Feeding truncated heat shock protein 70s protect Artemia franciscana against virulent Vibrio campbellii challenge
文献类型：期刊论文
| 作者 | Baruah, Kartik1,2; Norouzitallab, Parisa1,2; Li Shihao3; Sorgeloos, Patrick1,2; Bossier, Peter1,2 |
| 刊名 | FISH & SHELLFISH IMMUNOLOGY
 |
| 出版日期 | 2013 |
| 卷号 | 34期号:1页码:183-191 |
| 关键词 | Truncated heat shock protein 70 Phenoloxidase Priming Artemia franciscana Vibrio campbellii |
| ISSN号 | 1050-4648 |
| 通讯作者 | Baruah, K |
| 中文摘要 | 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. |
| 英文摘要 | 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. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 学科主题 | Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences |
| 类目[WOS] | Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences |
| 研究领域[WOS] | Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences |
| 关键词[WOS] | MOLECULAR CHAPERONES ; DROSOPHILA-MELANOGASTER ; INVERTEBRATE IMMUNITY ; DENDRITIC CELLS ; HEAT-SHOCK-PROTEIN-70 ; HSP70 ; BINDING ; SYSTEM ; LARVAE ; THERMOTOLERANCE |
| 收录类别 | SCI |
| 原文出处 | 10.1016/j.fsi.2012.10.025 |
| 语种 | 英语 |
| WOS记录号 | WOS:000314743600022 |
| 公开日期 | 2014-07-17 |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/16572]  |
| 专题 | 海洋研究所_实验海洋生物学重点实验室 |
| 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.(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. |
入库方式： OAI收割
来源：海洋研究所
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