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Selenomonas sputigena

ABSTRACT: Selenomonas sputigena overview

PROVIDER: PRJNA37563 | ENA |

REPOSITORIES: ENA

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			Action	DRS
		Other
	SRR036289.fastq.gz	Fastqsanger.gz
	SRR036289_1.fastq.gz	Fastqsanger.gz
	SRR036289_2.fastq.gz	Fastqsanger.gz
	SRR072768.fastq.gz	Fastqsanger.gz

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Glycoproteomics of Flagellin C9LY14 from Selenomonas sputigena

Project description: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.

2018-01-24 | PXD005859 | Pride

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