Worldwide increase in drug resistant malaria strains has fueled renewed efforts to identify effective therapies for this damaging disease of the developing world. Plasmepsin-V (PM-V) has been identified as an enzyme with a central role in directing P. falciparum proteins to the host erythrocyte, with resulting remodeling of erythrocyte metabolism to support the parasite. The development of potent inhibitors of PM-V aspartyl protease will be greatly advanced by expression and purification of recombinant enzyme for compound library screening and structural studies.  One strategy has been to express PM-V in E. coli as inclusion bodies followed by refolding and purification of active protease.  A series of expression constructs were created to determine the effect of the protease prodomain on refolding efficiency, and results of these studies and characterization of PM-V enzyme activity will be reported.

Expression and characterization of plasmepsin-V, a potential malaria drug target

243rd National Meeting (2012)

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