Evaluation of the vaccine potential of a cytotoxic protease and a protective immunogen from a pathogenic Vibrio harveyi strain

CORC > 烟台海岸带研究所 > 中国科学院烟台海岸带研究所 > 中科院海岸带环境过程与生态修复重点实验室 > 环境化学实验室

	Evaluation of the vaccine potential of a cytotoxic protease and a protective immunogen from a pathogenic Vibrio harveyi strain
	Cheng, Shuang 1,2; Zhang, Wei-wei 1,3; Zhang, Min 1; Sun, Li 1
刊名	VACCINE
	2010-01-22
卷号	28 期号:4 页码:1041-1047
关键词	Cytotoxin Immunoprotective Protease Vaccine Vibrio Harveyi
ISSN号	0264-410X
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
内容类型	期刊论文
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.