Detection and Analysis of Quorum‐Quenching Enzymes Against Acyl Homoserine Lactone Quorum‐Sensing Signals

ABSTRACTSsoPox, a bifunctional enzyme with organophosphate hydrolase andN-acyl homoserine lactonase activities from the hyperthermophilic archaeonSulfolobus solfataricus, was overexpressed and purified from recombinantPseudomonas putidaKT2440 with a yield of 9.4 mg of protein per liter of culture. The enzyme has a preference forN-acyl homoserine lactones (AHLs) with acyl chain lengths of at least 8 carbon atoms, mainly due to lowerKmvalues for these substrates. The highest specificity constant obtained was forN-3-oxo-decanoyl homoserine lactone (kcat/Km= 5.5 × 103M−1·s−1), but SsoPox can also degradeN-butyryl homoserine lactone (C4-HSL) andN-oxo-dodecanoyl homoserine lactone (oxo-C12-HSL), which are important for quorum sensing in ourPseudomonas aeruginosamodel system. WhenP. aeruginosaPAO1 cultures were grown in the presence of SsoPox-immobilized membranes, the production of C4-HSL- and oxo-C12-HSL-regulated virulence factors, elastase, protease, and pyocyanin were significantly reduced. This is the first demonstration that immobilized quorum-quenching enzymes can be used to attenuate the production of virulence factors controlled by quorum-sensing signals.

Download Full-text

Perception and Degradation ofN-Acyl Homoserine Lactone Quorum Sensing Signals by Mammalian and Plant Cells

Chemical Reviews ◽

10.1021/cr100045m ◽

2011 ◽

Vol 111 (1) ◽

pp. 100-116 ◽

Cited By ~ 121

Author(s):

Max Teplitski ◽

Ulrike Mathesius ◽

Kendra P. Rumbaugh

Keyword(s):

Quorum Sensing ◽

Plant Cells ◽

Homoserine Lactone ◽

Acyl Homoserine Lactone ◽

Quorum Sensing Signals

Download Full-text

In vivo effects of single or combined N-acyl homoserine lactone quorum sensing signals on the performance of Macrobrachium rosenbergii larvae

Aquaculture ◽

10.1016/j.aquaculture.2008.11.034 ◽

2009 ◽

Vol 288 (3-4) ◽

pp. 233-238 ◽

Cited By ~ 29

Author(s):

Kartik Baruah ◽

Dang T.V. Cam ◽

Kristof Dierckens ◽

Mathieu Wille ◽

Tom Defoirdt ◽

...

Keyword(s):

Quorum Sensing ◽

Macrobrachium Rosenbergii ◽

Homoserine Lactone ◽

Acyl Homoserine Lactone ◽

In Vivo Effects ◽

Quorum Sensing Signals

Download Full-text

A Rhodococcus qsdA-Encoded Enzyme Defines a Novel Class of Large-Spectrum Quorum-Quenching Lactonases

Applied and Environmental Microbiology ◽

10.1128/aem.02014-07 ◽

2008 ◽

Vol 74 (5) ◽

pp. 1357-1366 ◽

Cited By ~ 120

Author(s):

Stéphane Uroz ◽

Phil M. Oger ◽

Emilie Chapelle ◽

Marie-Thérèse Adeline ◽

Denis Faure ◽

...

Keyword(s):

Quorum Sensing ◽

Genomic Library ◽

Acyl Chain ◽

Rhodococcus Erythropolis ◽

Quorum Quenching ◽

Homoserine Lactone ◽

Acyl Homoserine Lactone ◽

Degrading Enzymes ◽

Regulated Functions ◽

The Relationship

ABSTRACT A gene involved in N-acyl homoserine lactone (N-AHSL) degradation was identified by screening a genomic library of Rhodococcus erythropolis strain W2. This gene, named qsdA (for quorum-sensing signal degradation), encodes an N-AHSL lactonase unrelated to the two previously characterized N-AHSL-degrading enzymes, i.e., the lactonase AiiA and the amidohydrolase AiiD. QsdA is related to phosphotriesterases and constitutes the reference of a novel class of N-AHSL degradation enzymes. It confers the ability to inactivate N-AHSLs with an acyl chain ranging from C6 to C14, with or without substitution at carbon 3. Screening of a collection of 15 Rhodococcus strains and strains closely related to this genus clearly highlighted the relationship between the ability to degrade N-AHSLs and the presence of the qsdA gene in Rhodococcus. Bacteria harboring the qsdA gene interfere very efficiently with quorum-sensing-regulated functions, demonstrating that qsdA is a valuable tool for developing quorum-quenching procedures.

Download Full-text