TY - JOUR
T1 - Identifying Sialylation Linkages at the Glycopeptide Level by Glycosyltransferase Labeling Assisted Mass Spectrometry (GLAMS)
AU - Zhu, He
AU - Wang, Shuaishuai
AU - Liu, Ding
AU - Ding, Lang
AU - Chen, Congcong
AU - Liu, Yunpeng
AU - Wu, Zhigang
AU - Bollag, Roni
AU - Liu, Kebin
AU - Alexander, William Max
AU - Yin, Jun
AU - Ma, Cheng
AU - Li, Lei
AU - Wang, Peng George
N1 - Funding Information:
We sincerely thank Dr. Wenfeng Zeng from the Key Lab of Intelligent Information Processing of Chinese Academy of Sciences for the help on parameter setting of pGlyco 3.0, Georgia Cancer Center Biorepository for providing human serum samples, and Georgia Research Alliance for financial support to purchase mass spectrometers. This work is supported by National Institute of Health (U54HL142019 and U01GM116263).
Publisher Copyright:
© 2020 American Chemical Society.
PY - 2020/5/5
Y1 - 2020/5/5
N2 - Precise assignment of sialylation linkages at the glycopeptide level is of importance in bottom-up glycoproteomics and 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, we developed an innovative glycosyltransferase labeling assisted mass spectrometry (GLAMS) strategy. After specific enzymatic labeling, oxonium ions from higher-energy C-trap dissociation (HCD) fragmentation of α2,3-sailoglycopeptides then generate unique reporters to distinctly differentiate those of α2,6-sailoglycopeptide isomers. With this strategy, a total of 1236 linkage-specific sialoglycopeptides were successfully identified from 161 glycoproteins in human serum.
AB - Precise assignment of sialylation linkages at the glycopeptide level is of importance in bottom-up glycoproteomics and 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, we developed an innovative glycosyltransferase labeling assisted mass spectrometry (GLAMS) strategy. After specific enzymatic labeling, oxonium ions from higher-energy C-trap dissociation (HCD) fragmentation of α2,3-sailoglycopeptides then generate unique reporters to distinctly differentiate those of α2,6-sailoglycopeptide isomers. With this strategy, a total of 1236 linkage-specific sialoglycopeptides were successfully identified from 161 glycoproteins in human serum.
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U2 - 10.1021/acs.analchem.9b05068
DO - 10.1021/acs.analchem.9b05068
M3 - Article
AN - SCOPUS:85084830654
SN - 0003-2700
VL - 92
SP - 6297
EP - 6303
JO - Analytical Chemistry
JF - Analytical Chemistry
IS - 9
ER -