关键词：恶性疟原虫；裂殖子表面蛋白1；原核表达
摘要 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
Miao Jun Xue Caifang Li Xun Zhen Rongfen
(Department of Parasitology,Fourth Military Medical University,Xi'a n 710032)
ABSTRACT Aim To further research on Plasmodi um falciparum merozoite surface protein 1 block 17(MSP1-17),MSP1-17 wa s prokaryotic expressed,purified and identified.
Method MSP1-17 gen e fragment was cloned into prokaryotic expression vector pGEX-4T-1 to form pGE X-4T-1/MSP1-17.The expressed protein was purified by GST purification kit aft er IPTG induced BL21 which is transfected with pGEX-4T-1/MSP1-17.The expresse d 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 rec ognized by McAb 5.2.
Conclusions MSP1-17 gene was successfully exp ressed purified.A good basis for research of MSP1-17 was built up.
KEY WORDS Plasmodium falciparum Merozoite surface protei n 1 Prokaryotic expression
恶性疟原虫裂殖子表面蛋白1(MSP1)是恶性疟原虫红内期重要抗原 ......
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