Cloning and characterization of a Plasmodium falciparum cyclophilin gene that is stage-specifically expressed
Identifieur interne : 002B19 ( Main/Exploration ); précédent : 002B18; suivant : 002B20Cloning and characterization of a Plasmodium falciparum cyclophilin gene that is stage-specifically expressed
Auteurs : G. Roman Reddy [États-Unis]Source :
- Molecular & Biochemical Parasitology [ 0166-6851 ] ; 1995.
English descriptors
- Teeft :
- Acad, Additional sequence, Amino, Amino acid, Amino acids, Antimalarial, Antimalarial activity, Approx, Assay, Biochemical parasitology, Biol, Capital letters, Cdna, Cdna clones, Cdna sequence, Clone, Coding sequence, Coli, Cyclophilin, Cyclophilins, Cyclosporin, Falciparum, Falciparum cyclophilin, Falciparum growth, Falciparum strains, Filter hybridization, Genomic, Human cyclophilin, Human cyclophilins, Hybridization, Initiation codon, Isomerase, Malaria, Mature protein, Multiple sequence alignment, Natl, Northern blot analysis, Nucleic acids, Nucleotide sequence, Parasite, Parasite growth, Parasitology, Peptide, Pet9a, Pet9a vector, Pfcyp, Pfcyp gene product, Pfcyp transcript, Plasmodium, Plasmodium species, Ppiase, Ppiase activity, Primer, Proc, Reddy, Several species, Signal peptide, Signal sequence, Time points.
Abstract
Abstract: An immunosuppressive agent, cyclosporin A (CsA), has antimalarial activity in several Plasmodium species. Cyclophilins of several species including Plasmodium falciparum exhibit peptidyl-prolyl cis-trans isomerase activity which is inhibited by CsA. A gene encoding P. falciparum cyclophilin (PFCyP) was cloned and characterized. This gene has the entire coding sequence for the mature protein plus a 39-amino-acid-long N-terminal extension. Most of the amino acids predicted to be involved in the peptidyl-prolyl cis-trans isomerase activity and CsA binding are present in the cloned gene. The PFCyP also has the single highly conserved tryptophan residue that is a major determinant in the inhibition of PPIase activity by CsA. The PFCyP coding sequence with or without the N-terminal amino-acid extension was used to construct recombinant expression vectors which were transformed into E. coli. Both vectors produced enzymatically active mature PFCyP proteins that were sensitive to CsA. Northern blot analysis of RNA isolated from the synchronized parasite cultures verified the expression of PFCyP in all erythrocytic stages of the parasite, but at variable levels. The highest level of expression was observed in ring-stage parasites, a stage shown to be more susceptible to CsA. Inhibition of P. falciparum growth in vitro by CsA was re-evaluated for chloroquine-sensitive and chloroquine-resistant strains of the parasite. Essentially, there was no difference between the two strains for the concentration of CsA required to yield 50% inhibition in 48 h of exposure (0.25-0.4 μM).
Url:
DOI: 10.1016/0166-6851(95)00103-8
Affiliations:
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Le document en format XML
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<front><div type="abstract" xml:lang="en">Abstract: An immunosuppressive agent, cyclosporin A (CsA), has antimalarial activity in several Plasmodium species. Cyclophilins of several species including Plasmodium falciparum exhibit peptidyl-prolyl cis-trans isomerase activity which is inhibited by CsA. A gene encoding P. falciparum cyclophilin (PFCyP) was cloned and characterized. This gene has the entire coding sequence for the mature protein plus a 39-amino-acid-long N-terminal extension. Most of the amino acids predicted to be involved in the peptidyl-prolyl cis-trans isomerase activity and CsA binding are present in the cloned gene. The PFCyP also has the single highly conserved tryptophan residue that is a major determinant in the inhibition of PPIase activity by CsA. The PFCyP coding sequence with or without the N-terminal amino-acid extension was used to construct recombinant expression vectors which were transformed into E. coli. Both vectors produced enzymatically active mature PFCyP proteins that were sensitive to CsA. Northern blot analysis of RNA isolated from the synchronized parasite cultures verified the expression of PFCyP in all erythrocytic stages of the parasite, but at variable levels. The highest level of expression was observed in ring-stage parasites, a stage shown to be more susceptible to CsA. Inhibition of P. falciparum growth in vitro by CsA was re-evaluated for chloroquine-sensitive and chloroquine-resistant strains of the parasite. Essentially, there was no difference between the two strains for the concentration of CsA required to yield 50% inhibition in 48 h of exposure (0.25-0.4 μM).</div>
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