Quorum quenching enzyme activity is widely conserved in the sera of mammalian species

被引：167

作者：

Yang, F

Wang, LH

Wang, J

Dong, YH

Hu, JY

Zhang, LH

机构：

[1] Natl Univ Singapore, Dept Civil Engn, Water Res Ctr, Singapore 119260, Singapore

[2] Inst Mol & Cell Biol, Singapore 138673, Singapore

来源：

FEBS LETTERS | 2005年 / 579卷 / 17期

关键词：

quorum sensing; acyl-homoserine lactone; AHL-lactonase; paraoxonase; PON enzymes; Pseudomonas aeruginosa;

D O I：

10.1016/j.febslet.2005.05.060

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

收藏

页码：3713 / 3717

页数：5

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