弧菌琼胶酶和丝氨酸蛋白酶的筛选、分析以及免疫应用
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摘要
从山东黄岛海水养殖场分离到一株弧菌V134,从中克隆得到琼胶酶基因agaV,并将其在大肠杆菌中表达,纯化得到重组的琼胶酶AgaV。酶活分析发现该琼胶酶的最适温度在40℃左右,对pH比较敏感,pH 7.0时具有最高的琼胶裂解活性。对AgaV进行了两种应用性探索:(1)利用AgaV从琼脂糖凝胶中回收DNA,回收效率可达90%以上;(2)利用agaV作为报告基因构建了捕获分泌序列的载体pBU,并用其从革兰氏阳性细菌(G+菌)和革兰氏阴性细菌(G-菌)中筛选出了一系列分泌蛋白。将利用pBU从一株哈维氏弧菌T4中筛选出的6个分泌蛋白分别进行基因克隆、蛋白表达纯化和牙鲆免疫实验,发现其中一个蛋白,命名为DegQ_(Vh),具有免疫保护效应,其免疫保护率(RPS)可达64%。为了提高DegQ_(Vh)的免疫保护效应,将AgaV的分泌结构域与DegQ_(Vh)融合,构成融合抗原AgaV-DegQ_(Vh)。利用大肠杆菌作为载体菌构建了AgaV-DegQ_(Vh)融合抗原递呈系统,用其作为疫苗进行免疫,发现其RPS可达到95%。酶活分析表明DegQ_(Vh)在50℃、pH 8.0时具有最高的活性。突变分析表明83位的组氨酸、113位的天冬氨酸和188位的丝氨酸以及两个PDZ结构域是DegQ_(Vh)活性所必需的。表达分析发现degQ_(Vh)表达受温度和细胞浓度调控,并且其上游有一个受σE调控的启动子。进一步的分析发现DegQ_(Vh)能够与大肠杆菌的DegP功能互补。
Vibrio sp V134 was isolated from a fish farm in Huangdao Shandong Province. agaV gene was cloned and expressed in BL21(DE3), the recombinant protein AgaV was purified with nichel-nitrilotriacetic acid agarose under native conditions. The purified protein was analyzed using agarose as substrate to establish the optimum temperature and pH of the agarase, which was around 40℃and pH 7.0, with a narrow agarolytic range of pH respectively. AgaV was demonstrated in two aspects: first, as an agarolytic enzyme, the purified recombinant AgaV could be employed in the recovery of DNA from agarose gels; second, as a secretion protein, AgaV was explored at genetic level and used as a reporter in the construction of a secretion signal trap which proved to be a simple and efficient molecular tool for selection of genes encoding secretion proteins from both G+ and G- bacteria.
Of the six signal sequences selected by pBU from fish pathogen T4, a Vibrio harveyi strain, one characterized to be a serine protease and named degQ_(Vh), was tested to be an immunoprotective protein agaist T4. The protease exhibited highly RPS (Relative Percentage Survival)≈65% aganist the disease caused by T4. To enhance RPS, AgaV-DegQ_(Vh) fusion protein was expressed in DH5αto form the antigen delivery system, which was proved to increase the RPS about 30%. degQ_(Vh) was cloned into PET258 and expressed in BL21 (DE3), the recombinant DegQvh was purified and characterized, which showed the highest protelytic activity around 50℃ and pH 8.0. Five mutations concluding three site mutations and two PDZ deletion mutations demonstrated that the protease activity of DegQ_(Vh) need His(83), Asp (113) and Ser (188), the three typical catalytic amino acid and both of the PDZ domains. Analysis indicated that the expression of degQ_(Vh) was regulated by temperature and cell density. The sequence alignment of up stream of degQ_(Vh) indicated that it contained oneσE–dependent promoter. Further study indicated that degQ_(Vh) could complement the function of DegP in E. coli.
Vibrio sp V134 was isolated from a fish farm in Huangdao Shandong Province. agaV gene was cloned and expressed in BL21(DE3), the recombinant protein AgaV was purified with nichel-nitrilotriacetic acid agarose under native conditions. The purified protein was analyzed using agarose as substrate to establish the optimum temperature and pH of the agarase, which was around 40℃and pH 7.0, with a narrow agarolytic range of pH respectively. AgaV was demonstrated in two aspects: first, as an agarolytic enzyme, the purified recombinant AgaV could be employed in the recovery of DNA from agarose gels; second, as a secretion protein, AgaV was explored at genetic level and used as a reporter in the construction of a secretion signal trap which proved to be a simple and efficient molecular tool for selection of genes encoding secretion proteins from both G+ and G- bacteria.
Of the six signal sequences selected by pBU from fish pathogen T4, a Vibrio harveyi strain, one characterized to be a serine protease and named degQ_(Vh), was tested to be an immunoprotective protein agaist T4. The protease exhibited highly RPS (Relative Percentage Survival)≈65% aganist the disease caused by T4. To enhance RPS, AgaV-DegQ_(Vh) fusion protein was expressed in DH5αto form the antigen delivery system, which was proved to increase the RPS about 30%. degQ_(Vh) was cloned into PET258 and expressed in BL21 (DE3), the recombinant DegQvh was purified and characterized, which showed the highest protelytic activity around 50℃ and pH 8.0. Five mutations concluding three site mutations and two PDZ deletion mutations demonstrated that the protease activity of DegQ_(Vh) need His(83), Asp (113) and Ser (188), the three typical catalytic amino acid and both of the PDZ domains. Analysis indicated that the expression of degQ_(Vh) was regulated by temperature and cell density. The sequence alignment of up stream of degQ_(Vh) indicated that it contained oneσE–dependent promoter. Further study indicated that degQ_(Vh) could complement the function of DegP in E. coli.
引文
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