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当前位置: 首页 > 文章 > 细粒棘球绦虫Eg95-5蛋白生物信息学分析及鉴定 黑龙江畜牧兽医 2019 (5) 26-30+176-177
Position: Home > Articles > Bioinformatics analysis and identification of Eg95-5 protein of Echinococcus granulosus Heilongjiang Animal Science and Veterinary Medicine 2019 (5) 26-30+176-177

细粒棘球绦虫Eg95-5蛋白生物信息学分析及鉴定

作  者：
胡尊楠;马忠臣;何金科;徐明国;陈创夫;王震
单  位：
西部地区高发人兽共患传染性疾病防治协同创新中心;石河子大学动物科技学院;石河子大学生命科学学院
关键词：
棘球蚴;细粒棘球绦虫;Eg95-5;生物信息学;原核表达;Western-blot
摘  要：
为了制备一定纯度和浓度细粒棘球绦虫(Echinococcus granulosus, Eg)Eg95-5蛋白,进一步开发新型疫苗和建立新的疾病诊断方法,试验采用生物信息学分析、pMD19-T-Eg95-5与pET30a-Eg95-5载体的构建、Eg95-5蛋白诱导表达及纯化、免疫印迹技术(Western-blot)对Eg95-5蛋白序列和反应原性进行研究。结果表明:Eg95-5蛋白无信号肽和跨膜结构,蛋白含有6个抗原决定簇和12个磷酸化位点,二级结构以无规则卷曲(39.25%)、延伸链(33.64%)和α-螺旋(21.50%)为主,并获得了Eg95-5的三级结构模型;成功克隆并构建Eg95-5重组表达载体,获得了高纯度的Eg95-5蛋白,该蛋白可与患病动物血清发生特异性反应。说明Eg95-5蛋白结构较为保守,是无信号肽和非跨膜蛋白,作为抗原可以引起良好的免疫反应。
译  名：
Bioinformatics analysis and identification of Eg95-5 protein of Echinococcus granulosus
作  者：
HU Zunnan;MA Zhongchen;HE Jinke;XU Mingguo;CHEN Chuangfu;WANG Zhen;College of Animal Science and Technology, Shihezi University;College of Life Sciences,Shihezi University;Co-innovation Center for Zoonotic Infectious Diseases in the Western Region;
单  位：
HU Zunnan%MA Zhongchen%HE Jinke%XU Mingguo%CHEN Chuangfu%WANG Zhen%College of Animal Science and Technology, Shihezi University%College of Life Sciences,Shihezi University%Co-innovation Center for Zoonotic Infectious Diseases in the Western Region
关键词：
hydatid;;Echinococcus granulosus;;Eg95-5;;bioinformatics;;prokaryotic expression;;Western-blot
摘  要：
In this study, the Eg95-5 protein sequence and reactogenicity were studied with the utilization of bioinformatics software and construction of pET30 a-Eg95-5 vector, Eg95-5 protein induced expression and purification, and Western-blott in order to prepare Eg95-5 protein of Echinococcus granulosus(Eg) with certain purity and concentration, further develop new vaccines and establish new disease diagnosis methods. The results showed that the Eg95-5 protein had no signal peptide and transmembrane structure, the protein contained 6 antigenic determinants and 12 phosphorylation sites, and the secondary structure was randomly coiled(39.25%), extended chain(33.64%) and α-Helix(21.50%) dominated and obtained the tertiary structure model of Eg95-5. Eg95-5 recombinant expression vector were successfully cloned and constructed, and high purity Eg95-5 protein were obtained, which can be correlated specific reaction with serum of sick animals. It indicates that the Eg95-5 protein structure is relatively conservative, and it is a signal-free peptide and a non-transmembrane protein. As an antigen, it can cause a good immune response.

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