CAJ | 학술논문

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。
위료연구면양폐염지원체P109단백질적결구여공능，본시험대p109기인진행생물신식학분석，병대기부분기인편단진행료PCR확증、극륭화원핵표체，채용Western-blot방법대기면역반응성진행분석。결과현시， P109기인여저폐염지원체점부상관기인mhp384고도동원。중조단백질재대장간균Rosetta ( DE3)공정균중성공획득표체，이포함체적형식존재；경순화적중조단백질여산양항면양폐염지원체전균혈청발생결합반응，표명P109단백질시면양폐염지원체적면역원지일。
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.