Quorum quenching enzyme activity is widely conserved in the sera of mammalian species.
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.
Yang
Fan
F
Institute of Molecular and Cell Biology, 61 Biopolis Drive, Singapore 138673.
Wang
Lian-Hui
LH
Wang
Jing
J
Dong
Yi-Hu
YH
Hu
Jiang Yong
JY
Zhang
Lian-Hui
LH
D015107:4-Butyrolactone / Q000031:analogs & derivatives* / Q000378:metabolism; D000818:Animals; D043303:Aryldialkylphosphatase / Q000235:genetics / Q000378:metabolism; D016466:CHO Cells; D002265:Carboxylic Ester Hydrolases / Q000097:blood*; D002460:Cell Line; D006224:Cricetinae; D003412:Cricetulus; D051379:Mice; D011550:Pseudomonas aeruginosa / Q000378:metabolism*; D011817:Rabbits; D013379:Substrate Specificity; D014774:Virulence
C088386:homoserine lactone; D002265:Carboxylic Ester Hydrolases; C432003:N-acyl homoserine lactonase; D043303:Aryldialkylphosphatase; D015107:4-Butyrolactone