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© Research
Publication : Proceedings of the National Academy of Sciences of the United States of America

Plasmodium chabaudi p68 serine protease activity required for merozoite entry into mouse erythrocytes

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Proceedings of the National Academy of Sciences of the United States of America - 15 Oct 1992

Breton CB, Blisnick T, Jouin H, Barale JC, Rabilloud T, Langsley G, Pereira da Silva LH

Link to Pubmed [PMID] – 1409678

Proc. Natl. Acad. Sci. U.S.A. 1992 Oct;89(20):9647-51

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.

http://www.ncbi.nlm.nih.gov/pubmed/1409678