Feeding truncated heat shock protein 70s protect Artemia franciscana against virulent Vibrio campbellii challenge

doi:10.1016/j.fsi.2012.10.025

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	Feeding truncated heat shock protein 70s protect Artemia franciscana against virulent Vibrio campbellii challenge
	Baruah, Kartik 1,2; Norouzitallab, Parisa 1,2; Li Shihao 3; Sorgeloos, Patrick 1,2; Bossier, Peter 1,2; Baruah, K
	2013
发表期刊	FISH & SHELLFISH IMMUNOLOGY
ISSN	1050-4648
卷号	34 期号:1 页码:183-191
文章类型	Article
摘要	The 70 kDa heat shock proteins (Hsp70s) are highly conserved in evolution, leading to striking similarities in structure and composition between eukaryotic Hsp70s and their homologs in prokaryotes. The eukaryotic Hsp70 like the DnaK (Escherichia coli equivalent Hsp70) protein, consist of three functionally distinct domains: an N-terminal 44-kDa ATPase portion, an 18-kDa peptide-binding domain and a C-terminal 10-kDa fragment. Previously, the amino acid sequence of eukaryotic (the brine shrimp Anemia franciscana) Hsp70 and DnaK proteins were shown to share a high degree of homology, particularly in the peptide-binding domain (59.6%, the putative innate immunity-activating portion) compared to the N-terminal ATPase (48.8%) and the C-terminal lid domains (19.4%). Next to this remarkable conservation, these proteins have been shown to generate protective immunity in Artemia against pathogenic Vibrio campbellii. This study, aimed to unravel the Vibrio-protective domain of Hsp70s in vivo, demonstrated that gnotobiotically cultured Artemia fed with recombinant C-terminal fragment (containing the conserved peptide binding domain) of Artemia Hsp70 or DnaK protein were well protected against subsequent Vibrio challenge. In addition, the prophenoloxidase (proPO) system, at both mRNA and protein activity levels, was also markedly induced by these truncated proteins, suggesting epitope(s) responsible for priming the proPO system and presumably other immune-related genes, consequently boosting Anemia survival upon challenge with V. campbellii, might be located within this conserved region of the peptide binding domain. (c) 2012 Elsevier Ltd. All rights reserved.; The 70 kDa heat shock proteins (Hsp70s) are highly conserved in evolution, leading to striking similarities in structure and composition between eukaryotic Hsp70s and their homologs in prokaryotes. The eukaryotic Hsp70 like the DnaK (Escherichia coli equivalent Hsp70) protein, consist of three functionally distinct domains: an N-terminal 44-kDa ATPase portion, an 18-kDa peptide-binding domain and a C-terminal 10-kDa fragment. Previously, the amino acid sequence of eukaryotic (the brine shrimp Anemia franciscana) Hsp70 and DnaK proteins were shown to share a high degree of homology, particularly in the peptide-binding domain (59.6%, the putative innate immunity-activating portion) compared to the N-terminal ATPase (48.8%) and the C-terminal lid domains (19.4%). Next to this remarkable conservation, these proteins have been shown to generate protective immunity in Artemia against pathogenic Vibrio campbellii. This study, aimed to unravel the Vibrio-protective domain of Hsp70s in vivo, demonstrated that gnotobiotically cultured Artemia fed with recombinant C-terminal fragment (containing the conserved peptide binding domain) of Artemia Hsp70 or DnaK protein were well protected against subsequent Vibrio challenge. In addition, the prophenoloxidase (proPO) system, at both mRNA and protein activity levels, was also markedly induced by these truncated proteins, suggesting epitope(s) responsible for priming the proPO system and presumably other immune-related genes, consequently boosting Anemia survival upon challenge with V. campbellii, might be located within this conserved region of the peptide binding domain. (c) 2012 Elsevier Ltd. All rights reserved.
关键词	Truncated Heat Shock Protein 70 Phenoloxidase Priming Artemia Franciscana Vibrio Campbellii
学科领域	Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
DOI	10.1016/j.fsi.2012.10.025
URL	查看原文
收录类别	SCI
语种	英语
WOS研究方向	Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
WOS类目	Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
WOS记录号	WOS:000314743600022
WOS关键词	MOLECULAR CHAPERONES ; DROSOPHILA-MELANOGASTER ; INVERTEBRATE IMMUNITY ; DENDRITIC CELLS ; HEAT-SHOCK-PROTEIN-70 ; HSP70 ; BINDING ; SYSTEM ; LARVAE ; THERMOTOLERANCE
WOS标题词	Science & Technology ; Life Sciences & Biomedicine
引用统计	被引频次：21[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/337002/16572
专题	实验海洋生物学重点实验室
通讯作者	Baruah, K
作者单位	1.Univ Ghent, Fac Biosci Engn, Lab Aquaculture, B-9000 Ghent, Belgium 2.Univ Ghent, Fac Biosci Engn, Artemia Reference Ctr, B-9000 Ghent, Belgium 3.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
推荐引用方式 GB/T 7714	Baruah, Kartik,Norouzitallab, Parisa,Li Shihao,et al. Feeding truncated heat shock protein 70s protect Artemia franciscana against virulent Vibrio campbellii challenge[J]. FISH & SHELLFISH IMMUNOLOGY,2013,34(1):183-191.
APA	Baruah, Kartik,Norouzitallab, Parisa,Li Shihao,Sorgeloos, Patrick,Bossier, Peter,&Baruah, K.(2013).Feeding truncated heat shock protein 70s protect Artemia franciscana against virulent Vibrio campbellii challenge.FISH & SHELLFISH IMMUNOLOGY,34(1),183-191.
MLA	Baruah, Kartik,et al."Feeding truncated heat shock protein 70s protect Artemia franciscana against virulent Vibrio campbellii challenge".FISH & SHELLFISH IMMUNOLOGY 34.1(2013):183-191.

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