柔嫩艾美耳球虫serpin基因克隆与生物信息学分析  

Cloning and bioinformatics analysis of Eimeria tenella serpin gene

作　　者：李文超[1,2] 顾有方[1] 宫鹏涛[2] 李建华[2] 杨举[2] 邱发贵[2] 张西臣[2] 

机构地区：[1]安徽科技学院动物科学学院,安徽凤阳233100 [2]吉林大学畜牧兽医学院,吉林长春130062

出　　处：《中国兽医学报》2013年第2期212-216,共5页Chinese Journal of Veterinary Science

基　　金：国家"863"计划资助项目(2011AA10A215);安徽省教育厅优秀青年人才基金资助项目(2011SQRL120);安徽科技学院重点学科建设资助项目(AKXK20101-2)

摘　　要：根据GenBank发表的Eimeria tenella serpin(Etserpin)基因设计1对引物,从孢子化卵囊总RNA中用RT-PCR方法扩增Etserpin基因,克隆后测序,应用生物信息学分析预测其核苷酸及其编码蛋白的结构与功能。结果表明,Etserpin开放阅读框为1 248bp,编码一分泌蛋白,N端具有1个28aa的信号肽,有1个跨膜区域,有2个糖基化位点和21个磷酸化位点,88,89,98～101,208～212,283～287,302～304区段是其可能的B细胞表位;同源性比对与进化树的分析表明其为抑制性serpin蛋白,结构保守,与E.acervulina、T.gondii和N.caninum亲缘关系较近。二级结构以!螺旋和随机卷曲为主,具有类似于serpin家族蛋白的三级结构。Based on the published ORF of E. tenella serpin gene, a pair of primers were designed. The gene was amplified by RT-PCR from E. tenella total RNA, then cloned and sequenced. Subse- quently,the structure and functions of this gene was analyzed by bioinformatics method. The resuits showed Etserpin had an open reading frame（ORF） of 1 248 bp encoded a secreted protein, the 1st to 18th amino acid residues of the N-teriminal represented signal peptide sequences,while there were one transmembrane peptides,two N-glycosylation sites and 2t phosphorylation sites. The B- cell epitopes were probably at its fragment No88-89,98-101,208-212,283-287,302-304. Homology analysis indicated that Etserpin was a structurally conserved,inhibitory serpin protein which had a close identity with serpin of E. acervulina, T. gondii and N. caninum. The Etserpin protein had the secondary structure mainly composed of α helix,random coil and similar tertiary structure of protein in the serpin superfamily.

关 键 词：柔嫩艾美球虫 serpin基因 生物信息学分析 

分 类 号：S852.723[农业科学—基础兽医学]