| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2052440 | FEBS Letters | 2005 | 5 Pages |
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.
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Authors
Fan Yang, Lian-Hui Wang, Jing Wang, Yi-Hu Dong, Jiang Yong Hu, Lian-Hui Zhang,