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首页> 外文期刊>Vaccine >Evaluation of the vaccine potential of a cytotoxic protease and a protective immunogen from a pathogenic Vibrio harveyi strain.
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Evaluation of the vaccine potential of a cytotoxic protease and a protective immunogen from a pathogenic Vibrio harveyi strain.

机译：评估致病性哈维弧菌菌株的细胞毒性蛋白酶和保护性免疫原的疫苗潜力。

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Vibrio harveyi is an important aquaculture pathogen that can infect a number of fish species and marine invertebrates. A putative protease, Vhp1, was identified from 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 an effective vaccine candidate against V. harveyi infection.
机译：哈维弧菌是一种重要的水产养殖病原体，可以感染多种鱼类和海洋无脊椎动物。从致病性V中鉴定出一种推定的蛋白酶Vhp1。从患病鱼中分离出的harveyi品系具有分泌能力的蛋白质。 Vhp1的长度为530个氨基酸，与 Vibrio 菌种的几种胞外丝氨酸蛋白酶具有高度的序列同一性。在计算机分析中确定了Vhp1中的蛋白酶结构域，其前是枯草杆菌蛋白酶N结构域，然后是细菌前肽酶C末端结构域。纯化的对应于Vhp1蛋白酶结构域的重组蛋白表现出明显的蛋白水解活性，该蛋白相对稳定，在pH 8.0和50摄氏度时达到最大值。Ca 2 + 并被Mn 2 + 和亚乙基二三氟四乙酸抑制。细胞毒性分析表明重组Vhp1蛋白酶对培养的日本比目鱼细胞具有毒性，并可能导致细胞完全裂解。以日本比目鱼为动物模型的免疫保护分析表明，以变性且蛋白水解失活的蛋白质形式纯化的重组Vhp1是有效的亚单位疫苗。为了提高Vhp1的疫苗潜力，构建了一种表达和分泌细胞毒性受损的Vhp1的大肠杆菌菌株，当用作活疫苗时，该疫苗对接种的鱼提供了高水平的保护，使其免于感染致命的harveyi 挑战。综上所述，这些结果表明Vhp1是一种细胞毒性蛋白酶，并且是针对V的有效候选疫苗。 harveyi 感染。

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