This research aimed to molecularly analyze the glideosome complex in the parasites Toxoplasma and Plasmodium, comparing it with apicomplexans of interest in arthropods of agricultural importance (such as gregarines), to identify relevant structural and functional similarities and differences in their motility and potential therapeutic targets. Through a systematic review of databases (PubMed, Google Scholar, NCBI, PDB) and comparative analysis of amino acid sequences, we evaluated whether the molecular conformation of the glideosome in arthropod apicomplexans bears similarities to those of medical relevance. The glideosome, essential for gliding locomotion, a movement without morphological changes that facilitates cell invasion, is composed of proteins such as Myosin A (MyoA), its light chain (MLC1/MTIP), and the proteins GAP45 and GAP50. Post-translationally modified (myristoylation, palmitoylation), the latter act as anchors between the motor complex and the parasite's inner membrane. The study revealed notable differences: Toxoplasma gondii MyoA has 1,810 amino acids, while in Gregarina polymorpha it reaches 2,846, suggesting evolutionary adaptations linked to their niches (invasion of mammalian cells vs. extracellular environments in arthropods). Despite these divergences, conserved domains were identified in MyoA, indicating a common functional core for motility. These findings support that the glideosome is an ancestral system optimized for invasion, but with structural variations that reflect ecological pressures. The comparison among apicomplexans positions this complex as a key model for studying pathogenicity mechanisms and developing broad or specific control strategies, depending on the differences identified. This work underscores the importance of comparative approaches for understanding the evolution of molecular systems in parasites with a medical and agricultural impact.