The aspartic proteinase from the rodent parasite Plasmodium berghei as a potential model for plasmepsins from the human malaria parasite, Plasmodium falciparum

Citation
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
Citations number
17
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
463
Issue
1-2
Year of publication
1999
Pages
43 - 48
Database
ISI
SICI code
0014-5793(199912)463:1-2<43:TAPFTR>2.0.ZU;2-6
Abstract
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.