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Cholera toxin interactions with lipid bilayers.

M T Tosteson, D C Tosteson, J Rubnitz

    Acta Physiologica Scandinavica. Supplementum
    |January 1, 1980
    PubMed
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    Cholera toxin binds to its receptor, monosialoganglioside GM1, in artificial cell membranes. This binding affinity is comparable to that observed in living cells, providing insights into toxin-receptor interactions.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Membrane Biophysics

    Background:

    • Cholera toxin is a bacterial toxin that affects cell membranes.
    • Monosialoganglioside GM1 is a known receptor for cholera toxin.
    • Understanding toxin-receptor interactions is crucial for cell biology.

    Purpose of the Study:

    • To quantify the binding affinity of cholera toxin to GM1-containing lipid bilayers.
    • To investigate the role of GM1's negative surface charge in cholera toxin binding.
    • To compare binding constants in artificial bilayers with those in intact cells.

    Main Methods:

    • Lipid bilayer formation using mixtures of GM1 and glycerolmonooleate (GMO).
    • Measurement of bilayer electrical conductance (G) to estimate surface charge.

    Related Experiment Videos

  • Assay of cholera toxin and choleragenoid binding to GM1-modified bilayers.

    • Main Results:

    • The molar ratio of GM1 in bilayers reflected the composition of the membrane-forming solution.
    • Cholera toxin and choleragenoid specifically bound to GM1-containing bilayers, not to those with phosphatidyl serine or GD1a.
    • The apparent dissociation constant (Kd) for choleragen binding to GM1 was determined to be 10(-11) M.

    Conclusions:

    • GM1-containing lipid bilayers serve as a valid model for studying cholera toxin binding.
    • The high affinity of cholera toxin for GM1 in bilayers is consistent with findings in intact cells.
    • This study provides quantitative data on cholera toxin-GM1 interactions at the molecular level.