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The Mutation of the DNA-Binding Domain of Fur Protein Enhances the Pathogenicity of Edwardsiella piscicida via Inducing Overpowering Pyroptosis

文献类型： 外文期刊

作者： Niu, Mimi 1 ; Sui, Zhihai 5 ; Jiang, Guoquan 2 ; Wang, Ling 2 ; Yao, Xuemei 1 ; Hu, Yonghua 2 ;

作者机构： 1.Hainan Univ, State Key Lab Marine Resource Utilizat South China, 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.Hainan Univ, Sch Life Sci, Haikou 570228, Peoples R China

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

6.Huazhong Agr Univ, Coll Fisheries, Wuhan 430070, Peoples R China

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

8.Hainan Univ, Sch Marine Biol & Aquaculture, Haikou 570228, Peoples R China

关键词： fish pathogen; ferric uptake regulator; N-terminal domain; stress tolerance; virulence

期刊名称：MICROORGANISMS （ 影响因子：4.5； 五年影响因子：4.8 ）

ISSN：

年卷期： 2024 年 12 卷 1 期

页码：

收录情况： SCI

摘要： Edwardsiella piscicida is an important fish pathogen with a broad host that causes substantial economic losses in the aquaculture industry. Ferric uptake regulator (Fur) is a global transcriptional regulator and contains two typical domains, the DNA-binding domain and dimerization domain. In a previous study, we obtained a mutant strain of full-length fur of E. piscicida, TX01 Delta fur, which displayed increased siderophore production and stress resistance factors and decreased pathogenicity. To further reveal the regulatory mechanism of Fur, the DNA-binding domain (N-terminal) of Fur was knocked out in this study and the mutant was named TX01 Delta fur2. We found that TX01 Delta fur2 displayed increased siderophore production and enhanced adversity tolerance, including a low pH, manganese, and high temperature stress, which was consistent with the phenotype of TX01 Delta fur. Contrary to TX01 Delta fur, whose virulence was weakened, TX01 Delta fur2 displayed an ascended invasion of nonphagocytic cells and enhanced destruction of phagocytes via inducing overpowering or uncontrollable pyroptosis, which was confirmed by the fact that TX01 Delta fur2 induced higher levels of cytotoxicity, IL-1 beta, and p10 in macrophages than TX01. More importantly, TX01 Delta fur2 displayed an increased global virulence to the host, which was confirmed by the result that TX01 Delta fur2 caused higher lethality outcomes for healthy tilapias than TX01. These results demonstrate that the mutation of the Fur N-terminal domain augments the resistance level against the stress and pathogenicity of E. piscicida, which is not dependent on the bacterial number in host cells or host tissues, although the capabilities of biofilm formation and the motility of TX01 Delta fur2 decline. These interesting findings provide a new insight into the functional analysis of Fur concerning the regulation of virulence in E. piscicida and prompt us to explore the subtle regulation mechanism of Fur in the future.

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