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Endopeptidases from Plasmodium knowlesi.

E Hempelmann, R J Wilson

    Parasitology
    |April 1, 1980
    PubMed
    Summary
    This summary is machine-generated.

    Researchers identified Plasmodium knowlesi parasite endopeptidases in infected rhesus monkey erythrocytes. These enzymes show activity only under acidic conditions, aiding in understanding parasite biochemistry.

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    Area of Science:

    • Biochemistry
    • Parasitology
    • Molecular Biology

    Background:

    • Plasmodium knowlesi is a significant cause of malaria in Southeast Asia.
    • Understanding parasite-specific enzymes is crucial for developing targeted therapies.
    • Erythrocytes are the primary host cells targeted by Plasmodium parasites.

    Purpose of the Study:

    • To identify and characterize endopeptidases present in Plasmodium knowlesi-infected rhesus monkey erythrocytes.
    • To determine the optimal conditions for the activity of these parasite-derived enzymes.
    • To differentiate parasite endopeptidases from host red blood cell enzymes.

    Main Methods:

    • Fractionation of infected erythrocyte extracts using polyacrylamide gel electrophoresis (PAGE).
    • Detection of endopeptidase activity using an imprint-digest method.

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  • Enzyme activity assays performed across a range of pH values (acidic to neutral).
  • Substrate utilization assessed using hemoglobin, albumin, and erythrocyte lysate.

    • Main Results:

    • Several zones of endopeptidase activity were detected in infected erythrocyte extracts.
    • Parasite-derived endopeptidases exhibited optimal activity under acidic conditions (pH 3.2).
    • No significant activity was observed between pH 6.4 and 8.9.
    • Optimized PAGE identified highly active parasite enzymes with specific Rf values (73, 63, 53) and a host red cell endopeptidase (Rf44).
    • Minor activity bands were associated with platelets.

    Conclusions:

    • Plasmodium knowlesi possesses distinct acid-active endopeptidases within infected erythrocytes.
    • These findings provide insights into the enzymatic machinery of the parasite during infection.
    • Characterization of these enzymes could inform the development of novel anti-malarial strategies targeting parasite proteases.