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PXD015752

PXD015752 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleArg-GlcNAcylation of GshB, An intra-bacterial activity for a T3SS effector
DescriptionMany 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.
HostingRepositoryPRIDE
AnnounceDate2024-10-22
AnnouncementXMLSubmission_2024-10-22_04:05:47.003.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterNichollas Scott
SpeciesList scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationListcomplex glycosylation
InstrumentOrbitrap Fusion Lumos; LTQ Orbitrap Elite
Dataset History
RevisionDatetimeStatusChangeLog Entry
02019-10-09 01:23:48ID requested
12020-01-14 00:00:38announced
22024-10-22 04:05:47announced2024-10-22: 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 affiliationCollege of Veterinary Medicine, Kansas State University, Manhattan, KS, United States
contact emailhardwidg@vet.k-state.edu
lab head
Nichollas Scott
contact affiliationUniversity of Melbourne
contact emailnichollas.scott@unimelb.edu.au
dataset submitter
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Dataset FTP location
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PRIDE project URI
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