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Toxic membrane fractions from Mycoplasma fermentans.

M G Gabridge, W H Murphy

    Infection and Immunity
    |December 1, 1971
    PubMed
    Summary

    A Mycoplasma fermentans isolate caused lethal toxicity in mice. The toxic factor, located in reaggregated cell membranes, was a heat-stable lipid-protein complex, not lipids or proteins alone.

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    Area of Science:

    • Microbiology
    • Immunology
    • Toxicology

    Background:

    • Mycoplasma fermentans is a bacterium known to cause various infections.
    • Certain strains of Mycoplasma fermentans can induce toxic effects in mammalian hosts.
    • Understanding the specific components responsible for Mycoplasma-induced toxicity is crucial for developing therapeutic strategies.

    Purpose of the Study:

    • To identify the component of Mycoplasma fermentans responsible for lethal toxicity in mice.
    • To characterize the nature of the toxic factor present in the bacterium.

    Main Methods:

    • Induction of toxicity in mice using viable and inactivated Mycoplasma fermentans cells, lysates, membranes, cytoplasm, and extracted lipids.
    • Detergent solubilization and Mg(2+)-mediated reaggregation of membrane components.
    • Fractionation of membrane components using acetone washes and ammonium sulfate precipitation.
    • Analysis of protein composition using polyacrylamide gel electrophoresis.
    • Assessment of the toxic factor's stability to heat, Pronase, trypsin, and lipase.

    Main Results:

    • A specific isolate of Mycoplasma fermentans (strain K10) induced a lethal toxicity syndrome in mice.
    • Whole cell lysates and isolated membranes were toxic, while cytoplasm was not.
    • A toxic lipid-protein complex was formed when membranes were dissolved and reaggregated.
    • Isolated lipids or protein-rich fractions were non-toxic.
    • The toxic factor was heat-stable but degraded by Pronase, trypsin, and lipase, suggesting a protein component is involved.

    Conclusions:

    • The lethal toxicity induced by this Mycoplasma fermentans isolate is mediated by a heat-stable lipid-protein complex found in the cell membranes.
    • Neither lipids nor proteins alone account for the observed toxicity.
    • The toxic factor's sensitivity to proteases and lipase indicates a crucial role for protein in its activity.

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