We are investigating a largely unexplored family of parasite enzymes known as serine hydrolases, which regulate diverse biological processes and have proven to be attractive drug targets in many human diseases. Despite the P. falciparum genome encoding more than 50 predicted serine hydrolases, only a small fraction has been functionally characterized. Recently, We discovered that one of these proteins localize to the apicoplast, an essential plastid-like organelle that supports critical metabolic pathways required for parasite survival. Our preliminary studies demonstrate that parasites lacking this enzyme are unable to proliferate, indicating that it plays an indispensable role during the blood stage of infection. Current work aims to determine how this enzyme functions at the molecular level. We are identifying its enzymatic activity, defining its physiological substrates, and determining how it contributes to apicoplast biogenesis and inheritance. Understanding these processes will provide new insights into the biology of this unique organelle and may reveal vulnerabilities that can be exploited for antimalarial drug development.

Malaria associated symptoms arise when the parasite repeatedly invades and multiplies inside human red blood cells (RBCs). This invasion process is driven by the precise release of proteins from specialized secretory organelles known as rhoptries, making these organelles essential for parasite survival and attractive targets for new antimalarial therapies. We are investigating the molecular mechanisms that control rhoptry biogenesis and function. Rhoptries are assembled during parasite replication and mature into highly organized organelles consisting of a bulb and a narrow neck, each containing distinct sets of proteins that are released in a tightly regulated sequence during red blood cell invasion. A major focus of our research is the essential rhoptry-localized aspartic protease Plasmepsin IX (PM IX). We have shown that parasites lacking PM IX form defective rhoptries that are unable to discharge their contents, rendering the parasites incapable of invading red blood cells. We are investigating how PM IX regulates rhoptry maturation by processing key proteins required for organelle development.

Our research investigates the molecular mechanisms that enable Plasmodium falciparum to escape from infected red blood cells, a critical step required for parasite survival, replication, and disease progression. We focus on the essential protease SUB1, which triggers a cascade of events leading to the rupture of the parasitophorous vacuole and host cell membranes during parasite egress. Using cell biology, genetics, and biochemical approaches, we aim to define how SUB1 coordinates these membrane disruption events and identify the proteins involved. This work will advance our understanding of a fundamental stage of the malaria parasite life cycle and may reveal new targets for the development of antimalarial therapies.