ArticleScientific reports2015
Structure, function and inhibition of the phosphoethanolamine methyltransferases of the human malaria parasites Plasmodium vivax and Plasmodium knowlesi.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- Mass spectrometry-based metabolomics uncovers distinct metabolic signatures and potential therapeutic targets in Plasmodium knowlesi.PloS one · 2025Article
- Sexual differentiation in human malaria parasites is regulated by competition between phospholipid metabolism and histone methylation.Nature microbiology · 2023Article
- A non-canonical sensing pathway mediates Plasmodium adaptation to amino acid deficiency.Communications biology · 2023Article
- Adapt or Die: Targeting Unique Transmission-Stage Biology for Malaria Elimination.Frontiers in cellular and infection microbiology · 2022Review
- Synthesis, Molecular Docking and Antiplasmodial Activities of New Tetrahydro-β-Carbolines.International journal of molecular sciences · 2021Article
- Article
- Role of phospholipid synthesis in the development and differentiation of malaria parasites in the blood.The Journal of biological chemistry · 2018Review
- Allosteric Site Inhibitor Disrupting Auto-Processing of Malarial Cysteine Proteases.Scientific reports · 2018Article
- A novel fluorescence assay for measuring phosphatidylserine decarboxylase catalysis.The Journal of biological chemistry · 2018Article
- Review
- Phosphoethanolamine-N-methyltransferase is a potential biomarker for the diagnosis of P. knowlesi and P. falciparum malaria.PloS one · 2018Article
- Conformational changes in the di-domain structure ofThe Journal of biological chemistry · 2017Article
- Structural and Functional Studies of Pavine N-Methyltransferase from Thalictrum flavum Reveal Novel Insights into Substrate Recognition and Catalytic Mechanism.The Journal of biological chemistry · 2016Article
- Radical cure of experimental babesiosis in immunodeficient mice using a combination of an endochin-like quinolone and atovaquone.The Journal of experimental medicine · 2016Article
- Characterization of Plasmodium phosphatidylserine decarboxylase expressed in yeast and application for inhibitor screening.Molecular microbiology · 2016Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
Abstract
Phosphoethanolamine methyltransferases (PMTs) catalyze the three-step methylation of phosphoethanolamine to form phosphocholine, a critical step in the synthesis of phosphatidylcholine in a select number of eukaryotes including human malaria parasites, nematodes and plants. Genetic studies in the malaria parasite Plasmodium falciparum have shown that the methyltransferase PfPMT plays a critical function in parasite development and differentiation. The presence of PMT orthologs in other malaria parasites that infect humans and their absence in mammals make them ideal targets for the development of selective antimalarials with broad specificity against different Plasmodium species. Here we describe the X-ray structures and biochemical properties of PMT orthologs from Plasmodium vivax and Plasmodium knowlesi and show that both enzymes are inhibited by amodiaquine and NSC158011, two drugs with potent antimalarial activity. Metabolic studies in a yeast mutant that relies on PkPMT or PvPMT for survival demonstrated that these compounds inhibit phosphatidylcholine biosynthesis from ethanolamine. Our structural and functional data provide insights into the mechanism of catalysis and inhibition of PMT enzymes and set the stage for a better design of more specific and selective antimalarial drugs.
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