PXD005859 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Glycoproteomics of Flagellin C9LY14 from Selenomonas sputigena |
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. |
HostingRepository | PRIDE |
AnnounceDate | 2018-01-24 |
AnnouncementXML | Submission_2018-01-25_01:30:05.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Daniel Kolarich |
SpeciesList | scientific name: Escherichia coli; NCBI TaxID: 562; scientific name: Selenomonas sputigena ATCC 35185; NCBI TaxID: 546271; |
ModificationList | N-acetylhexosaminylated; monohydroxylated residue |
Instrument | amaZon Speed ETD |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2017-02-06 03:34:32 | ID requested | |
⏵ 1 | 2018-01-25 01:30:06 | announced | |
2 | 2024-10-22 04:35:32 | announced | 2024-10-22: Updated project metadata. |
Publication List
Rath CB, Schirmeister F, Figl R, Seeberger PH, Sch, รค, ffer C, Kolarich D, -glycans and Rhamnose Fragment Rearrangement Occurring on the Glycopeptides. Mol Cell Proteomics, 17(4):721-736(2018) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: Selenomonas sputigena, flagellin glycosylation, periodontitis, glycoproteomics, glycomics, LC-MSMS |
Contact List
Associate Professor Daniel Kolarich, PhD |
contact affiliation | Institute for Glycomics, Gold Coast Campus, Griffith University, QLD 4222, Australia |
contact email | d.kolarich@griffith.edu.au |
lab head | |
Daniel Kolarich |
contact affiliation | Griffith University, Institute for Glycomics |
contact email | d.kolarich@griffith.edu.au |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD005859
- Label: PRIDE project
- Name: Glycoproteomics of Flagellin C9LY14 from Selenomonas sputigena