Evaluation of the vaccine potential of a cytotoxic protease and a protective immunogen from a pathogenic Vibrio harveyi strain
文献类型：期刊论文
| 作者 | Cheng, Shuang1,2; Zhang, Wei-wei1,3; Zhang, Min1; Sun, Li1 |
| 刊名 | VACCINE
 |
| 出版日期 | 2010-01-22 |
| 卷号 | 28期号:4页码:1041-1047 |
| ISSN号 | 0264-410X |
| 关键词 | Cytotoxin Immunoprotective Protease Vaccine Vibrio Harveyi |
| 通讯作者 | Sun, L, Chinese Acad Sci, Inst Oceanol, 7 Nanhai Rd, Qingdao 266071, Peoples R China |
| 产权排序 | [Cheng, Shuang; Zhang, Wei-wei; Zhang, Min; Sun, Li] Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China; [Cheng, Shuang] Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China; [Zhang, Wei-wei] Chinese Acad Sci, Yantai Inst Coastal Zone Res Sustainable Dev, Yantai 264003, Peoples R China |
| 文献子类 | Article |
| 英文摘要 | Vibrio harveyi is an important aquaculture pathogen that can infect a number of fish species and marine invertebrates. A putative protease. Vhp1, was identified front a pathogenic V harveyi strain isolated from diseased fish as a protein with secretion capacity Vhp1 is 530 amino acids in length and shares high sequence identities with several extracellular serine proteases of the Vibrio species In silico analysis identified a protease domain in Vhp1. which is preceded by a subtilisin-N domain and followed by a bacterial pre-peptidase C-terminal domain Purified recombinant protein corresponding to the protease domain of Vhp1 exhibited apparent proteolytic activity that was relatively heat-stable and reached maximum at pH 8 0 and 50 degrees C The activity of purified recombinant Vhp1 protease was enhanced by Ca2+ and inhibited by Mn2+ and ethylenedinitrilotetraacetic acid Cytotoxicity analyses indicated that recombinant Vhp1 protease was toxic to cultured Japanese flounder cells and could cause complete cell lysis. Immunoprotective analysis using Japanese flounder as an animal model showed that purified recombinant Vhp1 in the form of a denatured and proteolytically inactive protein was an effective subunit vaccine To improve the vaccine potential of Vhp1. an Escherichia coli strain that expresses and secrets a cytotoxically impaired Vhp1 was constructed. which, when used as a live vaccine, afforded a high level of protection upon the vaccinated fish against lethal V. harveyi challenge Taken together, these results demonstrate that Vhp1 is a cytotoxic protease and in effective vaccine candidate against V harveyi infection. (C) 2009 Elsevier Ltd All rights reserved; Vibrio harveyi is an important aquaculture pathogen that can infect a number of fish species and marine invertebrates. A putative protease. Vhp1, was identified front a pathogenic V harveyi strain isolated from diseased fish as a protein with secretion capacity Vhp1 is 530 amino acids in length and shares high sequence identities with several extracellular serine proteases of the Vibrio species In silico analysis identified a protease domain in Vhp1. which is preceded by a subtilisin-N domain and followed by a bacterial pre-peptidase C-terminal domain Purified recombinant protein corresponding to the protease domain of Vhp1 exhibited apparent proteolytic activity that was relatively heat-stable and reached maximum at pH 8 0 and 50 degrees C The activity of purified recombinant Vhp1 protease was enhanced by Ca2+ and inhibited by Mn2+ and ethylenedinitrilotetraacetic acid Cytotoxicity analyses indicated that recombinant Vhp1 protease was toxic to cultured Japanese flounder cells and could cause complete cell lysis. Immunoprotective analysis using Japanese flounder as an animal model showed that purified recombinant Vhp1 in the form of a denatured and proteolytically inactive protein was an effective subunit vaccine To improve the vaccine potential of Vhp1. an Escherichia coli strain that expresses and secrets a cytotoxically impaired Vhp1 was constructed. which, when used as a live vaccine, afforded a high level of protection upon the vaccinated fish against lethal V. harveyi challenge Taken together, these results demonstrate that Vhp1 is a cytotoxic protease and in effective vaccine candidate against V harveyi infection. (C) 2009 Elsevier Ltd All rights reserved |
| 学科主题 | Immunology ; Medicine, Research & Experimental |
| URL标识 | 查看原文 |
| WOS关键词 | SUBTILISIN-TYPE PROTEASE ; SOLEA-SENEGALENSIS KAUP ; LATES-CALCARIFER BLOCH ; AQUALYSIN-I ; EXTRACELLULAR PRODUCTS ; MOLECULAR APPLICATION ; CYSTEINE PROTEASE ; PENAEUS-MONODON ; METALLOPROTEASE ; ANGUILLARUM |
| WOS研究方向 | Immunology ; Research & Experimental Medicine |
| 语种 | 英语 |
| WOS记录号 | WOS:000274943300029 |
| 资助机构 | National Basic Research Program of China [2006CB101807] |
| 公开日期 | 2011-07-14 |
| 源URL | [http://ir.yic.ac.cn/handle/133337/3714]  |
| 专题 | 烟台海岸带研究所_环境化学实验室 |
| 作者单位 | 1.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China 3.Chinese Acad Sci, Yantai Inst Coastal Zone Res Sustainable Dev, Yantai 264003, Peoples R China |
| 推荐引用方式 GB/T 7714 | Cheng, Shuang,Zhang, Wei-wei,Zhang, Min,et al. Evaluation of the vaccine potential of a cytotoxic protease and a protective immunogen from a pathogenic Vibrio harveyi strain[J]. VACCINE,2010,28(4):1041-1047. |
| APA | Cheng, Shuang,Zhang, Wei-wei,Zhang, Min,&Sun, Li.(2010).Evaluation of the vaccine potential of a cytotoxic protease and a protective immunogen from a pathogenic Vibrio harveyi strain.VACCINE,28(4),1041-1047. |
| MLA | Cheng, Shuang,et al."Evaluation of the vaccine potential of a cytotoxic protease and a protective immunogen from a pathogenic Vibrio harveyi strain".VACCINE 28.4(2010):1041-1047. |
入库方式： OAI收割
来源：烟台海岸带研究所
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