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Identifying Sialylation Linkages at the Glycopeptide Level by Glycosyltransferase Labeling Assisted Mass Spectrometry (GLAMS)

By He Zhu, Shuaishuai Wang, Ding Liu, Lang Ding, Congcong Chen, Yunpeng Liu, Zhigang Wu, Roni Bollag, Kebin Liu, Jun Yin, Cheng Ma, Lei Li, Peng George Wang

Posted 21 Oct 2019
bioRxiv DOI: 10.1101/811554 (published DOI: 10.1021/acs.analchem.9b05068)

Precise assignment of sialylation linkages at the glycopeptide level is of importance in bottom-up glycoproteomics, and is also an indispensable step to understand the function of glycoproteins in pathogen-host interactions and cancer progression. Even though some efforts have been dedicated to the discrimination of α2,3/α2,6-sialylated isomers, unambiguous identification of sialoglycopeptide isomers is still needed. Herein, an innovative strategy of glycosyltransferase labeling assisted mass spectrometry (GLAMS) was developed. After specific enzymatic labeling, oxonium ions from higher-energy C-trap dissociation (HCD) fragmentation of α2,3-sailoglycopeptides generate unique reporters to distinctly differentiate those of α2,6-sailoglycopeptide isomers. Using this strategy, a total of 1,236 linkage-specific sialoglycopeptides were successfully identified from 161 glycoproteins in human serum. ![Figure][1]</img> [1]: pending:yes

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