PXD015752 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Arg-GlcNAcylation of GshB, An intra-bacterial activity for a T3SS effector |
Description | Many Gram-negative bacterial pathogens interact with mammalian cells by using type III secretion systems (T3SS) to inject virulence proteins directly into infected host cells. A subset of these injected protein ‘effectors’ are enzymes that modify the structure and inhibit the function of human proteins by catalyzing the addition of unusual post-translational modifications. T3SS effectors play essential roles in bacterial virulence and their modes of action have provided great insight into the functions and the components of the innate immune system. The E. coli and Citrobacter rodentium NleB effectors, as well as the Salmonella enterica SseK effectors are glycosyltransferases that modify host protein substrates with N-acetyl glucosamine (GlcNAc) on arginine residues. Arginine glycosylation is unusual because it occurs on the guanidinium groups of arginines, which are poor nucleophiles. This post-translational modification disrupts the normal functioning of host immune response proteins. T3SS effectors are chaperoned in the bacterium to keep the effectors partially unfolded and competent for secretion, as well as for targeting the effectors to the T3SS sorting platform. The chaperones are then stripped from their effector substrates at the sorting platform and the effectors are secreted in an unfolded conformation. T3SS effectors are thought to be inactive within the bacterium and fold into their active conformations after they are injected into host cells. While performing mass spectrometry experiments to identify glycosylation substrates of NleB orthologs, we unexpectedly observed that the E. coli glutathione synthetase (GshB) is glycosylated on an arginine residue (R256) by NleB. NleB glycosyltransferase activity is essential to C. rodentium survival in oxidative stress conditions because glycosylation of GshB results in enhanced glutathione production. These data represent, to our knowledge, the first intra-bacterial activity for a T3SS effector and show that effector activities thought to be restricted to host cell compartments additionally play important roles in regulating bacterial physiology. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_04:05:47.003.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Nichollas Scott |
SpeciesList | scientific name: Escherichia coli; NCBI TaxID: 562; |
ModificationList | complex glycosylation |
Instrument | Orbitrap Fusion Lumos; LTQ Orbitrap Elite |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2019-10-09 01:23:48 | ID requested | |
1 | 2020-01-14 00:00:38 | announced | |
⏵ 2 | 2024-10-22 04:05:47 | announced | 2024-10-22: Updated project metadata. |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: Citrobacter rodentium, EHEC, NleB,Glycosylation, EPEC, effectors |
Contact List
Philip R. Hardwidge |
contact affiliation | College of Veterinary Medicine, Kansas State University, Manhattan, KS, United States |
contact email | hardwidg@vet.k-state.edu |
lab head | |
Nichollas Scott |
contact affiliation | University of Melbourne |
contact email | nichollas.scott@unimelb.edu.au |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD015752
- Label: PRIDE project
- Name: Arg-GlcNAcylation of GshB, An intra-bacterial activity for a T3SS effector