TY - JOUR
T1 - Identification of Glycopeptides with Multiple Hydroxylysine O-Glycosylation Sites by Tandem Mass Spectrometry
AU - Zhang, Yanlin
AU - Yu, Chuan Yih
AU - Song, Ehwang
AU - Li, Shuai Cheng
AU - Mechref, Yehia
AU - Tang, Haixu
AU - Liu, Xiaowen
N1 - Publisher Copyright:
© 2015 American Chemical Society.
PY - 2015/12/4
Y1 - 2015/12/4
N2 - 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.
AB - 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.
KW - Alignment algorithm
KW - MS/MS spectra
KW - O-linked glycosylation
KW - collagen α-(II) chain
KW - glycopeptide identification
UR - http://www.scopus.com/inward/record.url?scp=84948981801&partnerID=8YFLogxK
U2 - 10.1021/acs.jproteome.5b00299
DO - 10.1021/acs.jproteome.5b00299
M3 - Article
C2 - 26565680
AN - SCOPUS:84948981801
VL - 14
SP - 5099
EP - 5108
JO - Journal of Proteome Research
JF - Journal of Proteome Research
SN - 1535-3893
IS - 12
ER -