| 微病毒phiCPAR39衣壳Vp1蛋白生物多态性及表位研究 |
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| 引用本文： | 姚卫锋,;卢桂玲,;谢艳秋,;于旺,;宋蒙蒙,;李士颖.微病毒phiCPAR39衣壳Vp1蛋白生物多态性及表位研究[J].武警医学院学报,2014(4):281-283. |
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| 作者姓名： | 姚卫锋 ;卢桂玲 ;谢艳秋 ;于旺 ;宋蒙蒙 ;李士颖 |
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| 作者单位： | [1]天津中医药研究院附属医院皮肤科,天津300120; [2]天津公安医院内三科,天津300042 |
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| 摘 要： | 【目的】分析衣原体微病毒phiCPAR39 Vp1蛋白的亚结构，揭示其在衣原体病毒研究中的价值。【方法】以phiCPAR39 Vp1氨基酸序列为基础，采用Gamier—Robson法、Chou—Fasman法和Karplus—Schulz法分析二级结构；按Kyte—Doolittle法、Hopp—Woods法、Emini法和Jameson—Wolf法分析蛋白的抗原表位。ProteinBlast多序列比对分析蛋白序列多态性。【结果】phiCPAR39 Vp1蛋白序列保守度高，有以B折叠为主的亚三级结构，全序列形成多个抗原位点，预测其N端1～10，103～109，158～166，190～197，252～260，273～285，310～316，333～341，359—367，414～420，466～476，511～516为优势抗原位点。【结论】phiCPAR39 Vp1蛋白结构复杂，抗原位点繁多而利于重组挑选。
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| 关 键 词： | 微病毒 蛋白结构 信息 宿主嗜性 |
The biological polymorphism and epitope analysis of Chlamydiamicrovirus phiCPAR39 protein Vpl |
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| Institution: | YAO Wei-feng, LU Gui-ling, XIE Yan-qiu, YU Wang, SONG Meng-meng, LI Shi-yin (Department of Dermatology, Tianjin Academy of Traditional Chinese Medicine Affiliated Hospital, Tianjin 300120, China) |
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| Abstract: | Objective]To analyze the Chlamydiamicrovirus substructures and reveal its value in Chlamydia virus research. Methods] The secondary structure was analyzed by the method of Gamier-Robson, Chou-Fasman and Karplus-Schulz, and its cell epitopes was analysized by the method of Kyte-Doolittle,Hopp-Woods, Emini and Jameson-Wolf. With the Proteinblast the sequences aligment were analyzed.Results] phiCPAR39 Vplprotein has the conservative sequence. The sections of 1-10, 103-109, 158-166, 190-197, 252- 260, 273-285, 310-316, 333-341,359-367, 414-420, 466-476, 511-516 in the N- terminal of phiCPAR39 Vp1 protein could be the epitopes of B cell. Beta foldings were the priority construction to its second struction. Conclusion] PphiCPAR39 Vp1 protein has the complicated constructures. There are some antigen sites to he choozen for the recombinant rearch. |
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| Keywords: | Microvirus Protein structure Information Host tropism |
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