Plasmodium falciparum, the deadliest malaria parasite, poses a significant global health threat. Belonging to the Apicomplexa phylum, Plasmodium parasites have an apical complex crucial for motility and host cell invasion. The conoid, a dynamic organelle of elusive function composed of spiraling tubulin fibers, was previously thought to be lost in Plasmodium. Recent evidence from the host laboratory challenges this belief, identifying conoid complex proteins and an apical tubulin ring (ATR) in the ookinete stage responsible for colonizing the mosquito midgut. Preliminary investigations suggest a further reduction of the conoid complex at the merozoite stage, responsible for invading human red blood cells. This master’s thesis explores the conoid complex in P. falciparum merozoites, examining the expression of key components shared with other apicomplexan parasites, such as Myosin B (MyoB), double-cortin domain (DCX), and apical annuli protein 4 (AAP4). Using expansion microscopy (U-ExM), we confirm the expression of a conoid complex by observing a MyoB-GFP ring. However, no tubulin ring is observed, suggesting a reductive evolution of the conoid complex at the merozoite stage. In addition, we provide evidence that DCX plays an unexpected role in a distinct noninvasive stage that does not express a conoid. Generating a mixed population of PfAAP4-DiCre-HA parasites marked a significant step in understanding AAP4's role in the conoid complex. Our findings reveal that the conoid complex in P. falciparum merozoites is minimally conserved and that conoid proteins might be repurposed in non-invasive stages.