Characterization of core fucosylation via sequential enzymatic treatments of intact glycopeptides and mass spectrometry analysis

Liwei Cao, T. Mamie Lih, Yingwei Hu, Michael Schnaubelt, Shao-Yung Chen, Yangying Zhou, Chuanyu Guo, Mingming Dong, Weiming Yang, Rodrigo Vargas Eguez, Lijun Chen, David J. Clark, Akrit Sodhi, Qing Kay Li and Hui Zhang ()
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Liwei Cao: Johns Hopkins University
T. Mamie Lih: Johns Hopkins University
Yingwei Hu: Johns Hopkins University
Michael Schnaubelt: Johns Hopkins University
Shao-Yung Chen: Johns Hopkins University
Yangying Zhou: Johns Hopkins University
Chuanyu Guo: Johns Hopkins University School of Medicine
Mingming Dong: Johns Hopkins University
Weiming Yang: Johns Hopkins University
Rodrigo Vargas Eguez: Johns Hopkins University
Lijun Chen: Johns Hopkins University
David J. Clark: Johns Hopkins University
Akrit Sodhi: Johns Hopkins University School of Medicine
Qing Kay Li: Johns Hopkins University
Hui Zhang: Johns Hopkins University

Nature Communications, 2022, vol. 13, issue 1, 1-12

Abstract: Abstract Core fucosylation of N-linked glycoproteins has been linked to the functions of glycoproteins in physiological and pathological processes. However, quantitative characterization of core fucosylation remains challenging due to the complexity and heterogeneity of N-linked glycosylation. Here we report a mass spectrometry-based method that employs sequential treatment of intact glycopeptides with enzymes (STAGE) to analyze site-specific core fucosylation of glycoproteins. The STAGE method utilizes Endo F3 followed by PNGase F treatment to generate mass signatures for glycosites that are formerly modified by core fucosylated N-linked glycans. We benchmark the STAGE method and use it to characterize site specific core fucosylation of glycoproteins from human hepatocellular carcinoma and pancreatic ductal adenocarcinoma, resulting in the identification of 1130 and 782 core fucosylated glycosites, respectively. These results indicate that our STAGE method enables quantitative characterization of core fucosylation events from complex protein mixtures, which may benefit our understanding of core fucosylation functions in various diseases.

Date: 2022
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DOI: 10.1038/s41467-022-31472-4

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