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Applied and Environmental Microbiology, March 2008, p. 1357-1366, Vol. 74, No. 5
0099-2240/08/$08.00+0 doi:10.1128/AEM.02014-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.
,
Phil M. Oger,2*
Emilie Chapelle,1
Marie-Thérèse Adeline,3
Denis Faure,1 and
Yves Dessaux1
Interactions Plantes et Microorganismes de la Rhizosphère, Institut des Sciences du Végétal, CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette Cedex,1 Laboratoire de Sciences de la Terre, UMR CNRS 5570, Ecole Normale Supérieure, 46, Allée d'Italie, 69364 Lyon Cedex,2 Institut de Chimie des Substances Naturelles, CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette Cedex, France3
Received 3 September 2007/ Accepted 22 December 2007
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.
Published ahead of print on 11 January 2008.
Supplemental material for this article may be found at http://aem.asm.org/.
Present address: Interactions Arbres Microorganismes, INRA, 54280 Champenoux, France.
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