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The cyclic AMP (cAMP) phosphodiesterase CpdA required for growth, biofilm formation, motility and pathogenicity of Edwardsiella piscicida

文献类型： 外文期刊

作者： Cai, Yidong 1 ; Dong, Jinggang 2 ; Huang, Jianqiang 7 ; He, Jiaojiao 1 ; Hu, Yonghua 2 ; Sui, Zhihai 4 ; Tang, Ping 5 ;

作者机构： 1.Hainan Univ, Sch Life & Hlth, Haikou 570228, Peoples R China

2.Chinese Acad Trop Agr Sci, Inst Trop Biosci & Biotechnol, Key Lab Biol & Genet Resources Trop Crops, Haikou 571101, Peoples R China

3.Hainan Inst Trop Agr Resources, Key Lab Biol & Genet Resources Trop Crops Hainan P, Haikou 571101, Peoples R China

4.Linyi Univ, Sch Life Sci, Linyi 276000, Peoples R China

5.Yunnan Agr Univ, Coll Plant Protect, State Key Lab Conservat & Utilizat Biol Resources, Kunming 650201, Peoples R China

6.Hainan Prov Key Lab Funct Components Res & Utiliza, Haikou 571101, Peoples R China

7.Chinese Acad Trop Agr Sci, Zhanjiang Expt Stn, Zhanjiang 524013, Peoples R China

8.west Side north Sect Ind Ave, Linyi, Shandong, Peoples R China

9.95 Heijin Rd, Kunming, Yunnan, Peoples R China

关键词： Edwardsiella piscicida; cAMP phosphodiesterase; Biofilm formation; Motility; Pathogenicity

期刊名称：MICROBIAL PATHOGENESIS （ 影响因子：3.8； 五年影响因子：4.0 ）

ISSN： 0882-4010

年卷期： 2024 年 188 卷

页码：

收录情况： SCI

摘要： Edwardsiella piscicida is a severe fish pathogen with wide host range, causing the huge economic losses in the aquaculture industry. Cyclic adenosine monophosphate (cAMP) as an important second messenger regulates the physiological and behavioral responses to environmental cues in eukaryotic and prokaryotic. The intracellular level of cAMP for effective activity is tightly controlled by the synthesis of adenylate cyclase, excretion and degradation of phosphodiesterase. In this study, we identified and characterized a class III cAMP phosphodiesterase, named as CpdA, in the E. piscicida. To investigate the role of CpdA in the physiology and pathogenicity, we constructed the in-frame deletion mutant of cpdA of E. piscicida, TX01 Delta cpdA. The results showed that TX01 Delta cpdA accumulated the higher intracellular cAMP concentration than TX01, indicating that CpdA exerted the hydrolysis of cAMP. In addition, compared to the TX01, the TX01 Delta cpdA slowed growth rate, diminished biofilm formation and lost motility. More importantly, pathogenicity analysis confirmed that TX01 Delta cpdA significantly impaired the ability of invading the epithelial cells, reproduction in macrophages, tissues dissemination and lethality for healthy tilapias. The most of lost properties of TX01 Delta cpdA were restored partially or fully by the introduction of cpdA gene. These results suggest that cpdA is required for regulation of the physiology and virulence of E. piscicida.

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