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Plasmodium falciparum PfMyoF with a Rab-like tail domain associates with perinuclear membranes and trafficking proteins

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 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.

INSTRUMENT(S):

ORGANISM(S): Plasmodium (paraplasmodium)

TISSUE(S): Blood Cell, Cell Culture

DISEASE(S): Malaria

SUBMITTER: Robin Antrobus

LAB HEAD: Folma Buss

PROVIDER: PXD077305 | Pride | 2026-04-27

REPOSITORIES: Pride

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			Action	DRS
	FB_AH_CoIP20251_F1_2.raw	Raw
	FB_AH_CoIP20251_F2_2.raw	Raw
	FB_AH_CoIP20251_F3_2.raw	Raw
	FB_AH_CoIP20251_Fmore_2.raw	Raw
	FB_AH_CoIP20251_MyoK_2.raw	Raw

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