鸡朊蛋白序列分析及结构特征探究  

Sequence analysis and structural features of chicken prion protein

作　　者：刁小龙[1,2] 吴润[1,2] 刘磊[1,2] 王川[1,2] 赵春林[1,2] 王雄[1,2] 管宏伟[1,2] 

机构地区：[1]甘肃农业大学动物医学院,兰州730070 [2]中国农业科学院兰州兽医研究所/家畜疫病病原生物学国家重点实验室,兰州730046

出　　处：《中国人兽共患病学报》2010年第6期535-539,共5页Chinese Journal of Zoonoses

基　　金：家畜疫病病原生物学国家重点实验室基金项目(SKLVEB2009KFKT012);高等学校博士学科点专项科研基金项目(20060733006)联合资助

摘　　要：目的分析罗曼鸡朊蛋白高级结构,探讨朊蛋白病种间屏障形成机制和朊蛋白构象转变机理。方法根据Gen-Bank提供的鸡朊蛋白基因序列设计特异性引物,扩增出8只罗曼鸡朊蛋白基因的完整开放阅读框(ORF)。结果序列分析表明8只罗曼鸡朊蛋白基因ORF有两处发生碱基置换(243C→T,296A→G),其中243位点为同义码替换。应用生物信息学工具分析罗曼鸡和已知的68个物种的朊蛋白基因,获得基于PrP氨基酸序列的遗传进化信息,进一步依据同源建模法构建人和鸡朊蛋白三维结构模型。结论不同物种朊蛋白构象同源性在很大程度上决定了朊蛋白病种间屏障的形成,多种因素共同作用导致正常朊蛋白转变为致病型构象。In order to analyze the advanced structure of prion protein in Lohmann Brown laying hen,the species barriers in prion diseases and the mechanism of conformational transition,specific primers were designed based on the gene sequence of chicken prion protein in GenBank,and the ORFs of prion protein genes from eight Lohmann Brown laying hens were amplified.Results of sequence analysis showed that there were two base-pair substitutions（243C→T,296A→G）in ORFs,and synonymous mutation was on the site of 243.The genetic evolution information of Lohmann Brown laying hens and other 68 species was obtained based on the amino acid sequence of prion protein gene by bioinformatics analysis,and the three-dimensional structure modeling of prion protein from Lohmann Brown laying hens and human were predicted by homology modeling.It＇s suggested that conformation homology of different species would decide the species barrier mechanism of prion diseases in a great degree.Moreover,the transformation from normal type prion protein to pathotype one would be affected by many factors.

关 键 词：罗曼鸡 朊蛋白 序列分析 结构预测 

分 类 号：R392[医药卫生—免疫学]