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>The aspartic proteinase from the rodent parasite Plasmodium berghei as a potential model for plasmepsins from the human malaria parasite, Plasmodium falciparum
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The aspartic proteinase from the rodent parasite Plasmodium berghei as a potential model for plasmepsins from the human malaria parasite, Plasmodium falciparum
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 was prevented by the general aspartic proteinase inhibitor, isovaleryl pepstatin and by Ro40-4388, 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.
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机译:编码来自啮齿动物疟疾寄生虫伯氏疟原虫的天冬氨酸蛋白酶前体(原质丙肽)的基因已被克隆。重组 P. berghei 纤溶蛋白酶水解合成肽底物,一般天冬氨酸蛋白酶抑制剂异戊酰胃蛋白酶抑制剂和 Ro40-4388(一种用于抑制人类疟疾寄生虫恶性疟原虫纤溶蛋白酶的先导化合物)阻止了这种裂解。Southern 印迹在 P. berghei 中仅检测到一个原生肌蛋白酶基因。先前在恶性疟原虫中报道了两种纤溶蛋白酶。在这里,我们描述了来自该物种的另外两个原质蛋白酶基因。讨论了 P. berghei 作为纤溶蛋白酶抑制剂体内评估模型的适用性。
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