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Structure and function of concanavalin A.

G N Reeke, J W Becker, B A Cunningham

    Advances in Experimental Medicine and Biology
    |January 11, 1975
    PubMed
    Summary
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    Concanavalin A (Con A) structure was determined, revealing its role in lymphocyte mitogenesis. Dimeric Con A stimulates cells without altering receptor mobility, suggesting a colchicine-sensitive protein network mediates signaling.

    Area of Science:

    • Molecular Biology
    • Cell Biology
    • Biochemistry

    Background:

    • Lectins are crucial tools for analyzing fundamental cell biology processes.
    • Concanavalin A (Con A), a mitogenic lectin from jack beans, is widely used in cell surface and mitosis studies.

    Purpose of the Study:

    • To determine the amino acid sequence and three-dimensional structure of concanavalin A (Con A).
    • To interpret Con A's effects on lymphocyte mitogenesis and cell surface receptor mobility.
    • To investigate the mechanism of lectin-induced cell stimulation and receptor modulation.

    Main Methods:

    • Amino acid sequencing and X-ray crystallography to determine Con A's 3D structure.
    • Carbohydrate binding assays to examine saccharide-binding properties.
    • Preparation and testing of dimeric Con A derivatives (e.g., succinyl-Con A) for biological activity.

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  • Analysis of Con A's effects on lymphocyte cell surface receptor mobility and cap formation.

    • Main Results:

    • The 3D structure of Con A tetramers was elucidated, showing dome-like subunits with specific symmetry.
    • Differences in Con A's saccharide-binding behavior were observed between solution and crystalline states.
    • Dimeric succinyl-Con A is a potent mitogen but does not modulate cell surface receptor mobility, unlike native Con A.
    • Native Con A exhibits antagonistic effects: inducing cap formation and inhibiting receptor mobility.

    Conclusions:

    • Neither receptor immobilization nor cap formation is essential for lectin-induced cell stimulation.
    • A colchicine-sensitive protein network likely connects cell surface receptors, mediating signal transmission.
    • Changes in receptor attachment to this network may alter signal transduction, potentially influencing mitosis.