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Acyl-homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum-quenching enzymes

Lin, Yi-Han and Xu, Jin-Ling and Hu, Jiangyong and Wang, Lian-Hui and Ong, Say Leong and Leadbetter, Jared Renton and Zhang, Lian-Hui (2003) Acyl-homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum-quenching enzymes. Molecular Microbiology, 47 (3). pp. 849-860. ISSN 0950-382X. http://resolver.caltech.edu/CaltechAUTHORS:20111018-090155298

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Abstract

N -acylhomoserine lactones (AHLs) are used as signal molecules by many quorum-sensing Proteobacteria. Diverse plant and animal pathogens use AHLs to regulate infection and virulence functions. These signals are subject to biological inactivation by AHL-lactonases and AHL-acylases. Previously, little was known about the molecular details underlying the latter mechanism. An AHL signal-inactivating bacterium, identified as a Ralstonia sp., was isolated from a mixed-species biofilm. The signal inactivation encoding gene from this organism, which we call aiiD , was cloned and successfully expressed in Escherichia coli and inactivated three AHLs tested. The predicted 794-amino-acid polypeptide was most similar to the aculeacin A acylase (AAC) from Actinoplanes utahensis and also shared significant similarities with cephalosporin acylases and other N-terminal (Ntn) hydrolases. However, the most similar homologues of AiiD are deduced proteins of undemonstrated function from available Ralstonia , Deinococcus and Pseudomonas genomes. LC-MS analyses demonstrated that AiiD hydrolyses the AHL amide, releasing homoserine lactone and the corresponding fatty acid. Expression of AiiD in Pseudomonas aeruginosa PAO1 quenched quorum sensing by this bacterium, decreasing its ability to swarm, produce elastase and pyocyanin and to paralyse nematodes. Thus, AHL-acylases have fundamental implications and hold biotechnological promise in quenching quorum sensing.


Item Type:Article
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http://dx.doi.org/10.1046/j.1365-2958.2003.03351.xDOIUNSPECIFIED
http://onlinelibrary.wiley.com/doi/10.1046/j.1365-2958.2003.03351.x/abstractPublisherUNSPECIFIED
Additional Information:© 2003 Blackwell Publishing Ltd. Accepted 1 November, 2002. Article first published online: 15 Jan. 2003. We thank A. Kerr and M. Tate for critical review of the manuscript. This work was supported by the Agency for Science and Technology and Research, Singapore (L.-H.Z.) and by the US Department of Agriculture, Soils and Soil Biology Program (no. 2001-01242; J.R.L.).
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Funding AgencyGrant Number
Agency for Science, Technology and ResearchUNSPECIFIED
Department of Agriculture Soils and Soil Biology Program2001-01242
Record Number:CaltechAUTHORS:20111018-090155298
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20111018-090155298
Official Citation:Lin, Y.-H., Xu, J.-L., Hu, J., Wang, L.-H., Ong, S. L., Leadbetter, J. R. and Zhang, L.-H. (2003), Acyl-homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum-quenching enzymes. Molecular Microbiology, 47: 849–860. doi: 10.1046/j.1365-2958.2003.03351.x
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:27270
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:24 Oct 2011 22:58
Last Modified:24 Oct 2011 22:58

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