Abstract
In the recent article in Parasitology Today by Thierry Meinnel, a putative peptide deformylase (PDF) gene was identified in the Plasmodium falciparum genome and was suggested as a new target for antiparasitic therapy 1. Meinnel T Peptide deformylase of eukaryotic protists: A target for new antiparasitic agents?. Parasitol. Today. 2000; 16: 165-168 Abstract Full Text Full Text PDF PubMed Scopus (66) Google Scholar . Following the same approach, we have tested the antimalarial activity of the antibiotic actinonin, which was described as a potent inhibitor of bacterial PDF ( 2. Chen D.Z et al. Actinonin, a naturally occurring antibacterial agent, is a potent deformylase inhibitor. Biochemistry. 2000; 39: 1256-1262 Crossref PubMed Scopus (279) Google Scholar ). P. falciparum-infected erythrocytes were incubated in an isotopic microdilution assay with actinonin for 48 h before the addition of [3H]hypoxanthine for a further 24 h. The determined concentrations of actinonin causing half-maximal growth inhibition (IC50) were 3.0 μm for the wild-type P. falciparum strain 3D7 and 3.6 μm for the multidrug-resistant strain Dd2. In a rodent malaria model with Plasmodium vinckei-infected mice, no antimalarial activity was observed when actinonin was administrated daily with a dosage of 300 mg kg−1 by intraperitoneal injection. The failure to cure malaria with actinonin in the rodent model is most likely attributed to the relatively high IC50 of actinonin compared with standard antimalarials. Nevertheless, actinonin representsan interesting lead compound for the development of new antimalarial drugs.
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