PXD006086

PXD006086 is an original dataset announced via ProteomeXchange.

Title	LC-MS/MS of the secreted fraction of Shigella
Description	Many human Gram-negative bacterial pathogens express a Type Three Secretion Apparatus (T3SA), including among the most notorious Shigella spp., Salmonella enterica, Yersinia enterocolitica and enteropathogenic Escherichia coli (EPEC). These bacteria express on their surface multiple copies of the T3SA that mediate the delivery into host cells of specific protein substrates critical to pathogenesis. Shigella spp. are Gram-negative bacterial pathogens responsible for human bacillary dysentery. The effector function of several Shigella T3SA substrates has largely been studied but their potential cellular targets are far from having been comprehensively delineated. In addition, it is likely that some T3SA substrates have escaped scrutiny as yet. Indeed, sequencing of the virulence plasmid of Shigella flexneri has revealed numerous open reading frames with unknown functions that could encode additional T3SA substrates. Taking advantage of label-free mass spectrometry detection of proteins secreted by a constitutively secreting strain of S. flexneri, we identified five novel substrates of the T3SA. We further confirmed their secretion through the T3SA and translocation into host cells using b-lactamase assays. The coding sequences of two of these novel T3SA substrates (Orf13 and Orf131a) have a guanine-cytosine content comparable to those of T3SA components and effectors. The three other T3SA substrates identified (Orf48, Orf86 and Orf176) have significant homology with antitoxin moieties of type II Toxin-Antitoxin systems usually implicated in the maintenance of low copy plasmids. While Orf13 and Orf131a might constitute new virulence effectors contributing to S. flexneri pathogenicity, potential roles for the translocation into host cells of antitoxins or antitoxin-like proteins during Shigella infection are discussed.
HostingRepository	PRIDE
AnnounceDate	2017-10-17
AnnouncementXML	Submission_2017-11-06_00:50:31.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Nico Jehmlich
SpeciesList	scientific name: Shigella flexneri; NCBI TaxID: 623;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2017-03-14 02:30:53	ID requested
1	2017-10-17 08:09:41	announced
⏵ 2	2017-11-06 00:50:32	announced	Updated publication reference for PubMed record(s): 29073283.

Pinaud L, Ferrari ML, Friedman R, Jehmlich N, von Bergen M, Phalipon A, Sansonetti PJ, Campbell-Valois FX, Identification of novel substrates of Shigella T3SA through analysis of its virulence plasmid-encoded secretome. PLoS One, 12(10):e0186920(2017) [pubmed]

curator keyword: Biological

submitter keyword: Gram-negative bacterial pathogens, Shigella, Proteomics, Plasmid

Nico Jehmlich
contact affiliation	Department Molekulare Systembiologie Helmholtz-Zentrum für Umweltforschung GmbH - UFZ Permoserstraße 15 | 04318 Leipzig
contact email	nico.jehmlich@ufz.de
lab head
Nico Jehmlich
contact affiliation	Helmholtz-Centre for Environmental Research - UFZ
contact email	nico.jehmlich@ufz.de
dataset submitter

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/2017/10/PXD006086

PRIDE project URI

• PRIDE
  1. PXD006086
     1. Label: PRIDE project
     2. Name: LC-MS/MS of the secreted fraction of Shigella