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Plasmodium falciparum proteinases: cloning of the putative gene coding for the merozoite proteinase for erythrocyte invasion (MPEI) and determination of hydrolysis sites of spectrin by Pf37 proteinase

Abstract

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.

Plasmodium falciparum; proteinases; spectrin; erythrocyte invasion


ABSTRACT

Plasmodium falciparum proteinases: cloning of the putative gene coding for the merozoite proteinase for erythrocyte invasion (MPEI) and determination of hydrolysis sites of spectrin by Pf37 proteinase

I. Florent1

S. Le Bonniec1

B. Carcy1

P. Grellier1

O. Mercereau-Puijalon2

S. Bonnefoy3

D. Dhermy4

M. Monsigny5

R. Mayer1

J. Schrével1

URA CNRS 114, Laboratoire de Biologie Parasitaire et Chimiothérapie, France

Institut Pasteur, Laboratoire de Parasitologie Expérimentale, Paris, France

Institut Pasteur, Laboratoire de Parasitologie Laboratoire de Parasitologie, Paris, France

ISERM U. 160, Laboratorie de Pathologie Cellulaire et Moleculaire en Hematologie, France

Département de Biochimie des Glycoconjugués, Centre de Biophysique Moleculaire CNRS, France

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.

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Publication Dates

  • Publication in this collection
    15 June 2009
  • Date of issue
    1994
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