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

被引:37
作者
Humphreys, MJ
Moon, RP
Klinder, A
Fowler, SD
Rupp, K
Bur, D
Ridley, RG
Berry, C
机构
[1] Cardiff Univ, Cardiff Sch Biosci, Cardiff CF1 3US, S Glam, Wales
[2] F Hoffmann La Roche & Co Ltd, Div Pharmaceut, Pharma Res Preclin, Basel, Switzerland
关键词
aspartic proteinase; plasmepsin; malaria; Plasmodium berghei; Plasmodium falciparum;
D O I
10.1016/S0014-5793(99)01597-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 cleavage nas prevented by the general aspartic proteinase inhibitor, isovaleryl pepstatin and by Ro40-3388, a lead compound for the inhibition of plasmepsins from the human malaria parasite Plasmodium falciparum. Southern blotting detected only one proplasmepsin gene in P, berghei. Two plasmepsins have previously been reported in P, falciparum. Here, we describe two further proplasmepsin genes from this species. The suitability of P, berghei as a model for the in vivo evaluation of plasmepsin inhibitors is discussed. (C) 1999 Federation of European Biochemical Societies.
引用
收藏
页码:43 / 48
页数:6
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