Edwardsiella tarda DnaJ is a virulence-associated molecular chaperone with immunoprotective potential

doi:10.1016/j.fsi.2011.05.001

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	Edwardsiella tarda DnaJ is a virulence-associated molecular chaperone with immunoprotective potential
	Dang, Wei 1,2; Zhang, Min 1; Sun, Li 1
刊名	FISH & SHELLFISH IMMUNOLOGY
	2011-08-01
卷号	31 期号:2 页码:182-188
关键词	Dnaj Edwardsiella Tarda Hsp40 Vaccine Virulence
ISSN号	1050-4648
DOI	10.1016/j.fsi.2011.05.001
文献子类	Article
英文摘要	Members of the DnaJ/Hsp40 family play an important role in protein homeostasis by regulating the activity of DnaK/Hsp70. In this study, we examined the activity and function of the DnaJ from Edwardsiella tarda, a serious fish pathogen that can also infect humans and birds. In silico analysis indicated that E. tarda DnaJ contains structural features, i.e. the J domain, the glycine/phenylalanine-rich region, and the zinc-finger domain, that are conserved among Type I Hsp40. Purified recombinant DnaJ was able to stimulate the ATPase activity of DnaK. Pull-down assay indicated that DnaJ could interact specifically with DnaK. Mutation of the conserved HPD site in the J domain completely abolished the DnaJ-stimulating effect of DnaJ. To examine the functional importance of DnaJ, a dnaJ-defective mutant was constructed. Compared to the wild type, the dnaJ mutant (i) was retarded in growth and more sensitive to H(2)O(2)-induced oxidative damage, (ii) dramatically reduced in general bacterial virulence and in blood dissemination capacity, and (iii) significantly weakened in the ability to block macrophage activation and to survive within macrophages. Furthermore, when used as a subunit vaccine, purified recombinant DnaJ induced protective immunity in Japanese flounder (Paralichthys olivaceus). Taken together, these results indicate that DnaJ plays an important role in the pathogenesis of E. tarda probably by functioning as a DnaK partner and that DnaJ, with its immunoprotective property, may be useful in the control of E. tarda infection in aquaculture. (C) 2011 Elsevier Ltd. All rights reserved.; Members of the DnaJ/Hsp40 family play an important role in protein homeostasis by regulating the activity of DnaK/Hsp70. In this study, we examined the activity and function of the DnaJ from Edwardsiella tarda, a serious fish pathogen that can also infect humans and birds. In silico analysis indicated that E. tarda DnaJ contains structural features, i.e. the J domain, the glycine/phenylalanine-rich region, and the zinc-finger domain, that are conserved among Type I Hsp40. Purified recombinant DnaJ was able to stimulate the ATPase activity of DnaK. Pull-down assay indicated that DnaJ could interact specifically with DnaK. Mutation of the conserved HPD site in the J domain completely abolished the DnaJ-stimulating effect of DnaJ. To examine the functional importance of DnaJ, a dnaJ-defective mutant was constructed. Compared to the wild type, the dnaJ mutant (i) was retarded in growth and more sensitive to H(2)O(2)-induced oxidative damage, (ii) dramatically reduced in general bacterial virulence and in blood dissemination capacity, and (iii) significantly weakened in the ability to block macrophage activation and to survive within macrophages. Furthermore, when used as a subunit vaccine, purified recombinant DnaJ induced protective immunity in Japanese flounder (Paralichthys olivaceus). Taken together, these results indicate that DnaJ plays an important role in the pathogenesis of E. tarda probably by functioning as a DnaK partner and that DnaJ, with its immunoprotective property, may be useful in the control of E. tarda infection in aquaculture. (C) 2011 Elsevier Ltd. All rights reserved.
学科主题	Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
URL标识	查看原文
语种	英语
WOS记录号	WOS:000293204500002
公开日期	2012-07-03
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/11848]
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	Dang, Wei,Zhang, Min,Sun, Li. Edwardsiella tarda DnaJ is a virulence-associated molecular chaperone with immunoprotective potential[J]. FISH & SHELLFISH IMMUNOLOGY,2011,31(2):182-188.
APA	Dang, Wei,Zhang, Min,&Sun, Li.(2011).Edwardsiella tarda DnaJ is a virulence-associated molecular chaperone with immunoprotective potential.FISH & SHELLFISH IMMUNOLOGY,31(2),182-188.
MLA	Dang, Wei,et al."Edwardsiella tarda DnaJ is a virulence-associated molecular chaperone with immunoprotective potential".FISH & SHELLFISH IMMUNOLOGY 31.2(2011):182-188.