PXD004429

PXD004429 is an original dataset announced via ProteomeXchange.

Title	Role of proteins belonging to the OMP biogenesis machinery for virulence of Yersinia enterocolitica
Description	The outer membrane (OM) of Gram-negative bacteria acts as a physical barrier protecting Gram-negative species from harmful environmental influences. At the same time it facilitates the import of nutrients, the export of proteins, the passage of signaling molecules and also harbors proteins associated with virulence. Transmembrane traffic particularly is facilitated by membrane-integral proteins. In order to insert these into the OM, an essential oligomeric membrane-associated protein complex, the beta-barrel assembly machinery (BAM) is required. Being essential for the biogenesis of outer membrane proteins (OMPs) the BAM and also periplasmic chaperones (termed the OMP biogenesis machinery as an entity herein) may serve as attractive targets to develop novel antimicrobial or antiinfective agents. We aimed to elucidate which proteins belonging to the OMP biogenesis machinery have the most important function in granting bacterial fitness, facilitating biogenesis of dedicated virulence factors and determination of overall virulence. To this end we used the enteropathogen Yersinia enterocolitica (Ye) as a model system. We individually knocked out all non-essential components of the BAM (BamB, C and E) as well as the periplasmic chaperones DegP, SurA and Skp. In summary, we found that the most profound phenotypes were produced by the loss of BamB or SurA with both knockouts resulting in significant attenuation or even avirulence of Ye in a mouse infection model. Thus, both BamB and SurA are promising targets for the development of new antimicrobials in the future.
HostingRepository	PRIDE
AnnounceDate	2018-10-17
AnnouncementXML	Submission_2018-10-17_00:39:51.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Nicolas Nalpas
SpeciesList	scientific name: Yersinia enterocolitica; NCBI TaxID: 630;
ModificationList	No PTMs are included in the dataset
Instrument	LTQ Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2016-06-23 05:45:47	ID requested
⏵ 1	2018-10-17 00:39:53	announced

Weirich J, Br, ä, utigam C, M, ü, hlenkamp M, Franz-Wachtel M, Macek B, Meuskens I, Skurnik M, Leskinen K, Bohn E, Autenrieth I, Sch, ü, tz M, Identifying components required for OMP biogenesis as novel targets for antiinfective drugs. Virulence, 8(7):1170-1188(2017) [pubmed]

submitter keyword: outer membrane protein biogenesis, bacterial infection, cell surface molecules

Monika Schütz
contact affiliation	Institut für Medizinische Mikrobiologie und Hygiene Universitätsklinikum Tübingen Elfriede-Aulhorn-Str. 6 72076 Tübingen Germany
contact email	monika.schuetz@med.uni-tuebingen.de
lab head
Nicolas Nalpas
contact affiliation	Tuebingen University
contact email	nalpas.nicolas@gmail.com
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/2018/10/PXD004429

PRIDE project URI

• PRIDE
  1. PXD004429
     1. Label: PRIDE project
     2. Name: Role of proteins belonging to the OMP biogenesis machinery for virulence of Yersinia enterocolitica