The aspartic proteinase from the rodent parasite Plasmodium berghei as a potential model for plasmepsins from the human malaria parasite, Plasmodium falciparum
Mj. Humphreys et al., The aspartic proteinase from the rodent parasite Plasmodium berghei as a potential model for plasmepsins from the human malaria parasite, Plasmodium falciparum, FEBS LETTER, 463(1-2), 1999, pp. 43-48
The gene encoding an aspartic proteinase precursor (proplasmepsin) from the
rodent malaria parasite Plasmodium berghei has been cloned. Recombinant P.
berghei plasmepsin hydrolysed a synthetic peptide substrate and this cleav
age nas prevented by the general aspartic proteinase inhibitor, isovaleryl
pepstatin and by Ro40-3388, a lead compound for the inhibition of plasmepsi
ns from the human malaria parasite Plasmodium falciparum. Southern blotting
detected only one proplasmepsin gene in P, berghei. Two plasmepsins have p
reviously been reported in P, falciparum. Here, we describe two further pro
plasmepsin genes from this species. The suitability of P, berghei as a mode
l for the in vivo evaluation of plasmepsin inhibitors is discussed. (C) 199
9 Federation of European Biochemical Societies.