摘要
目的明确衣原体噬菌体Vp2蛋白在病毒重组、筛查研究中的作用,评估Vp2的临床价值。方法以COBALT程序在线比对各株衣原体噬菌体衣壳蛋白Vp2蛋白序列;并以ProteinBlast的Distance tree功能构建种系发生树。以高保守区氨基酸序列为基础,采用Gamier-Robson法、Chou-Fasman法分析蛋白二级结构;以Karplus-Schulz法分析柔性区域;Kyte-Doolittle法、Hopp-Woods法分析亲水性;Emini法分析表面可及性;Jameson-Wolf法分析抗原指数。结果 6株衣原体噬菌体Vp2蛋白序列高度保守,差异主要在Chp1与其他5株噬菌体的Vp2蛋白之间亲缘关系较远。各株噬菌体的Vp2蛋白均有α螺旋为主的二级结构,蛋白序列高保守区存在多个细胞表位。结论 Vp2蛋白性质保守,是衣原体噬菌体衣壳的重要组分。其蛋白分子结构复杂,高保守区有较强的免疫原性,在病毒重组、沙眼衣原体噬菌体野生株筛查研究中有实际研究价值。
Objective To evaluate the effect of chlamydiaphage virus protein 2(Vp2) on the recombinant virus and virus screening research, and it clinical value thereof. Methods To compare the Vp2 protein sequences to get the conserva-tive region with COBALT. A phylogenetic tree was built with ProteinBlast of Distance tree. The amino acid sequence in the high conservative region was predicted by the methods of Gamier-Robson and Chou-Fasman, and its flexibe regions were predicted by Karplus method. The hydrophilicity plot was predicted by Kyte-Doolittle and Hopp-Woods method. The sur-face probability was analysed by Emini, and the antigenic index was analysed by Jameson-Wolf method. Results The six Chlamydiaphage Vp2 proteins were the highly conserved sequences. There were obvious differences between Chp1Vp2 and other 5 Vp2 proteins. There were the main structure-alpha helix and some cell epitopes in the high conserved region. Con-clusion Vp2 protein is the important component of chlamydia phage capsid with the conservative nature. Vp2 protein has complicated structures and high conservative region with strong immunogenicity, playing a practical value of research in vi-rus recombinantment and screening the wild strains of chlaymdia trachomatis phage.
出处
《天津医药》
CAS
北大核心
2014年第7期634-637,共4页
Tianjin Medical Journal
基金
天津市中医药管理局科技基金资助项目(13017)