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Quorum quenching enzyme activity is widely conserved in the sera of mammalian species
Authors:Yang Fan  Wang Lian-Hui  Wang Jing  Dong Yi-Hu  Hu Jiang Yong  Zhang Lian-Hui
Institution:Institute of Molecular and Cell Biology, 61 Biopolis Drive, Singapore 138673.
Abstract:Acyl-homoserine lactone (AHL) quorum sensing signals play a key role in synchronizing virulence gene expression in Pseudomonas aeruginosa, which could cause fatal bloodstream infections. We showed that AHL inactivation activity, albeit with variable efficiency, was conserved in the serum samples of all the 6 tested mammalian animals. High-performance liquid chromatography and mass spectrometry analyses revealed that mammalian sera had a lactonase-like enzyme(s), which hydrolyzed the lactone ring of AHL to produce acyl homoserine, with enzyme properties reminiscent of paraoxonases (PONs). We further showed that the animal cell lines expressing three mouse PON genes, respectively, displayed strong AHL degradation activities.
Keywords:Quorum sensing  Acyl-homoserine lactone  AHL-lactonase  Paraoxonase  PON enzymes  Pseudomonas aeruginosa
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