期刊
JOURNAL OF PROTEOME RESEARCH
卷 9, 期 2, 页码 1063-1075出版社
AMER CHEMICAL SOC
DOI: 10.1021/pr900956x
关键词
bioinformatics; glycoinformatics; N-glycan; O-glycan; glycosylation; sIgA; glycoproteomics; glycopeptide; graphitized carbon; mass spectrometry; colostrum
资金
- Danish Agency for Science, Technology and Innovation [272-07-0066]
- Austrian Science Fund [J2661]
- Macquarie University
- Austrian Science Fund (FWF) [J2661] Funding Source: Austrian Science Fund (FWF)
With the emergence of glycoproteomics, there is a need to develop bioinformatic tools to identify glycopeptides in protease digests of glycoproteins. GlycoSpectrumScan is a web-based tool that identifies the glycoheterogeneity on a peptide from mass spectrometric data. Two experimental data sets are required as inputs: (1) oligosaccharide compositions of the N- and/or O-linked glycans present in the sample and (2) in silico derived peptide masses of proteolytically digested proteins with a potential number of N- and/or O-glycosylation sites. GlycoSpectrumScan uses MS data, rather than MS/MS data, to identify glycopeptides and determine the relative distribution of N- and O-glycoforms at each site. It is functional for assigning monosaccharide compositions on glycopeptides with single and multiple sites of glycosylation. The algorithm allows the input of raw mass data, including multiply charged ions, making it applicable for both ESI and MALDI data from all mass spectrometer platforms. Manual analysis time for identifying glycosylation heterogeneity at each site on glycoprotein(s) is substantially decreased. The application of this tool to characterize the N- and O-linked glycopeptides from human secretory IgA (sIgA), consisting of secretory component (7 N-linked sites), IgA1 (2 N-linked, <= 5 O-linked sites), IgA2 (4 N-linked sites) and J-chain (1 N-linked site) is described. GlycoSpectrumScan is freely available at www.glycospectrumscan.org.
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