PfMyoF is a plus-end-directed, processive motor containing a novel Rab-like tail domain that associates with perinuclear membrane trafficking proteins in Plasmodium falciparum.
PfMyoF is the first myosin identified with a Rab-like domain and plays a potential role in membrane trafficking during the pathogenic blood stages of Plasmodium falciparum.
Abstract Members of the myosin superfamily are found in all eukaryotes, including Plasmodium falciparum , the parasite that causes the majority of severe malaria. The P. falciparum genome encodes six myosins, but apart from PfMyoA and B, these remain largely uncharacterised. Here, we characterise PfMyoF, a class XXII myosin, using structural prediction, biochemical assays, and imaging. We show that PfMyoF is a plus-end-directed, processive motor with a long neck region with capacity to bind up to six copies of the calmodulin homologue PfCaM. The PfMyoF tail contains predicted WD40 and Rab-like domains that have not been identified in any other eukaryotic myosin class. Pull-down experiments identify PfMyoF interactions with trafficking proteins, including the vesicle marker PfRab18. Expansion and immunoelectron microscopy reveal that PfMyoF localises to a perinuclear membrane compartment and transient knockdown using the glmS ribozyme system impairs growth, potentially indicating an important function during asexual replication. Our findings define PfMyoF as the first myosin with a Rab-like domain and highlight its potential role in membrane trafficking pathways during the pathogenic blood stages of parasite development.
Holmes et al. (Fri,) conducted a other in Malaria (Plasmodium falciparum). PfMyoF is a plus-end-directed, processive motor containing a novel Rab-like tail domain that associates with perinuclear membrane trafficking proteins in Plasmodium falciparum.