摘要
为进一步研究绵羊肺炎支原体P113蛋白的结构与功能,在进行生物信息学分析的基础上,对编码其C端重复区的基因片段进行了PCR扩增、克隆和原核表达,并采用Western-blotting方法对P113蛋白的免疫原性进行了分析。结果显示,P113蛋白与猪肺炎支原体黏附素P97蛋白高度同源,并具有相似的C端重复区;该区域在大肠杆菌Rosetta(DE3)中成功获得表达,重组蛋白以可溶性的形式存在;经纯化的重组蛋白与抗绵羊肺炎支原体全菌血清发生结合反应,表明P113蛋白是良好的免疫原。
To investigate the structure and functions of Pl13 protein of Mycoplasma ovipneumoniae, following bioinformatics analysis,a fragment coding for a C terminal repeat region of the Pl13 was cloned and expressed in Escherichia coli. Immunogenicity of the expressed Pl13 was analyzed by Western-blot. The results showed that Pl13 was homologous to Mycoplasma hyopneurnoniae adhesin P97 and shared the similar C terminal repeat region. The repeat region was successfully expressed in E. coli Rosetta（DE3） and the recombinant protein was proved to be soluble. The purified recombinant protein reacted with rabbit serum against M. ovipneumoniae,suggesting that Pl13 is one of the immunogens of the bacteria.
出处
《中国兽医科学》
CAS
CSCD
北大核心
2013年第7期733-737,共5页
Chinese Veterinary Science
基金
国家自然科学基金项目(31272588)
