ArticleProteomics2015
Comprehensive mapping of O-glycosylation in flagellin from Campylobacter jejuni 11168: A multienzyme differential ion mobility mass spectrometry approach.
Article in Proteomics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Review
- Review
- The Missing Pieces: The Role of Secretion Systems inBiomolecules · 2023Review
- Open Database Searching Enables the Identification and Comparison of Bacterial Glycoproteomes without Defining Glycan Compositions Prior to Searching.Molecular & cellular proteomics : MCP · 2020Article
- Binding of Phage-Encoded FlaGrab to MotileFrontiers in microbiology · 2020Article
- Cj1388 Is a RidA Homolog and Is Required for Flagella Biosynthesis and/or Function inFrontiers in microbiology · 2019Article
- Campylobacter jejuni: collective components promoting a successful enteric lifestyle.Nature reviews. Microbiology · 2018Review
- Recent advances in ion mobility-mass spectrometry for improved structural characterization of glycans and glycoconjugates.Current opinion in chemical biology · 2018Review
- Importance ofFrontiers in microbiology · 2017Article
- Localization of Post-Translational Modifications in Peptide Mixtures via High-Resolution Differential Ion Mobility Separations Followed by Electron Transfer Dissociation.Journal of the American Society for Mass Spectrometry · 2016Article
- To What Extent is FAIMS Beneficial in the Analysis of Proteins?Journal of the American Society for Mass Spectrometry · 2016Article
- The Minor Flagellin ofFrontiers in microbiology · 2016Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycosylation of flagellin is essential for the virulence of Campylobacter jejuni, a leading cause of bacterial gastroenteritis. Here, we demonstrate comprehensive mapping of the O-glycosylation of flagellin from Campylobacter jejuni 11168 by use of a bottom-up proteomics approach that incorporates differential ion mobility spectrometry (also known as high field asymmetric waveform ion mobility spectrometry or FAIMS) together with proteolysis with proteinase K. Proteinase K provides complementary sequence coverage to that achieved following trypsin proteolysis. The use of FAIMS increased the number of glycopeptides identified. Novel glycans for this strain were identified (pseudaminic acid and either acetamidino pseudaminic acid or legionaminic acid), as were novel glycosylation sites: Thr208, Ser343, Ser348, Ser349, Ser395, Ser398, Ser423, Ser433, Ser436, Ser445, Ser448, Ser451, Ser452, Ser454, Ser457 and Thr465. Multiply glycosylated peptides were observed, as well as variation at individual residues in the nature of the glycan and its presence or absence. Such extreme heterogeneity in the pattern of glycosylation has not been reported previously, and suggests a novel dimension in molecular variation within a bacterial population that may be significant in persistence of the organism in its natural environment. These results demonstrate the usefulness of differential ion mobility in proteomics investigations of PTMs.
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