PXD008528

PXD008528 is an original dataset announced via ProteomeXchange.

Title	Exoproteome profiling reveals the involvement of the foldase PrsA in the cell surface properties and pathogenesis of S. aureus
Description	Staphylococcus aureus is a bacterial pathogen that produces and exports many virulence factors that cause human diseases. PrsA, a membrane-bound foldase that is found ubiquitously in Gram-positive bacteria, is required for the folding of exported proteins into a stable and active structure. However, the involvement of PrsA in post-translocational protein folding in S. aureus remains unclear. In this study, a PrsA-deficient mutant of S. aureus HG001 was constructed and prsA deletion was shown to enhance auto-aggregation and increase the ability of S. aureus HG001 to adhere to human lung epithelial cells. The lack of PrsA made the bacteria more sensitive to sonication-induced lysis. In a mouse infection model, mice that were infected with a prsA-knockout strain HG001ΔprsA had a higher survival rate than those infected with the wild-type strain. An iTRAQ-based quantitative exoproteome analysis was conducted to identify the proteins whose secretion was affected by PrsA. The exoproteomic analysis revealed that prsA deletion altered the amounts of several proteins that were related to the properties of the cell surface and virulence. These include proteins involved in cellular adhesion and cell wall synthesis such as extracellular adhesion protein (Eap), undecaprenyl-diphosphatase (UppP) and FmtA, and proteins involved in subverting host innate immunity such as immunoglobulin-binding proteins Spa and Sbi, chemotaxis inhibitory protein (CHIP) and staphylococcal complement inhibitor (SCIN). The results of this study suggested that PrsA is required for the post-translocational folding of many exported proteins and critically affects the cell surface properties and pathogenesis of S. aureus.
HostingRepository	PRIDE
AnnounceDate	2018-01-24
AnnouncementXML	Submission_2018-01-25_01:37:02.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Chih-Ching Wu
SpeciesList	scientific name: Staphylococcus aureus; NCBI TaxID: 1280;
ModificationList	iTRAQ4plex-116 reporter+balance reagent acylated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2017-12-21 02:52:16	ID requested
⏵ 1	2018-01-25 01:37:03	announced

Lin MH, Li CC, Shu JC, Chu HW, Liu CC, Wu CC, Exoproteome Profiling Reveals the Involvement of the Foldase PrsA in the Cell Surface Properties and Pathogenesis of Staphylococcus aureus. Proteomics, 18(5-6):e1700195(2018) [pubmed]

curator keyword: Biological, Biomedical

submitter keyword: PrsA, S. ureus, iTRAQ

Chih-Ching Wu
contact affiliation	Department of Medical Biotechnology and Laboratory Sciences, College of Medicine, Chang Gung University, Taiwan
contact email	luckywu@mail.cgu.edu.tw
lab head
Chih-Ching Wu
contact affiliation	Department of Medical Biotechnology and Laboratory Science, College of Medicine, Chang Gung University
contact email	luckywu@mail.cgu.edu.tw
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/2018/01/PXD008528

PRIDE project URI

• PRIDE
  1. PXD008528
     1. Label: PRIDE project
     2. Name: Exoproteome profiling reveals the involvement of the foldase PrsA in the cell surface properties and pathogenesis of S. aureus