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Significance The unicellular apicomplexan parasite,Plasmodium falciparum , causes malaria in humans that results in &gt;400,000 deaths per year. The parasite must produce force and motion to progress through its lifecycle and cause disease. The core of the macromolecular complex that powers invasion and motile stages consists of a unique single-headed myosin and a divergent actin (Pf Act1). We used total internal reflection fluorescence microscopy to visualize polymerization of individualPf Act1 filaments in real time in the absence of stabilizing agents. The unique dynamic properties of both ends of the polar filament, and the high actin concentration needed for it to polymerize, provide a molecular explanation for why these filaments have been notoriously hard to visualize both in vitro and in the parasite.

Unusual dynamics of the divergent malaria parasite Pf Act1 actin filament