HtpG is involved in the pathogenesis of Edwardsiella tarda

doi:10.1016/j.vetmic.2011.05.030

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	HtpG is involved in the pathogenesis of Edwardsiella tarda
	Dang, Wei 1,2; Hu, Yong-hua 1; Sun, Li 1
	2011-09-28
发表期刊	VETERINARY MICROBIOLOGY
ISSN	0378-1135
卷号	152 期号:3-4 页码:394-400
文章类型	Article
摘要	Hsp90 is a molecular chaperone that is involved in diverse cellular processes including protein folding/repairing and signal transduction. Edwardsiella tarda is a serious fish pathogen that affects fish aquaculture worldwide. The aim of this study was to investigate the potential importance of HtpG, the prokaryotic homologue of Hsp90, in the pathogenesis of E. tarda. E. tarda HtpG is 627-residue in length and contains domain structures that are conserved among Hsp90 family members. Quantitative real time RTPCR analysis indicated that expression of htpG is induced by heat shock and oxidative stress. Recombinant HtpG (rHtpG) purified from Escherichia coli exhibits apparent ATPase activity, which is optimal at 40 degrees C. Mutation of htpG (i) affects bacterial growth at elevated tempertaure and renders the cells more sensitive to stress induced by reactive oxygen species, (ii) causes dramatic reduction in blood dissemination and general bacterial virulence, (iii) weakens the ability of E. tarda to block head kidney macrophage activation and to resist against the bactericidal effect of macrophages, and (iv) upregulates the expression of pro-inflammatory cytokines in macrophages. Taken together, these results indicate that HtpG is a biologically active protein that is required for E. tarda to cope with various stress conditions especially that encountered in vivo the host system during infection. (C) 2011 Elsevier B.V. All rights reserved.; Hsp90 is a molecular chaperone that is involved in diverse cellular processes including protein folding/repairing and signal transduction. Edwardsiella tarda is a serious fish pathogen that affects fish aquaculture worldwide. The aim of this study was to investigate the potential importance of HtpG, the prokaryotic homologue of Hsp90, in the pathogenesis of E. tarda. E. tarda HtpG is 627-residue in length and contains domain structures that are conserved among Hsp90 family members. Quantitative real time RTPCR analysis indicated that expression of htpG is induced by heat shock and oxidative stress. Recombinant HtpG (rHtpG) purified from Escherichia coil exhibits apparent ATPase activity, which is optimal at 40 degrees C. Mutation of htpG (i) affects bacterial growth at elevated tempertaure and renders the cells more sensitive to stress induced by reactive oxygen species, (ii) causes dramatic reduction in blood dissemination and general bacterial virulence, (iii) weakens the ability of E. tarda to block head kidney macrophage activation and to resist against the bactericidal effect of macrophages, and (iv) upregulates the expression of pro-inflammatory cytokines in macrophages. Taken together, these results indicate that HtpG is a biologically active protein that is required for E. tarda to cope with various stress conditions especially that encountered in vivo the host system during infection. (C) 2011 Elsevier B.V. All rights reserved.
关键词	Edwardsiella Tarda Hsp90 Htpg Macrophage Virulence
学科领域	Microbiology ; Veterinary Sciences
DOI	10.1016/j.vetmic.2011.05.030
URL	查看原文
收录类别	SCI
语种	英语
WOS记录号	WOS:000294937500023
引用统计	被引频次：35[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.qdio.ac.cn/handle/337002/11867
专题	实验海洋生物学重点实验室
作者单位	1.Chinese Acad Sci, Key Lab Expt Marine Biol, Inst Oceanol, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China
第一作者单位	中国科学院海洋研究所
推荐引用方式 GB/T 7714	Dang, Wei,Hu, Yong-hua,Sun, Li. HtpG is involved in the pathogenesis of Edwardsiella tarda[J]. VETERINARY MICROBIOLOGY,2011,152(3-4):394-400.
APA	Dang, Wei,Hu, Yong-hua,&Sun, Li.(2011).HtpG is involved in the pathogenesis of Edwardsiella tarda.VETERINARY MICROBIOLOGY,152(3-4),394-400.
MLA	Dang, Wei,et al."HtpG is involved in the pathogenesis of Edwardsiella tarda".VETERINARY MICROBIOLOGY 152.3-4(2011):394-400.

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