天津医药
天津醫藥
천진의약
TIANJIN MEDICAL JOURNAL
2014年
7期
634-637
,共4页
姚卫锋%卢桂玲%谢艳秋%于旺%宋蒙蒙%李士颖
姚衛鋒%盧桂玲%謝豔鞦%于旺%宋矇矇%李士穎
요위봉%로계령%사염추%우왕%송몽몽%리사영
微病毒属%衣原体科%细菌噬菌体%蛋白质类%计算生物学
微病毒屬%衣原體科%細菌噬菌體%蛋白質類%計算生物學
미병독속%의원체과%세균서균체%단백질류%계산생물학
microvirus%chlamydiaceae%bacteriophages%proteins%computational biology
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。
目的:明確衣原體噬菌體Vp2蛋白在病毒重組、篩查研究中的作用,評估Vp2的臨床價值。方法以COBALT程序在線比對各株衣原體噬菌體衣殼蛋白Vp2蛋白序列;併以ProteinBlast的Distance tree功能構建種繫髮生樹。以高保守區氨基痠序列為基礎,採用Gamier-Robson法、Chou-Fasman法分析蛋白二級結構;以Karplus-Schulz法分析柔性區域;Kyte-Doolittle法、Hopp-Woods法分析親水性;Emini法分析錶麵可及性;Jameson-Wolf法分析抗原指數。結果6株衣原體噬菌體Vp2蛋白序列高度保守,差異主要在Chp1與其他5株噬菌體的Vp2蛋白之間親緣關繫較遠。各株噬菌體的Vp2蛋白均有α螺鏇為主的二級結構,蛋白序列高保守區存在多箇細胞錶位。結論 Vp2蛋白性質保守,是衣原體噬菌體衣殼的重要組分。其蛋白分子結構複雜,高保守區有較彊的免疫原性,在病毒重組、沙眼衣原體噬菌體野生株篩查研究中有實際研究價值。
목적:명학의원체서균체Vp2단백재병독중조、사사연구중적작용,평고Vp2적림상개치。방법이COBALT정서재선비대각주의원체서균체의각단백Vp2단백서렬;병이ProteinBlast적Distance tree공능구건충계발생수。이고보수구안기산서렬위기출,채용Gamier-Robson법、Chou-Fasman법분석단백이급결구;이Karplus-Schulz법분석유성구역;Kyte-Doolittle법、Hopp-Woods법분석친수성;Emini법분석표면가급성;Jameson-Wolf법분석항원지수。결과6주의원체서균체Vp2단백서렬고도보수,차이주요재Chp1여기타5주서균체적Vp2단백지간친연관계교원。각주서균체적Vp2단백균유α라선위주적이급결구,단백서렬고보수구존재다개세포표위。결론 Vp2단백성질보수,시의원체서균체의각적중요조분。기단백분자결구복잡,고보수구유교강적면역원성,재병독중조、사안의원체서균체야생주사사연구중유실제연구개치。
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.