PfMyoF is a class XXII myosin with a unique Rab-like tail domain that associates with perinuclear membrane trafficking proteins and is important for asexual replication in Plasmodium falciparum.
PfMyoF is the first identified myosin with a Rab-like domain, playing a potential role in membrane trafficking and asexual replication in Plasmodium falciparum.
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 eukarytotic 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 in 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.
Buß et al. (Wed,) conducted a other in Malaria (Plasmodium falciparum). PfMyoF characterization was evaluated. PfMyoF is a class XXII myosin with a unique Rab-like tail domain that associates with perinuclear membrane trafficking proteins and is important for asexual replication in Plasmodium falciparum.