中文摘要：

根据GenBank中猪链球菌鸟氨酸氨甲酰转移酶基因（oct）序列（GenBank登录号：NZ_CP007497）设计引物,克隆猪链球菌ZY05719株的oct基因,构建p ET-28a-oct原核表达质粒并在大肠杆菌Rosetta中诱导表达,重组OCT蛋白即鸟氨酸氨甲酰转移酶用镍亲和层析柱纯化后,研究它对猪链球菌生物被膜形成的影响及介导猪链球菌黏附PK-15细胞的作用。结果显示,克隆出1 014 bp的oct基因,并检测出纯化的40 ku OCT融合蛋白具有良好的反应原性,且能提高猪链球菌形成生物被膜的能力及降低黏附PK-15细胞的作用。本研究成功克隆并表达了ZY05719株的oct基因,初步揭示了其生物学功能,为深入研究鸟氨酸氨甲酰转移酶在猪链球菌致病机制中的作用奠定了基础。

英文摘要：

The oct gene fragment was amplified by PCR from Streptococcus suis ZY05719 strain and cloned into prokaryotic expression plasmid p ET-28 a to form p ET-28a-oct. The expression of recombinant protein was induced in E.coli Rosetta and was purified. The expressed and purified proteins were analyzed by SDS-PAGE and its antiserum was raised from immunized rabbits. The effect of purified recombinant protein and its antiserum on the biofilm formation and on adhesion of S.suis to PK-15 were assayed.In result, sequence analysis showed that the length of the oct gene was 1 014 bp. The prokaryotic expressed product was a fusion protein, whose molecular weight was about 40 ku and could improve the S.suis biofilm formation and could keep down adhesion of S.suis to PK-15. The oct gene of ZY05719 has been successfully cloned and highly expressed in E.coli Rosetta, the recombinant protein facilitates the further studies on the biofilm and the bacterial adhesion, and even the pathogenesis of S. suis.