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

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Abstract

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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Most cited references 1

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Essentials of Glycobiology

Varki A, A Varki (2009)

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Author and article information

Contributors

Roni Bollag:

ORCID: http://orcid.org/0000-0003-4963-6619

Kebin Liu

William Max Alexander

Journal

Journal ID (nlm-journal-id): 0370536

Journal ID (pubmed-jr-id): 519

Journal ID (nlm-ta): Anal Chem

Journal ID (iso-abbrev): Anal Chem

Title: Analytical chemistry

ISSN (Print): 0003-2700

ISSN (Electronic): 1520-6882

Publication date Nihms-submitted: 5 December 2020

Publication date (Electronic): 15 April 2020

Publication date (Print): 05 May 2020

Publication date PMC-release: 21 December 2020

Volume: 92

Issue: 9

Pages: 6297-6303

Affiliations

Department of Chemistry, Georgia State University, Atlanta, Georgia 30303, United States

Georgia Cancer Center, Augusta University, Augusta, Georgia 30912, United States

Department of Biochemistry and Molecular Biology, Augusta University, Augusta, Georgia 30912, United States

Department of Cancer Biology and Blais Proteomics Center, Dana-Farber Cancer Institute, Boston, Massachusetts 02215, United States

Department of Chemistry, Georgia State University, Atlanta, Georgia 30303, United States

Author notes

[∇]

These authors contributed equally.

Author Contributions

H.Z., L.L., and P.G.W. conceived the project; H.Z. designed and performed the experiments, analyzed the data, and wrote the manuscript; S.W. synthesized the sialoglycopeptides; D.L. and L.D. prepared the serum glycopeptides for collision energy optimization; C.C., Y.L., and Z.W. synthesized the UDP-GalNAz; R.B. and K.L. collected and prepared the human serum samples; W.M.A. wrote the script for extracting intensities of fragmentation ions. C.M., J.Y., L.L., and P.G.W. edited the manuscript. All the authors revised and approved the manuscript.

Corresponding Authors: Lei Li - Department of Chemistry, Georgia State University, Atlanta, Georgia 30303, United States; lli22@ 123456gsu.edu , Peng George Wang - Department of Chemistry, Georgia State University, Atlanta, Georgia 30303, United States; pengwang@ 123456gsu.edu