Structural and functional studies on Plasmodium actin-myosin class XIV motors

Malaria, a disease caused by parasites, is responsible for almost half a million deaths worldwide every year. For the parasite to survive, it requires motility. This work investigated the biochemical and structural properties of motor proteins called myosins and other proteins involved in the parasite molecular motor machinery. The major findings of this work were that: (i) parasite-specific chaperones and myosin light chains are essential for myosin stability and function; (ii) myosin light chains are naturally extended proteins and their interactions with other motor complex proteins are difficult to reconstitute in vitro; (iii) parasite myosins have degenerated binding sites to allow for redundant myosin light chain binding; (iv) at least one of the motor complex proteins is a potential target for drug discovery; and (v) a new actin filament stabilizing protein was described. Altogether, this work has shed light on several proteins involved in the malaria parasite's ability to move and invade human cells.