ArticleNature communications2023
Mechanism of small molecule inhibition of Plasmodium falciparum myosin A informs antimalarial drug design.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 13 citations in OpenAlex.
- Article
- Antimalarial cytoskeletal targeting with broad apicomplexan activity.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Identification of UCB-9721 as a potent inhibitor of MyoA, the essential class XIV myosin motor of apicomplexan parasites.bioRxiv : the preprint server for biology · 2026Article
- Plasmodium falciparum PfMyoF contains a Rab-like tail domain and associates with perinuclear membrane trafficking proteins.Communications biology · 2026Article
- Targeting protein-protein interactions in Plasmodium: from asexual replication to sexual development.Parasites & vectors · 2026Review
- ATPγS substantially defeats the biasing mechanism for kinesin steps.Nature communications · 2026Article
- Please inhibit responsibly: Natural and synthetic actin toxins as useful tools in cell biology.Molecular biology of the cell · 2025Review
- Structure and Functions of Actin and Actin-Binding Proteins inPathogens (Basel, Switzerland) · 2025Review
- Motility-dependent processes inmSphere · 2025Article
- Identification and biophysical characterization of Plasmodium peptide binding by common African HLAs.Scientific reports · 2025Article
- Motility-dependent processes inbioRxiv : the preprint server for biology · 2024Article
- Omecamtiv mecarbil and Mavacamten target the same myosin pocket despite opposite effects in heart contraction.Nature communications · 2024Article
- Omecamtiv mecarbil and Mavacamten target the same myosin pocket despite antagonistic effects in heart contraction.bioRxiv : the preprint server for biology · 2023Article
- MyosinA is a druggable target in the widespread protozoan parasite Toxoplasma gondii.PLoS biology · 2023Article
Corrections and comments
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Authors and funding
13 authors at 6 institutions in 4 countries.
Funding
Abstract
Malaria results in more than 500,000 deaths per year and the causative Plasmodium parasites continue to develop resistance to all known agents, including different antimalarial combinations. The class XIV myosin motor PfMyoA is part of a core macromolecular complex called the glideosome, essential for Plasmodium parasite mobility and therefore an attractive drug target. Here, we characterize the interaction of a small molecule (KNX-002) with PfMyoA. KNX-002 inhibits PfMyoA ATPase activity in vitro and blocks asexual blood stage growth of merozoites, one of three motile Plasmodium life-cycle stages. Combining biochemical assays and X-ray crystallography, we demonstrate that KNX-002 inhibits PfMyoA using a previously undescribed binding mode, sequestering it in a post-rigor state detached from actin. KNX-002 binding prevents efficient ATP hydrolysis and priming of the lever arm, thus inhibiting motor activity. This small-molecule inhibitor of PfMyoA paves the way for the development of alternative antimalarial treatments.
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Registered trials
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