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• W2141368045 abstract "ABSTRACT Here we report the isolation and characterization of three metagenome-derived clones that interfere with bacterial quorum sensing and degrade N -(3-oxooctanoyl)- l -homoserine lactone (3-oxo-C 8 -HSL). By using a traI-lacZ gene fusion, the metagenome-derived clones were identified from a soil DNA library and analyzed. The open reading frames linked to the 3-oxo-C 8 -HSL-degrading activities were designated bpiB01, bpiB04, and bpiB07. While the BpiB07 protein was similar to a known lactonase, no significant similarities were observed for the BpiB01 and BpiB04 proteins or the deduced amino acid sequences. High-performance liquid chromatography-mass spectrometry analyses confirmed that the identified genes encode novel lactone-hydrolyzing enzymes. The original metagenome-derived clones were expressed in Pseudomonas aeruginosa and employed in motility and biofilm assays. All clones were able to reproducibly inhibit motility in P . aeruginosa . Furthermore, these genes clearly inhibited biofilm formation in P . aeruginosa when expressed in P . aeruginosa PAO1. Thus, this is the first study in which metagenome-derived proteins have been expressed in P . aeruginosa to successfully inhibit biofilm formation." @default.
• W2141368045 created "2016-06-24" @default.
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• W2141368045 date "2009-01-01" @default.
• W2141368045 modified "2023-10-03" @default.
• W2141368045 title "Metagenome-Derived Clones Encoding Two Novel Lactonase Family Proteins Involved in Biofilm Inhibition in <i>Pseudomonas aeruginosa</i>" @default.
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• W2141368045 doi "https://doi.org/10.1128/aem.01389-08" @default.
• W2141368045 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2612230" @default.
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