Dioxygenase-Mediated Quenching of Quinolone-Dependent Quorum Sensing in Pseudomonas aeruginosa

被引：89

作者：

Pustelny, Christian ^{[1
]}

Albers, Alexander ^{[2
]}

Bueldt-Karentzopoulos, Klaudia ^{[2
]}

Parschat, Katja ^{[2
]}

Chhabra, Siri Ram ^{[1
]}

Camara, Miguel ^{[1
]}

Williams, Paul ^{[1
]}

Fetzner, Susanne ^{[2
]}

机构：

[1] Univ Nottingham, Sch Mol Med Sci, Ctr Biomol Sci, Nottingham NG7 2RD, England

[2] Westfalian Wilhelms Univ Muenster, Inst Mol Microbiol & Biotechnol, D-48149 Munster, Germany

来源：

CHEMISTRY & BIOLOGY | 2009年 / 16卷 / 12期

基金：

英国生物技术与生命科学研究理事会;

关键词：

ARTHROBACTER-NITROGUAJACOLICUS RU61A; HYDROLASE-FOLD SUPERFAMILY; HOMOSERINE LACTONE ACYLASE; TO-CELL COMMUNICATION; 1H-3-HYDROXY-4-OXOQUINALDINE 2,4-DIOXYGENASE; CYSTIC-FIBROSIS; SIGNAL MOLECULES; VIRULENCE GENE; ANTHRANILATE; SYSTEM;

D O I：

10.1016/j.chembiol.2009.11.013

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：

2-Heptyl-3-hydroxy-4(1H)-quinolone (PQS) is a quorum-sensing signal molecule used by Pseudomonas aeruginosa. The structural similarity between 3-hydroxy-2-methyl-4(1H)-quinolone, the natural substrate for the 2,4-dioxygenase, Hod, and PQS prompted us to investigate whether Hod quenched PQS signaling. Hod is capable of catalyzing the conversion of PQS to N-octanoylanthranilic acid and carbon monoxide. In P. aeruginosa PAO1 cultures, exogenously supplied Hod protein reduced expression of the PQS biosynthetic gene pqsA, expression of the PQS-regulated virulence determinants lectin A, pyocyanin, and rhamnolipids, and virulence in planta. However, the proteolytic cleavage of Hod by extracellular proteases, competitive inhibition by the PQS precursor 2-heptyl-4(1H)-quinolone, and PQS binding to rhamnolipids reduced the efficiency of Hod as a quorum-quenching agent. Nevertheless, these data indicate that enzyme-mediated PQS inactivation has potential as an antivirulence strategy against P. aeruginosa.

引用

页码：1259 / 1267

页数：9

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