PXD007278
PXD007278 is an original dataset announced via ProteomeXchange.
Dataset Summary
Title | Comprehensive redox profiling of the thiol proteome of Clostridium difficile |
Description | The strictly anaerobic bacterium C. difficile has become one of the most problematic hospital acquired pathogens and a major burden for health care systems. Although antibiotics work effectively in most C. difficile infections (CDIs), their detrimental effect on the intestinal microbiome paves the way for recurrent episodes of CDI. To develop alternative, non-antibiotics-based treatment strategies, deeper knowledge on the physiology of C. difficile, stress adaptation mechanisms and regulation of virulence factors is mandatory. Focus of this work was to tackle the thiol proteome of C. difficile and its stress-induced alterations, since recent research reported the amino acid cysteine to play a central role in the metabolism of the pathogen. We developed a novel cysteine labeling approach to determine the redox state of protein thiols on a global scale. Applicability of the technique was demonstrated by inducing disulfide stress using the chemical diamide. The method can be transferred to any kind of redox challenge and was applied in this work to assess the effect of bile acids on the thiol proteome of C. difficile. We present redox-quantification of more than 1,500 thiol peptides and discuss the general difficulty of redox analyses of peptides possessing more than a single cysteine residue. The presented method will be especially useful when not only redox status shall be determined, but information on protein quantity is needed as well. Not least, our comprehensive dataset reveals protein cysteine sites particularly susceptible to oxidation and builds a groundwork for redox proteomics studies in C. difficile. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_04:14:17.658.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Susanne Sievers |
SpeciesList | scientific name: Peptoclostridium difficile (strain 630) (Clostridium difficile); NCBI TaxID: 272563; |
ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | LTQ Orbitrap Velos; LTQ Orbitrap Elite |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
---|---|---|---|
0 | 2017-08-16 00:47:15 | ID requested | |
1 | 2018-03-05 00:22:33 | announced | |
⏵ 2 | 2024-10-22 04:14:18 | announced | 2024-10-22: Updated project metadata. |
Publication List
10.1074/mcp.tir118.000671; |
Sievers S, Dittmann S, Jordt T, Otto A, Hochgr, รค, fe F, Riedel K, . Mol Cell Proteomics, 17(5):1035-1046(2018) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: thiol redox proteomics, Clostridium difficile |
Contact List
Susanne Sievers | |
---|---|
contact affiliation | Institute of Microbiology, Department of Microbial Physiology & Molecular Biology, University of Greifswald, Felix-Hausdorff Str. 8, 17489 Greifswald, phone: ++49 3834 420 5913 |
contact email | susanne.sievers@uni-greifswald.de |
lab head | |
Susanne Sievers | |
contact affiliation | University of Greifswald |
contact email | susanne.sievers@uni-greifswald.de |
dataset submitter |
Full Dataset Link List
Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2018/03/PXD007278 |
PRIDE project URI |
Repository Record List
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