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dc.contributor.authorRath, Cornelia B
dc.contributor.authorSchirmeister, Falko
dc.contributor.authorFigl, Rudolf
dc.contributor.authorSeeberger, Peter H
dc.contributor.authorSchaeffer, Christina
dc.contributor.authorKolarich, Daniel
dc.date.accessioned2019-05-29T12:44:48Z
dc.date.available2019-05-29T12:44:48Z
dc.date.issued2018
dc.identifier.issn1535-9476
dc.identifier.doi10.1074/mcp.RA117.000394
dc.identifier.urihttp://hdl.handle.net/10072/382783
dc.description.abstractFlagellated, 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 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 identified from 22 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 only flagellin protein identified. The O-glycans additionally showed modifications by methylation and putative acetylation. Some O-glycans carried hitherto undescribed residues/modifications as determined by their respective m/z values, reflecting the high diversity of native S. sputigena flagellin. We also found that monosaccharide rearrangement occurred during collision-induced dissociation (CID) of protonated glycopeptide ions. This effect resulted in pseudo Y1-glycopeptide fragment ions that indicated the presence of additional glycosylation sites on a single glycopeptide. CID oxonium ions and electron transfer dissociation, however, confirmed that just a single site was glycosylated, showing that glycan-to-peptide rearrangement can occur on glycopeptides and that this effect is influenced by the molecular nature of the glycan moiety. This effect was most pronounced with disaccharides. This study is the first report on O-linked flagellin glycosylation in a Selenomonas species, revealing that C9LY14 is one of the most heavily glycosylated flagellins described to date. This study contributes to our understanding of the largely under-investigated surface properties of oral bacteria. The data have been deposited to the ProteomeXchange with identifier PXD005859.
dc.description.peerreviewedYes
dc.languageEnglish
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
dc.relation.ispartofpagefrom721
dc.relation.ispartofpageto736
dc.relation.ispartofissue4
dc.relation.ispartofjournalMOLECULAR & CELLULAR PROTEOMICS
dc.relation.ispartofvolume17
dc.subject.fieldofresearchMultidisciplinary
dc.subject.fieldofresearchcodeMD
dc.titleFlagellin Glycoproteomics of the Periodontitis Associated Pathogen Selenomonas sputigena Reveals Previously Not Described O-glycans and Rhamnose Fragment Rearrangement Occurring on the Glycopeptides
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
dc.description.versionPublished
gro.rights.copyrightThis research was originally published in Molecular & Cellular Proteomics (MCP). Kolarich, Daniel et al, Flagellin Glycoproteomics of the Periodontitis Associated Pathogen Selenomonas sputigena Reveals Previously Not Described O-glycans and Rhamnose Fragment Rearrangement Occurring on the Glycopeptides Molecular & Cellular Proteomics (MCP)  2018, 17 (4) 721-736. Copyright the American Society for Biochemistry and Molecular Biology. Reproduced in accordance with the copyright policy of the publisher. Please refer to the journal's website for access to the definitive version.
gro.hasfulltextFull Text
gro.griffith.authorKolarich, Daniel


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