恶性疟原虫裂殖子表面蛋白1-17区基因的原核表达、纯化及表达产物鉴定

目的　为进一步研究和应用恶性疟原虫裂殖子表面蛋白１ 的１７区基因（ＭＳＰ１－ １７），本文原核表达了ＦＵＰ株ＭＳＰ１ 的１７ 区基因，并纯化及鉴定了表达蛋白。方法　将ＭＳＰ１－ １７ 基因片段克隆入原核表达载体ｐＧＥＸ－ ４Ｔ－ １，形成ｐＧＥＸ－ ４Ｔ－ １／ＭＳＰ１－ １７。ＩＰＴＧ诱导ｐＧＥＸ－ ４Ｔ－ １／ＭＳＰ１－ １７ 转化的ＢＬ２１菌，纯化并用ＭＳＰ１－ １７ 特异性单克隆抗体鉴定表达产物。结果　成功地构建了ｐＧＥＸ－ ４Ｔ－ １／ＭＳＰ１－ １７，转化菌经诱导表达出与ＧＳＴ融合的蛋白（约４０ＫＤ），纯化后纯度达７２％ ，ＭＳＰ１－ １７ 特异性单克隆抗体可识别表达蛋白。结论　成功表达并纯化了ＭＳＰ１－ １７ 蛋白，为深入研究和应用ＭＳＰ１－ １７ 打下基础

PROKARYOTIC EXPRESSION,PURIFICATION AND IDENTIFICATON OF PLASMODIUM FALCIPARUM MEROZOITE SURFACE PROTEIN 1 BLOCK 17

Aim\ To further research on Plasmodium falciparum merozoite surface protein 1 block 17(MSP1 17),MSP1 17 was prokaryotic expressed,purified and identified.Method\ MSP1 17 gene fragment was cloned into prokaryotic expression vector pGEX 4T 1 to form pGEX 4T 1/MSP1 17.The expressed protein was purified by GST purification kit after IPTG induced BL21 which is transfected with pGEX 4T 1/MSP1 17.The expressed protein was identified by McAb 5 2 which is specific to MSP1 17.Results\ pGEX 4T 1/MSP1 17 was successfully constructed.After inducement,the transfected BL21 expressed a 40kD protein which is fussed with GST.This protein can reached to 72% pure after purification.This expressed protein could been recognized by McAb 5 2.Conclusions\ MSP1 17 gene was successfully expressed purified.A good basis for research of MSP1 17 was built up.