Identification of Glycopeptides with Multiple Hydroxylysine O-Glycosylation Sites by Tandem Mass Spectrometry

Yanlin Zhang, Chuan Yih Yu, Ehwang Song, Shuai Cheng Li, Yehia Mechref, Haixu Tang, Xiaowen Liu

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

Glycosylation is one of the most common post-translational modifications in proteins, existing in ∼50% of mammalian proteins. Several research groups have demonstrated that mass spectrometry is an efficient technique for glycopeptide identification; however, this problem is still challenging because of the enormous diversity of glycan structures and the microheterogeneity of glycans. In addition, a glycopeptide may contain multiple glycosylation sites, making the problem complex. Current software tools often fail to identify glycopeptides with multiple glycosylation sites, and hence we present GlycoMID, a graph-based spectral alignment algorithm that can identify glycopeptides with multiple hydroxylysine O-glycosylation sites by tandem mass spectra. GlycoMID was tested on mass spectrometry data sets of the bovine collagen α-(II) chain protein, and experimental results showed that it identified more glycopeptide-spectrum matches than other existing tools, including many glycopeptides with two glycosylation sites.

Original languageEnglish
Pages (from-to)5099-5108
Number of pages10
JournalJournal of Proteome Research
Volume14
Issue number12
DOIs
StatePublished - Dec 4 2015

Keywords

  • Alignment algorithm
  • MS/MS spectra
  • O-linked glycosylation
  • collagen α-(II) chain
  • glycopeptide identification

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