The two Dps of Edwardsiella tarda are involved in resistance against oxidative stress and host infection

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	The two Dps of Edwardsiella tarda are involved in resistance against oxidative stress and host infection
	Zheng, Wen-jiang 1,2; Hu, Yong-hua 1; Sun, Li 1
刊名	FISH & SHELLFISH IMMUNOLOGY
	2011-12-01
卷号	31 期号:6 页码:985-992
关键词	Dps Edwardsiella tarda Ferritin Oxidative stress Virulence
ISSN号	1050-4648
中文摘要	DNA-binding protein from starved cells (Dps) is a member of ferritin-like proteins that exhibit properties of nonspecific DNA binding and iron oxidation and storage. Although studies of Dps from many bacterial species have been reported, no investigations on Dps from fish pathogens have been documented. In this study, we examined the biological function of two Dps proteins, Dps1 and Dps2, from Edwardsiella tarda, an important fish bacterial pathogen that can also infect humans. Dps1 and Dps2 are, respectively, 163-and 174-residue in length and each contains the conserved ferroxidase center of Dps. Expression of dps1 and dps2 was growth phase-dependent and reached high levels in stationary phase. Purified recombinant Dps1 and Dps2 were able to mediate iron oxidation by H(2)O(2) and bind DNA. Compared to the wild type strain, (i) the dps1 mutant (TXDps1) and the dps2 mutant (TXDps2) were unaffected in growth, while the dps2 mutant with interfered dps1 expression (TXDps2RI) exhibited a prolonged lag phase: (ii) TXDps1, TXDps2, and especially TXDps2RI were significantly reduced in H(2)O(2) and UV tolerance and impaired in the capacity to invade into host tissues and replicate in head kidney macrophages; (iii) TXDps1, TXDps2, and TXDps2RI induced stronger macrophage respiratory burst activity and thus were defective in the ability to block the bactericidal response of macrophages. Taken together, these results indicate that Dps1 and Dps2 are functional analogues that possess ferroxidase activity and DNA binding capacity and are required for optimum oxidative stress resistance and full bacterial virulence. (C) 2011 Elsevier Ltd. All rights reserved.
英文摘要	DNA-binding protein from starved cells (Dps) is a member of ferritin-like proteins that exhibit properties of nonspecific DNA binding and iron oxidation and storage. Although studies of Dps from many bacterial species have been reported, no investigations on Dps from fish pathogens have been documented. In this study, we examined the biological function of two Dps proteins, Dps1 and Dps2, from Edwardsiella tarda, an important fish bacterial pathogen that can also infect humans. Dps1 and Dps2 are, respectively, 163-and 174-residue in length and each contains the conserved ferroxidase center of Dps. Expression of dps1 and dps2 was growth phase-dependent and reached high levels in stationary phase. Purified recombinant Dps1 and Dps2 were able to mediate iron oxidation by H(2)O(2) and bind DNA. Compared to the wild type strain, (i) the dps1 mutant (TXDps1) and the dps2 mutant (TXDps2) were unaffected in growth, while the dps2 mutant with interfered dps1 expression (TXDps2RI) exhibited a prolonged lag phase: (ii) TXDps1, TXDps2, and especially TXDps2RI were significantly reduced in H(2)O(2) and UV tolerance and impaired in the capacity to invade into host tissues and replicate in head kidney macrophages; (iii) TXDps1, TXDps2, and TXDps2RI induced stronger macrophage respiratory burst activity and thus were defective in the ability to block the bactericidal response of macrophages. Taken together, these results indicate that Dps1 and Dps2 are functional analogues that possess ferroxidase activity and DNA binding capacity and are required for optimum oxidative stress resistance and full bacterial virulence. (C) 2011 Elsevier Ltd. All rights reserved.
学科主题	Fisheries; Immunology; Marine & Freshwater Biology; Veterinary Sciences
收录类别	SCI
原文出处	10.1016/j.fsi.2011.08.018
语种	英语
WOS记录号	WOS:000298569700033
公开日期	2012-07-03
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/11978]
专题	海洋研究所_实验海洋生物学重点实验室
作者单位	1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China
推荐引用方式 GB/T 7714	Zheng, Wen-jiang,Hu, Yong-hua,Sun, Li. The two Dps of Edwardsiella tarda are involved in resistance against oxidative stress and host infection[J]. FISH & SHELLFISH IMMUNOLOGY,2011,31(6):985-992.
APA	Zheng, Wen-jiang,Hu, Yong-hua,&Sun, Li.(2011).The two Dps of Edwardsiella tarda are involved in resistance against oxidative stress and host infection.FISH & SHELLFISH IMMUNOLOGY,31(6),985-992.
MLA	Zheng, Wen-jiang,et al."The two Dps of Edwardsiella tarda are involved in resistance against oxidative stress and host infection".FISH & SHELLFISH IMMUNOLOGY 31.6(2011):985-992.