期刊
JOURNAL OF PROTEOME RESEARCH
卷 11, 期 12, 页码 5781-5793出版社
AMER CHEMICAL SOC
DOI: 10.1021/pr300584x
关键词
post-translational modification; glycosylation; O-linked; diNAcBac; HCD; CID; site assignment
资金
- Research Council of Norway [166931, 183613, 183814]
- GlycoNor, the Department of Molecular Biosciences and Center for Molecular Biology and Neurosciences of the University of Oslo
The bacterial human pathogen Neisseria gonorrhoeae expresses a general O-linked protein glycosylation (Pgl) system known to target at least 12 membrane-associated proteins. To facilitate a better understanding of the mechanisms, significance and function of this glycosylation system, we sought to further delineate the target proteome of the Pgl system. To this end, we employed immunoaffinity enrichment of glycoproteins using a monoclonal antibody against the glycan moiety. Enzymatically generated peptides were subsequently analyzed by MS to identify glycopeptides and glycosylation sites. In this way, we increase the total number of known glycoproteins in N. gonorrhoeae to 19. These new glycoproteins are involved in a wide variety of extracytoplasmic functions. By employing collision fragmentation, we mapped nine new glycosylation sites, all of which were serine. No target sequon was readily apparent, although attachment sites were most often localized with regions of low sequence complexity. Moreover, we found that 5 of the proteins were modified with more than one glycan. This work thus confirms and extends earlier observations on the structural features. of Neisseria glycoproteins.
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