Regulation of the physiology and virulence of Ralstonia solanacearum by the second messenger 2′,3′-cyclic guanosine monophosphate

Xia Li, Wenfang Yin, Junjie Desmond Lin, Yong Zhang, Quan Guo, Gerun Wang, Xiayu Chen, Binbin Cui, Mingfang Wang, Min Chen, Peng Li, Ya-Wen He, Wei Qian, Haibin Luo, Lian-Hui Zhang, Xue-Wei Liu (), Shihao Song () and Yinyue Deng ()
Additional contact information
Xia Li: Shenzhen Campus of Sun Yat-sen University, Sun Yat-sen University
Wenfang Yin: South China Agricultural University
Junjie Desmond Lin: Nanyang Technological University
Yong Zhang: Southwest University
Quan Guo: Shenzhen Campus of Sun Yat-sen University, Sun Yat-sen University
Gerun Wang: Shenzhen Campus of Sun Yat-sen University, Sun Yat-sen University
Xiayu Chen: Shenzhen Campus of Sun Yat-sen University, Sun Yat-sen University
Binbin Cui: Shenzhen Campus of Sun Yat-sen University, Sun Yat-sen University
Mingfang Wang: Shenzhen Campus of Sun Yat-sen University, Sun Yat-sen University
Min Chen: Southwest University
Peng Li: Hainan Normal University
Ya-Wen He: Shanghai Jiao Tong University
Wei Qian: Chinese Academy of Sciences
Haibin Luo: Hainan University
Lian-Hui Zhang: South China Agricultural University
Xue-Wei Liu: Nanyang Technological University
Shihao Song: Hainan University
Yinyue Deng: Shenzhen Campus of Sun Yat-sen University, Sun Yat-sen University

Nature Communications, 2023, vol. 14, issue 1, 1-13

Abstract: Abstract Previous studies have demonstrated that bis-(3',5')-cyclic diguanosine monophosphate (bis-3',5'-c-di-GMP) is a ubiquitous second messenger employed by bacteria. Here, we report that 2',3'-cyclic guanosine monophosphate (2',3'-cGMP) controls the important biological functions, quorum sensing (QS) signaling systems and virulence in Ralstonia solanacearum through the transcriptional regulator RSp0980. This signal specifically binds to RSp0980 with high affinity and thus abolishes the interaction between RSp0980 and the promoters of target genes. In-frame deletion of RSp0334, which contains an evolved GGDEF domain with a LLARLGGDQF motif required to catalyze 2',3'-cGMP to (2',5')(3',5')-cyclic diguanosine monophosphate (2',3'-c-di-GMP), altered the abovementioned important phenotypes through increasing the intracellular 2',3'-cGMP levels. Furthermore, we found that 2',3'-cGMP, its receptor and the evolved GGDEF domain with a LLARLGGDEF motif also exist in the human pathogen Salmonella typhimurium. Together, our work provides insights into the unusual function of the GGDEF domain of RSp0334 and the special regulatory mechanism of 2',3'-cGMP signal in bacteria.

Date: 2023
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DOI: 10.1038/s41467-023-43461-2

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