关键词: 汉滩病毒;核蛋白;原核表达;纯化;抗原位点

    摘 要:目的 进一步了解汉滩病毒核蛋白氨基端的抗原特性. 方法 构建汉滩病毒S基因5'端311bp片段的原核表达载体，并诱导表达和纯化了Mr 3.6×104 的融合蛋白(汉滩病毒核蛋白氨基端Mr 1.0×104 与Mr 2.6×104 GST融合);用mAb，以Western-blot和ELISA方法对该蛋白的抗原位点进行了鉴定. 结果 与完整核蛋白反应的mAb中仅有部分与Mr 3.6×104 融合蛋白反应，而与核蛋白氨基端Mr 2.6×104 片段反应的5株mAb(1A8，A35，8E8，3A9，3G11)都能与Mr 3.6×104 融合蛋白反应. 结论 汉滩病毒核蛋白氨基端Mr 1.0×104 以内存在一个或几个线性表位，而羧基端可能主要起着维持完整核蛋白立体构象的作用，并影响识别立体表位的mAb与该蛋白的结合.

    Prokaryotic expression，purification and antigentic analysis of hantaan virus S gene5'terminal311bp fragment

    LIU Yong，XU Zhi-Kai，YAN Yan，ZHANG Fang-Lin，WANG Hai-Tao，XUE Xiao-Ping，WU Xing-An

    Department of Microbiology，Faculty of Preclinical Medicine，Fourth Military Medical University，Xi'an710033，China

    Keywords:hataan virus;nucleoprotein;prokayotic expres-sion;purification;antigentic epitope

    Abstract:AIM To further understand the antigen charac-teristic of the amino proximal of hantaan virus nucleoprotein.METHODS We constructed the prokaryotic vector of han-taan S gene5'-terminal311bp，then inducingly expressed and purified the Mr 3.6×104 fusion protein.Then，we further identified its antigentic epitopes by Western blot and ELISA methods using the nucleoprotein specific mAbs.RESULTS We detected that only parts of mAbs reacting with integrated nucleoprotein could react with Mr 3.6×104 fusion protein ......