Phosphatidylinositol 4-kinase (Plasmodium falciparum, commonly referred to as "PfPI4K") (PI4K or PfPI4K (for the Plasmodium falciparum specific enzyme))

Phosphatidylinositol 4-kinase in Plasmodium falciparum (PfPI4K) is a lipid kinase that catalyzes the formation of phosphatidylinositol 4-phosphate (PI4P) from phosphatidylinositol. This enzyme is essential for membrane trafficking processes in the malaria parasite, especially Golgi organization, vesicle recruitment, and cytokinesis during erythrocytic and other life cycle stages. PfPI4K has been validated as a critical drug target required for parasite survival and has a distinct ATP-binding pocket targeted by new classes of antimalarial compounds, including imidazopyrazines and MMV390048. Inhibition of PfPI4K blocks multiple stages of the parasite lifecycle, providing a basis for drugs with both prophylactic and curative properties. Its essentiality, specific druggability, and role in parasite biology make it a focal point for current malaria drug development programs

Other names

PI4KIIIβ (Type III beta phosphatidylinositol 4-kinase)PfPI4K (Plasmodium falciparum PI4K)PF3D7_0509800 (Plasmodium falciparum gene identifier)

Inhibition of ATP-binding pocket of PI4K blocks kinase activity, preventing conversion of PI to PI4P and disrupting membrane trafficking in the parasite, which leads to failure of parasite development and division