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Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
Published on: February 25, 2010
Evaluation of codon optimized recombinant Plasmodium knowlesi merozoite surface protein-119 (pkMSP-119) expressed in
Y L Lau1, F W Cheong1, L C Chin1
1Department of Parasitology, Faculty of Medicine, University of Malaya, 50603 Kuala Lumpur, Malaysia.
Abstract:
Malaria causes high global mortality and morbidity annually. Plasmodium knowlesi has been recognised as the fifth human Plasmodium sp. and its infection is widely distributed in Southeast Asia. Merozoite surface protein-119 (MSP-119) appears as a potential candidate for malaria blood stage vaccine as it could induce protective immunity. In this study, codon optimized P. knowlesi MSP-119 (pkMSP-119) was expressed and purified in yeast Pichia pastoris expression system. The purified recombinant protein was further evaluated using Western blot assay using knowlesi malaria, non-knowlesi human malaria, non-malarial parasitic infections and healthy serum samples (n = 50). The sensitivity of purified pkMSP-119 towards detection of knowlesi infection was as 28.6% (2/7). pkMSP-119 did not react with all non-malarial parasitic infections and healthy donor sera, yet reacted with some non-knowlesi human malaria sera, therefore lead to a specificity of 86.0% (37/43).
