Abstract: 　Objective] To express the entire MSP1 gene of Plasmodium falciparum and its C-terminal 42 kDa fragment using a tetracycline-controlled P LtetO-1 promoter. [Methods] The entire MSP1 gene and 42 kDa fragment gene were cloned into the plasmid of pZE11,and transformed into E coli DH5αZ1. Restriction e nzyme analysis, SDS-PAGE and Western blotting were used to examine two recombinant plasmids and their expression in E coli DH5αZ1. [Results ] The recombinant plasmids of pZE11/MSP1 and pZE11/MSP1-42 were constructed successfully. The expressive products about 190 kDa and 42 kDa of two genes in E coli DH5αZ1 were identified by SDS-PAGE and Western blotting. [Conclusion] Tightly controlling expression of the MSP1 gene in E coli is essential to reduce the toxicity of the product to its host cells as well as to provide a feasibility to construct Salmonella vaccine strain which can inducibly express the important malarial vaccine candidate gene.

Key words: Escherichia coli, Plasmodium falciparum, MSP1, gene expression * Supported by National 863 Program (102-07-04-04) and National Natural Science Foundation (39780024)