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Plasmodium falciparum PfMyoF contains a Rab-like tail domain and associates with perinuclear membrane trafficking

Alexander J Holmes1, Philip Ilani1,2, Christopher Batters1

  • 1Cambridge Institute for Medical Research, Department of Clinical Biochemistry, University of Cambridge, Cambridge Biomedical Campus, The Keith Peters Building, Cambridge, UK.

Communications Biology
|May 15, 2026
PubMed

Insights

This study characterizes Plasmodium falciparum myosin F (PfMyoF), revealing it as a unique motor protein involved in parasite growth. PfMyoF

Area of Science:

  • Parasitology
  • Molecular Biology
  • Cell Biology

Background:

  • Myosins are essential motor proteins found in all eukaryotes.
  • Plasmodium falciparum, the parasite causing severe malaria, encodes six myosins, but most are uncharacterized.
  • Understanding Plasmodium falciparum myosins is crucial for targeting parasite development.

Purpose of the Study:

  • To characterize PfMyoF, a previously unstudied myosin from Plasmodium falciparum.
  • To elucidate the structure, function, and cellular localization of PfMyoF.
  • To investigate the role of PfMyoF in parasite growth and membrane trafficking.

Main Methods:

  • Structural prediction and biochemical assays to define PfMyoF motor properties.
  • Imaging techniques including expansion and immunoelectron microscopy for localization.
  • Protein interaction studies (pull-down assays) and gene knockdown (glmS ribozyme) to assess function.

Main Results:

  • PfMyoF is a plus-end-directed, processive motor with a unique tail containing WD40 and Rab-like domains.
  • PfMyoF interacts with trafficking proteins, including PfRab18, and localizes to a perinuclear membrane compartment.
  • Transient knockdown of PfMyoF impairs parasite growth, suggesting a role in asexual replication.

Conclusions:

  • PfMyoF is the first identified myosin with a Rab-like domain, expanding myosin classification.
  • PfMyoF likely plays a significant role in membrane trafficking during Plasmodium falciparum blood-stage development.
  • PfMyoF represents a potential new target for antimalarial therapies.

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