Malaria remains a scourge of mankind, and the protozoan parasite responsible for the most virulent form of the disease, Plasmodium falciparum, is developing resistance against even the most recent molecules in the antimalarial arsenal. New control agents with novel modes of action are urgently needed, and protein kinases have been proposed as attractive targets.
Two teams at the EPFL Faculty of Life Sciences, the INSERM-EPFL joint laboratory led by Christian Doerig and the Proteomics Core Facility led by Marc Moniatte, joined forces with a team at Institut Pasteur (Paris) to use reverse genetics and proteomics to gain insight into the cellular function of a parasitic protein kinase called CK2. The research demonstrates that both the regulatory and the catalytic subunits of the parasite’s CK2 enzyme are essential for parasite survival, validating CK2 as a potential target for chemotherapy. Proteomics-based identification of proteins from the parasite that form complexes with CK2 singled out chromatin assembly as a major CK2-regulated process in the parasite. This approach is now applied to the entire kinome of P. falciparum and is expected to provide a wealth of data with high relevance (i) to the functional characterization of potential novel targets for intervention, and (ii) to fascinating fundamental information on the biology of this widely divergent eukaryote.