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Quorum quenching enzyme activity is widely conserved in the sera of mammalian species
Author(s) -
Yang Fan,
Wang Lian-Hui,
Wang Jing,
Dong Yi-Hu,
Hu Jiang Yong,
Zhang Lian-Hui
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.05.060
Subject(s) - quorum quenching , quorum sensing , homoserine , virulence , enzyme , pseudomonas aeruginosa , biochemistry , biology , microbiology and biotechnology , gene , chemistry , bacteria , genetics
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.