Florent I, Le Bonniec S, Carcy B, Grellier P, Mercereau-Puijalon O, Bonnefoy S, Dhermy D, Monsigny M, Mayer R, Schrével J
Laboratoire de Biologie Parasitaire et Chimiothérapie, URA CNRS 114, Muséum National d'Histoire Naturelle, France.
Mem Inst Oswaldo Cruz. 1994;89 Suppl 2:47-9. doi: 10.1590/s0074-02761994000600012.
Numerous proteinase activities have been shown to be essential for the survival of Plasmodium falciparum. One approach to antimalarial chemotherapy, would be to block specifically one or several of these activities, by using compounds structurally analogous to the substrates of these proteinases. Such a strategy requires a detailed knowledge of the active site of the proteinase, in order to identify the best substrate for the proteinase. Aiming at developing such a strategy, two proteinases previously identified in our laboratory, were chosen for further characterization of their molecular structure and properties: the merozoite proteinase for erythrocytic invasion (MPEI), involved in the erythrocyte invasion by the merozoites, and the Pf37 proteinase, which hydrolyses human spectrin in vitro.
已证明许多蛋白酶活性对于恶性疟原虫的存活至关重要。抗疟化疗的一种方法是通过使用结构类似于这些蛋白酶底物的化合物来特异性阻断其中一种或几种活性。这种策略需要对蛋白酶的活性位点有详细的了解,以便确定蛋白酶的最佳底物。为了开发这样一种策略,我们选择了先前在我们实验室中鉴定出的两种蛋白酶,对其分子结构和性质进行进一步表征:参与裂殖子侵入红细胞的红细胞侵入裂殖子蛋白酶(MPEI),以及在体外水解人血影蛋白的Pf37蛋白酶。