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.
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.
Florent
I
I
Laboratoire de Biologie Parasitaire et Chimiothérapie, URA CNRS 114, Muséum National d'Histoire Naturelle, France.
Le Bonniec
S
S
Carcy
B
B
Grellier
P
P
Mercereau-Puijalon
O
O
Bonnefoy
S
S
Dhermy
D
D
Monsigny
M
M
Mayer
R
R
Schrével
J
J
D000818:Animals; D010450:Endopeptidases / Q000378:metabolism*; D004912:Erythrocytes / Q000469:parasitology; D017125:Genes, Protozoan / Q000235:genetics; D010963:Plasmodium falciparum / Q000201:enzymology* / Q000235:genetics; D011817:Rabbits; D013049:Spectrin / Q000008:administration & dosage
D013049:Spectrin; D010450:Endopeptidases; C084242:acidic proteinase Pf37, Plasmodium falciparum