ArticleParasitology research2003
Targeting enzymes involved in spermidine metabolism of parasitic protozoa--a possible new strategy for anti-parasitic treatment.
Article in Parasitology research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 29 citations in OpenAlex.
- A suggested vital function for eIF-5A and dhs genes during murine malaria blood-stage infection.FEBS open bio · 2016Article
- Systemic overexpression of antizyme 1 in mouse reduces ornithine decarboxylase activity without major changes in tissue polyamine homeostasis.Transgenic research · 2014Article
- In vitro and in vivo silencing of plasmodial dhs and eIf-5a genes in a putative, non-canonical RNAi-related pathway.BMC microbiology · 2012Article
- In Vitro and In Vivo Antimalarial Activity Assays of Seeds from Balanites aegyptiaca: Compounds of the Extract Show Growth Inhibition and Activity against Plasmodial Aminopeptidase.Journal of parasitology research · 2011Article
- Plasmodium falciparum spermidine synthase inhibition results in unique perturbation-specific effects observed on transcript, protein and metabolite levels.BMC genomics · 2010Article
- The guanylhydrazone CNI-1493: an inhibitor with dual activity against malaria-inhibition of host cell pro-inflammatory cytokine release and parasitic deoxyhypusine synthase.Parasitology research · 2008Article
- Cloning, expression and functional activity of deoxyhypusine synthase from Plasmodium vivax.BMC microbiology · 2006Article
- Piperidones with activity against Plasmodium falciparum.Parasitology research · 2006Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sequencing data obtained from the Plasmodium, Anopheles gambiae and human genome projects provide a new basis for drug and vaccine development. One of the most characteristic features in the process of drug development against parasitic protozoa is target identification in a biological pathway. The next step must be a structure-based rational drug design if the target is not only present in the parasite. In mouse models of malaria, such drugs should be tested for efficacy of the new therapies. Here, we present data that pinpoint the existence of two enzymes of the polyamine pathway involved in spermidine metabolism in P. falciparum, i.e. deoxyhypusine synthase (DHS; EC 1.1.1.249) and homospermidine synthase (HSS; EC 2.5.1.45). Recent data obtained from the malaria genome databases showed that at least a putative gene encoding DHS is present in the parasite. Sequencing data from the P. falciparum genome project prove that the eukaryotic initiation factor eIF5A (the substrate for DHS) exists in P. falciparum. Here, we present the amino acid sequence of eIF5A from P. vivax, which causes tertiary malaria. EIF5A from P. vivax shows 82% nucleic acid and 97% amino acid identity to its homologue from P. falciparum. GC/MS data and inhibitor studies with agmatine prove that the triamine homospermidine occurs in the parasite. These data suggest a separate locus encoding HSS in P. falciparum. The hss gene recruits from the dhs gene in eukaryotes. Here, we present genomic DNA fragments obtained by amplification with primers of a conserved region (amino acid positions 550-1,043) between the putative P. falciparum DHS gene ( dhs) and the HSS gene ( hss) from the plant Senecio vulgaris (Asteraceae). The amplification product from different P. falciparum strains reveals differences in sequence identity, compared with the putative dhs gene from P. falciparum strain 3D7. Expression of the full-length clone and determination of HSS-specific activity will finally prove whether a separate region encoding HSS exists.
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