PXD017421

PXD017421 is an original dataset announced via ProteomeXchange.

Title	Lactonase Specificity is Key to Quorum Quenching in Pseudomonas aeruginosa
Description	The human opportunistic pathogen Pseudomonas aeruginosa orchestrates the expression of many genes in a cell density-dependent manner by using a molecular communication system referred to as quorum sensing (QS). This bacterium uses an intricate network of regulators and QS molecules known as autoinducers. Among these autoinducers are two acyl-homoserine lactones (AHL) involved in QS circuits which modulate virulence factors production, biofilm formation, and antimicrobial sensitivity. Disrupting QS, a strategy referred to as quorum quenching (QQ), is a promising approach to modulate virulence while not directly challenging bacterial survival. For P. aeruginosa, QQ can be achieved using exogenous AHL-degrading lactonases. However, the importance of enzyme specificity on quenching efficacy has never been investigated. Here, we used two lactonases both targeting the signal molecules N-(3-oxododecanoyl)-L-Homoserine lactone (3-oxo-C12 HSL) and butyryl-homoserine lactone (C4 HSL) albeit with different efficacy on C4 HSL. Interestingly, both lactonases similarly decreased the concentrations of AHL and comparably impacted the expression of AHL-based circuits. Conversely, strong variations were observed in Pseudomonas Quinolone Signal (PQS) regulation. Both lactonases were then found to decrease virulence factors production and biofilm formation in vitro, albeit with different efficiencies. Unexpectedly, only the lactonase with substrate preference for 3-oxo-C12 HSL was able to inhibit P. aeruginosa pathogenicity in vivo in an amoeba infection model. Similarly, large variations between lactonases were observed in proteins involved in antibiotic resistance, biofilm formation, virulence and diverse cellular mechanisms. This global analysis provides the first evidence that QQ enzyme specificity is crucial to modulate QS-associated behavior in P. aeruginosa PA14.
HostingRepository	PRIDE
AnnounceDate	2020-05-27
AnnouncementXML	Submission_2020-05-26_16:52:01.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	DECLOQUEMENT Philippe
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	No PTMs are included in the dataset
Instrument	Synapt MS

Revision	Datetime	Status	ChangeLog Entry
0	2020-02-06 08:03:22	ID requested
⏵ 1	2020-05-26 16:52:02	announced

R, é, my B, Plener L, Decloquement P, Armstrong N, Elias M, Daud, é D, Chabri, è, re É, . Front Microbiol, 11():762(2020) [pubmed]

submitter keyword: Quorum quenching (QQ), Quorum Sensing (QS), Lactonase, Virulence, Pseudomonas aeruginosa, AHL (N-acyl-homoserine lactone), LC-MSMS

Chabrière Eric
contact affiliation	Responsable plateforme protéomique et analyse fonctionnelle des proteines IHU Mediterranée infection Marseille FRANCE
contact email	eric.chabriere@univ-amu.fr
lab head
DECLOQUEMENT Philippe
contact affiliation	IHU
contact email	philippe.decloquement@univ-amu.fr
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/2020/05/PXD017421

PRIDE project URI

• PRIDE
  1. PXD017421
     1. Label: PRIDE project
     2. Name: Lactonase Specificity is Key to Quorum Quenching in Pseudomonas aeruginosa