PXD006172

PXD006172 is an original dataset announced via ProteomeXchange.

Title	Chemical probes unravel an antimicrobial defense response triggered by binding of the human opioid dynorphin to a bacterial sensor kinase
Description	Host-microbe communication via small molecule signals is often poorly understood at the molecular level. Under conditions of host stress, levels of the human opioid peptide dynorphin are elevated, triggering virulence in the opportunistic pathogenic bacterium Pseudomonas aeruginosa (PAO1) via an unknown pathway. Here we apply multiple chemical biology strategies to unravel the mode of action of this putative interkingdom signal. We designed and applied dynorphin-inspired photoaffinity probes (DYN4 and DYN5) to reveal the protein targets of the peptide in live bacteria via chemical proteomics. Sensor kinase ParS was identified as a potential hit. Subsequent full proteome studies revealed that dynorphin(1-13) (DYN) induces an antimicrobial peptide-like response in Pseudomonas, with specific upregulation of membrane defence mechanisms (datasets Stat.10 and Exp.5). No such response was observed in a parS mutant (Stat.1), functionally linking DYN engagement with ParS to this phenotype.
HostingRepository	PRIDE
AnnounceDate	2017-04-03
AnnouncementXML	Submission_2017-04-03_02:40:56.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Megan Wright
SpeciesList	scientific name: Pseudomonas aeruginosa PAO1; NCBI TaxID: 208964;
ModificationList	iodoacetamide derivatized residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2017-03-27 01:45:48	ID requested
⏵ 1	2017-04-03 02:40:57	announced

Wright MH, Fetzer C, Sieber SA, Chemical Probes Unravel an Antimicrobial Defense Response Triggered by Binding of the Human Opioid Dynorphin to a Bacterial Sensor Kinase. J Am Chem Soc, 139(17):6152-6159(2017) [pubmed]

curator keyword: Biological, Biomedical

submitter keyword: Pseudomonas aeruginosa, Host-Microbe Communication, Photoaffinity Probes

Stephan A. Sieber
contact affiliation	Technische Universität München Chair of Organic Chemistry II Center for Integrated Protein Science (CIPSM) Lichtenbergstrasse 4 85748 Garching, Germany
contact email	stephan.sieber@mytum.de
lab head
Megan Wright
contact affiliation	University of Leeds
contact email	m.h.wright@leeds.ac.uk
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/2017/04/PXD006172

PRIDE project URI

• PRIDE
  1. PXD006172
     1. Label: PRIDE project
     2. Name: Chemical probes unravel an antimicrobial defense response triggered by binding of the human opioid dynorphin to a bacterial sensor kinase