Cis-2-dodecenoic acid receptor RpfR links quorum-sensing signal perception with regulation of virulence through cyclic dimeric guanosine monophosphate turnover

被引：131

作者：

Deng, Yinyue ^{[1
]}

Schmid, Nadine ^{[2
]}

Wang, Chao ^{[1
]}

Wang, Jianhe ^{[1
]}

Pessi, Gabriella ^{[2
]}

Wu, Donghui ^{[1
]}

Lee, Jasmine ^{[1
]}

Aguilar, Claudio ^{[2
]}

Ahrens, Christian H. ^{[3
]}

Chang, Changqing ^{[1
]}

Song, Haiwei ^{[1
]}

Eberl, Leo ^{[2
]}

Zhang, Lian-Hui ^{[1
]}

机构：

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

[2] Univ Zurich, Dept Microbiol, CH-8008 Zurich, Switzerland

[3] Univ Zurich, Inst Mol Life Sci, CH-8057 Zurich, Switzerland

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2012年 / 109卷 / 38期

基金：

瑞士国家科学基金会;

关键词：

signal transduction; second messenger; molecular recognition; pathogenesis; cell-cell communication; CELL-CELL COMMUNICATION; GYP DOMAIN PROTEIN; DI-GMP EFFECTORS; XANTHOMONAS-CAMPESTRIS; BURKHOLDERIA-CENOCEPACIA; CAENORHABDITIS-ELEGANS; PSEUDOMONAS-AERUGINOSA; CLP DEFINES; SYSTEM; PATHOGENICITY;

D O I：

10.1073/pnas.1205037109

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Many bacterial pathogens produce diffusible signal factor (DSF)-type quorum sensing (QS) signals in modulation of virulence and biofilm formation. Previous work on Xanthomonas campestris showed that the RpfC/RpfG two-component system is involved in sensing and responding to DSF signals, but little is known in other microorganisms. Here we show that in Burkholderia cenocepacia the DSF-family signal cis-2-dodecenoic acid (BDSF) negatively controls the intracellular cyclic dimeric guanosine monophosphate (c-di-GMP) level through a receptor protein RpfR, which contains Per/Arnt/Sim (PAS)-GGDEF-EAL domains. RpfR regulates the same phenotypes as BDSF including swarming motility, biofilm formation, and virulence. In addition, the BDSF-mutant phenotypes could be rescued by in trans expression of RpfR, or its EAL domain that functions as a c-di-GMP phosphodiesterase. BDSF is shown to bind to the PAS domain of RpfR with high affinity and stimulates its phosphodiesterase activity through induction of allosteric conformational changes. Our work presents a unique and widely conserved DSF-family signal receptor that directly links the signal perception to c-di-GMP turnover in regulation of bacterial physiology.

引用

页码：15479 / 15484

页数：6

共 35 条

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