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Related Experiment Videos

Lectin binding by trypanosoma equiperdum

P R Jackson

    The Journal of Parasitology
    |February 1, 1977
    PubMed
    Summary
    This summary is machine-generated.

    Surface coat of Trypanosoma equiperdum lacks accessible carbohydrate binding sites for most plant lectins. Proteolytic enzyme treatment exposes these sites, revealing potential D-mannose or N-acetyl-D-galactosamine residues.

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    Area of Science:

    • Parasitology
    • Biochemistry
    • Cell Biology

    Background:

    • The surface coat of Trypanosoma equiperdum plays a crucial role in parasite-host interactions.
    • Understanding the carbohydrate composition of the parasite surface is vital for developing targeted therapies.

    Purpose of the Study:

    • To investigate the carbohydrate-binding specificities of plant lectins on the surface of Trypanosoma equiperdum.
    • To determine if enzymatic treatments can expose lectin-binding sites on the parasite surface.

    Main Methods:

    • Agglutination assays using six different plant lectins (Concanavalin A, phytohemagglutinins M and P, wheat germ, Anti A, Anti H).
    • Treatment of Trypanosoma equiperdum with various enzymes including proteases (trypsin, pronase, chymopapain, papain), lipases, and amylases.

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  • Affinity chromatography using Concanavalin A immobilized on agarose beads.

    • Main Results:

    • Unmodified Trypanosoma equiperdum surface coat did not agglutinate with most tested lectins.
    • Treatment with specific proteases (trypsin, pronase, chymopapain, papain) exposed binding sites for Concanavalin A and phytohemagglutinins M and P.
    • Trypsinized parasites bound to Concanavalin A immobilized on agarose beads.
    • Other enzymes and lectins (wheat germ, Anti A, Anti H) did not induce agglutination.

    Conclusions:

    • The surface coat of Trypanosoma equiperdum contains or underlies carbohydrate residues, likely D-mannose or N-acetyl-D-galactosamine, masked from direct lectin binding.
    • Proteolytic digestion is effective in revealing these hidden carbohydrate structures, suggesting their presence within or beneath the surface coat proteins.