Plasmodium falciparum Myosin B is a slow motor optimized for force generation
Abstract
Malaria is a disease caused by apicomplexan parasites of the genus Plasmodium. These organisms express two atypical class-XIV myosins: Myosin A (MyoA), a core component of the glideosome expressed throughout the entire lifecycle, and Myosin B (MyoB), which is restricted to invasive stages and localizes to the apical region. Here, we determine the crystal structure of Plasmodium falciparum MyoB (PfMyoB) in the Rigor state and identify its essential light chain as the same subunit bound to MyoA. Combining structural analysis, molecular dynamics simulations and in vitro kinetic and motility assays, we show that PfMyoB is a slow motor optimized for force production during invasion. The Nterminal extensions of PfMyoA and PfMyoB exert distinct effects on each motor's mechanochemistry. Altogether, these findings reveal how Plasmodium myosins have evolved specialized functions during the complex parasite lifecycle and provide insight into developing multi-target inhibitors of erythrocytic invasion based on the PfMyoA inhibitor KNX-002.
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BibTeX
@misc{robblee2026plasmodium,
title = {{Plasmodium falciparum Myosin B is a slow motor optimized for force generation}},
author = {James P Robblee and Dihia Moussaoui and Carol S Bookwalter and Daniel Auguin and Patricia M Fagnant and Jill E Macfarlane and Michael J Previs and Anne Houdusse and Kathleen M Trybus and Julien Robert-Paganin},
howpublished = {HAL},
year = {2026},
month = sep,
doi = {10.64898/2026.09.11.750570},
url = {https://hal.science/hal-05748494v1},
note = {CC BY-NC-ND 4.0},
}
RIS
TY - UNPB
TI - Plasmodium falciparum Myosin B is a slow motor optimized for force generation
AU - James P Robblee
AU - Dihia Moussaoui
AU - Carol S Bookwalter
AU - Daniel Auguin
AU - Patricia M Fagnant
AU - Jill E Macfarlane
AU - Michael J Previs
AU - Anne Houdusse
AU - Kathleen M Trybus
AU - Julien Robert-Paganin
PY - 2026
DA - 2026/09/11
PB - HAL
DO - 10.64898/2026.09.11.750570
UR - https://hal.science/hal-05748494v1
AB - Malaria is a disease caused by apicomplexan parasites of the genus Plasmodium. These organisms express two atypical class-XIV myosins: Myosin A (MyoA), a core component of the glideosome expressed throughout the entire lifecycle, and Myosin B (MyoB), which is restricted to invasive stages and localizes to the apical region. Here, we determine the crystal structure of Plasmodium falciparum MyoB (PfMyoB) in the Rigor state and identify its essential light chain as the same subunit bound to MyoA. Combining structural analysis, molecular dynamics simulations and in vitro kinetic and motility assays, we show that PfMyoB is a slow motor optimized for force production during invasion. The Nterminal extensions of PfMyoA and PfMyoB exert distinct effects on each motor's mechanochemistry. Altogether, these findings reveal how Plasmodium myosins have evolved specialized functions during the complex parasite lifecycle and provide insight into developing multi-target inhibitors of erythrocytic invasion based on the PfMyoA inhibitor KNX-002.
ER -