A Rhodococcus qsdA-encoded enzyme defines a novel class of large-spectrum quorum-quenching lactonases.
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 C(6) to C(14), 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.
Uroz
Stéphane
S
Interactions Plantes et Microorganismes de Rhizosphère, Institut des Sciences du Végétal, CNRS, Avenue de Terrasse, 91198 Gif-sur-Yvette Cedex, France.
Oger
Phil M
PM
Chapelle
Emilie
E
Adeline
Marie-Thérèse
MT
Faure
Denis
D
Dessaux
Yves
Y
D015107:4-Butyrolactone / Q000031:analogs & derivatives / Q000378:metabolism; D001483:Base Sequence; D002851:Chromatography, High Pressure Liquid; D003001:Cloning, Molecular; D017931:DNA Primers; D015723:Gene Library; D008956:Models, Chemical; D008969:Molecular Sequence Data; D015394:Molecular Structure; D044345:Phosphoric Triester Hydrolases / Q000235:genetics*; D053038:Quorum Sensing / Q000235:genetics*; D012240:Rhodococcus / Q000201:enzymology*; D017422:Sequence Analysis, DNA
D017931:DNA Primers; C088386:homoserine lactone; D044345:Phosphoric Triester Hydrolases; D015107:4-Butyrolactone