ArticleScientific reports2017
The antimalarial activity of the pantothenamide α-PanAm is via inhibition of pantothenate phosphorylation.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers, 1 of them a synthesis that pooled it.
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Who cites it
7 citing papers in PubMed, 1 synthesis or guideline pooled it, 16 citations in OpenAlex.
- Plasmodial Kinase Inhibitors Targeting Malaria: Recent Developments.Molecules (Basel, Switzerland) · 2020Pooled it
- Article
- Evidence for a Conserved Function of Eukaryotic Pantothenate Kinases in the Regulation of Mitochondrial Homeostasis and Oxidative Stress.International journal of molecular sciences · 2022Article
- High-resolution crystal structure and chemical screening reveal pantothenate kinase as a new target for antifungal development.Structure (London, England : 1993) · 2022Article
- Preclinical characterization and target validation of the antimalarial pantothenamide MMV693183.Nature communications · 2022Article
- A novel heteromeric pantothenate kinase complex in apicomplexan parasites.PLoS pathogens · 2021Article
- The yeast pantothenate kinase Cab1 is a master regulator of sterol metabolism and of susceptibility to ergosterol biosynthesis inhibitors.The Journal of biological chemistry · 2019Article
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Authors and funding
13 authors at 4 institutions in 1 country.
Funding
Abstract
The biosynthesis of the major acyl carrier Coenzyme A from pantothenic acid (PA) is critical for survival of Plasmodium falciparum within human erythrocytes. Accordingly, a PA analog α-PanAm showed potent activity against blood stage parasites in vitro; however, its efficacy in vivo and its mode of action remain unknown. We developed a new synthesis route for α-PanAm and showed that the compound is highly effective against blood stages of drug-sensitive and -resistant P. falciparum strains, inhibits development of P. berghei in hepatocytes, and at doses up to 100 mg/kg also inhibits blood stage development of P. chabaudi in mice. We used yeast and its pantothenate kinase Cab1 as models to characterize mode of action of α-PanAm and found that α-PanAm inhibits yeast growth in a PA-dependent manner, and its potency increases dramatically in a yeast mutant with defective pantothenate kinase activity. Biochemical analyses using
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