Plasmodium chabaudi p68 serine protease activity required for merozoite entry into mouse erythrocytes.
To define the role of malaria parasite enzymes during the process of erythrocyte invasion, we have developed an in vitro serum-free invasion assay of mouse erythrocytes by purified Plasmodium chabaudi merozoites. The sensitivity of a merozoite-specific serine protease (p68) to various inhibitors and the effect of these inhibitors on invasion indicate a crucial role for p68. The substrate specificity of the purified enzyme has been partially defined using fluorogenic peptides. Consistent with this, in vitro incubation of mouse erythrocytes with the merozoite enzyme led to the cleavage of band 3 protein. The possible implication of erythrocyte band 3 truncation for the successful entry of the merozoite into the erythrocyte is discussed.
Breton
C B
CB
Unit of Experimental Parasitology, Institut Pasteur, Paris, France.
Blisnick
T
T
Jouin
H
H
Barale
J C
JC
Rabilloud
T
T
Langsley
G
G
Pereira da Silva
L H
LH
D000818:Animals; D001457:Anion Exchange Protein 1, Erythrocyte / Q000378:metabolism; D004910:Erythrocyte Membrane / Q000378:metabolism; D004912:Erythrocytes / Q000469:parasitology*; D051379:Mice; D008970:Molecular Weight; D016788:Plasmodium chabaudi / Q000201:enzymology*; D011480:Protease Inhibitors / Q000494:pharmacology; D012697:Serine Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity
D001457:Anion Exchange Protein 1, Erythrocyte; D011480:Protease Inhibitors; D012697:Serine Endopeptidases