摘要
为了研究绵羊肺炎支原体P109蛋白质的结构与功能,本试验对p109基因进行生物信息学分析,并对其部分基因片段进行了PCR扩增、克隆和原核表达,采用Western-blot方法对其免疫反应性进行分析。结果显示,P109基因与猪肺炎支原体黏附相关基因mhp384高度同源。重组蛋白质在大肠杆菌Rosetta(DE3)工程菌中成功获得表达,以包涵体的形式存在;经纯化的重组蛋白质与山羊抗绵羊肺炎支原体全菌血清发生结合反应,表明P109蛋白质是绵羊肺炎支原体的免疫原之一。
To study the structure and function of P109 protein of Mycoplasma ovipneumoniae, bioinformatics analysis were performed and a partial fragment of p109 was cloned and expressed in Escherichia coli. Immunoreactivity of P109 was analyzed by Western-blot. P109 was highly homologous to M. hyopneumoniae mhp384, an adhesion-related gene. The re-combinant protein was successfully expressed in Escherichia coli Rosetta(DE3) as inclusion body. The purified recombinant protein reacted with goat serum against M. ovipneumoniae, suggesting protein P109 was one of the immunogens of M. ovi-pneumoniae.
出处
《江苏农业学报》
CSCD
北大核心
2015年第4期824-828,共5页
Jiangsu Journal of Agricultural Sciences
基金
国家自然科学基金项目(31272588)
四川省杰出青年学术技术带头人培育计划项目(2013JQ0040)
