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The plasmodial CTP:phosphocholine cytidylyltransferase ( Pf CCT) is a promising antimalarial target, which can be inhibited to exploit the need for increased lipid biosynthesis during the erythrocytic life stage of  Plasmodium falciparum . Notable structural and regulatory differences of plasmodial and mammalian CCTs offer the possibility to develop species-specific inhibitors. The aim of this study was to use CHO-MT58 cells expressing a temperature-sensitive mutant CCT for the functional characterization of  Pf CCT. We show that heterologous expression of wild type  Pf CCT restores the viability of CHO-MT58 cells at non-permissive (40 °C) temperatures, whereas catalytically perturbed or structurally destabilized  Pf CCT variants fail to provide rescue. Detailed  in vitro  characterization indicates that the H630N mutation diminishes the catalytic rate constant of  Pf CCT. The flow cytometry-based rescue assay provides a quantitative readout of the  Pf CCT function opening the possibility for the functional analysis of  Pf CCT and the high throughput screening of antimalarial compounds targeting plasmodial CCT.

scientific reports

Heterologous expression of CTP:phosphocholine cytidylyltransferase from Plasmodium falciparum rescues Chinese Hamster Ovary cells deficient in the Kennedy phosphatidylcholine biosynthesis pathway