Dataset Information

Glycoproteomics of Flagellin C9LY14 from Selenomonas sputigena

ABSTRACT: The Gram-negative, flagellated, anaerobic, crescent-shaped bacterium Selenomonas sputigena is a potential human periodontal pathogen. Information on its virulence factors and underlying pathogenicity mechanisms is scarce. Here we show for the first time that S. sputigena produces a diversely and heavily O-glycosylated flagellin C9LY14 as a major cellular protein, which carries various hitherto undescribed rhamnose- and N acetylglucosamine-linked O-glycans in the range from mono- to hexasaccharides. A comprehensive glycomic and glycoproteomic assessment revealed extensive glycan macro- and microheterogeneity on 20 unique glycopeptide species. From the multiple sites of glycosylation, five were unambiguously identified on the 437-amino acid C9LY14 protein (Thr149, Ser182, Thr199, Thr259, and Ser334). The O-glycans additionally showed modifications by methylation and acetylation. This is the first report on O-linked flagellin glycosylation in S. sputigena, revealing that C9LY14 is one of the most heavily glycosylated flagellins described to date.

INSTRUMENT(S): amaZon Speed ETD

ORGANISM(S): Escherichia Coli Selenomonas Sputigena Atcc 35185

SUBMITTER: Daniel Kolarich

LAB HEAD: Associate Professor Daniel Kolarich, PhD

PROVIDER: PXD005859 | Pride | 2018-01-24

REPOSITORIES: Pride

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Publications

Flagellin Glycoproteomics of the Periodontitis Associated Pathogen Selenomonas sputigena Reveals Previously Not Described O-glycans and Rhamnose Fragment Rearrangement Occurring on the Glycopeptides.

Rath Cornelia B CB Schirmeister Falko F Figl Rudolf R Seeberger Peter H PH Schäffer Christina C Kolarich Daniel D

Molecular & cellular proteomics : MCP 20180116 4

Flagellated, Gram-negative, anaerobic, crescent-shaped Selenomonas species are colonizers of the digestive system, where they act at the interface between health and disease. Selenomonas sputigena is also considered a potential human periodontal pathogen, but information on its virulence factors and underlying pathogenicity mechanisms is scarce. Here we provide the first report of a Selenomonas glycoprotein, showing that S. sputigena produces a diversely and heavily < ...[more]

PMID: 29339411

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Dataset Information

Glycoproteomics of Flagellin C9LY14 from Selenomonas sputigena

Publications

Flagellin Glycoproteomics of the Periodontitis Associated Pathogen <i>Selenomonas sputigena</i> Reveals Previously Not Described <i>O</i>-glycans and Rhamnose Fragment Rearrangement Occurring on the Glycopeptides.

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