Open AccessPlasmodium chabaudi p68 serine protease activity required for merozoite entry into mouse erythrocytes.
Author(s) -
Catherine Braun Breton,
Thierry Blisnick,
H Jouin,
Jean-Christophe Barale,
Thierry Rabilloud,
Gordon Langsley,
L H Pereira da Silva
Publication year - 1992
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.89.20.9647
Subject(s) - plasmodium chabaudi , serine protease , plasmodium falciparum , protease , enzyme , biology , serine , in vitro , biochemistry , proteases , microbiology and biotechnology , chemistry , malaria , parasitemia , immunology
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.