High Level Expression and Purification of 1 C-terminal Fragment of Merozoite Surface Protein of Plasmodium falciparum in Pichia pastoris

To obtain an ideal recombinant C-terminal fragment of the merozoite surface protein of Plasmodium falciparum in the Pichia pastoris expression system, the major surface protein-1(subscript 19) (MSP-1(subscript 19)) gene sequence bearing the 6-his gene was inserted into expression vector pPIC9k and the target gene was transformed to the susceptible yeast cells GS115 by using electroporation. The multiple inserts were screened and the successfully expressed MSP-1(subscript 19) protein with the relative molecular weight of 12kDa in the supernatants of cell cultures could be detected by SDS-PAGE. Meanwhile, Western blot analysis also demonstrated that this protein reacted with mouse anti-MSP-1(subscript 19) monoclonal antibody, and the expression level of MSP-1(subscript 19) was more than 1.0 g/L. It is concluded that this recombinant protein expressed in the Pichia pastoris expression system resembles the native proteins existed.