

Liu Jialin12,Cheng Bo1,Fan Xinqi1,Zhou Xinyue1,Wang Jiankun1,Zhou Wen1,Li Hengyu1,Zeng Wenfeng3,Yang Pengyuan2,Chen Xing1ORCID

Affiliation:

1. College of Chemistry and Molecular Engineering Beijing National Laboratory for Molecular Sciences Peking-Tsinghua Center for Life Sciences Synthetic and Functional Biomolecules Center and Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education Peking University Beijing 100871 China

2. Institute of Biomedical Sciences and Department of Chemistry Fudan University Shanghai 200433 China

3. Key Lab of Intelligent Information Processing of Chinese Academy of Sciences (CAS) and Institute of Computing Technology CAS Beijing 100190 China

Abstract

AbstractProteins are ubiquitously modified with glycans of varied chemical structures through distinct glycosidic linkages, making the landscape of protein glycosylation challenging to map. Profiling of intact glycopeptides with mass spectrometry (MS) has recently emerged as a powerful tool for revealing matched information of the glycosylation sites and attached glycans (i.e., intact glycosites), but is largely limited to individual glycosylation types. Herein, we describe Click‐iG, which integrates metabolic labeling of glycans with clickable unnatural sugars, an optimized MS method, and a tailored version of pGlyco3 software to enable simultaneous enrichment and profiling of three types of intact glycopeptides: N‐linked, mucin‐type O‐linked, and O‐GlcNAcylated glycopeptides. We demonstrate the utility of Click‐iG by the identification of thousands of intact glycosites in cell lines and living mice. From the mouse lung, heart, and spleen, a total of 2053 intact N‐glycosites, 262 intact O‐GalNAc glycosites, and 1947 O‐GlcNAcylation sites were identified. Click‐iG‐enabled comprehensive coverage of the protein glycosylation landscape lays the foundation for interrogating crosstalk between different glycosylation pathways.

Funder

National Natural Science Foundation of China

Publisher

Wiley

Subject

General Medicine

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