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Related Experiment Videos

Interaction between tetanolysin and Mycoplasma cell membrane

S Rottem, M C Hardegree, M W Grabowski

    Biochimica Et Biophysica Acta
    |December 14, 1976
    PubMed
    Summary
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    Tetanolysin lyses sterol-requiring Mycoplasma capricolum cells by binding to membrane cholesterol. This interaction is inhibited by cholesterol and Mg2+, and affects membrane fluidity.

    Area of Science:

    • Microbiology
    • Biochemistry
    • Molecular Biology

    Background:

    • Mycoplasma species, such as Mycoplasma capricolum, require sterols for their cell membranes.
    • Tetanolysin is a toxin produced by Clostridium tetani.
    • Understanding the interaction between toxins and cell membranes is crucial for developing therapeutic strategies.

    Purpose of the Study:

    • To investigate the mechanism by which tetanolysin interacts with and lyses Mycoplasma capricolum cells.
    • To identify the specific components of the mycoplasma membrane responsible for tetanolysin binding.
    • To elucidate the effects of tetanolysin binding on membrane properties.

    Main Methods:

    • Cell lysis assays using Mycoplasma capricolum and Acholeplasma laidlawii.
    • Hemolytic assays to quantify tetanolysin activity.

    Related Experiment Videos

  • Membrane isolation and binding studies.
  • Pronase digestion of membrane proteins.
  • Electron paramagnetic resonance (EPR) spectrometry.

    • Main Results:

    • Tetanolysin specifically lysed sterol-requiring Mycoplasma capricolum but not sterol-non-requiring Acholeplasma laidlawii.
    • Lysis was temperature-dependent and inhibited by cholesterol, Mg2+, and lucensomycin.
    • Mycoplasma capricolum membranes bound significantly more tetanolysin than adapted strains, with binding dependent on membrane lipids, not proteins.
    • Two tetanolysin polypeptides (44,000 and 42,000 Da) bound to mycoplasma membranes.
    • Tetanolysin treatment increased membrane fluidity.

    Conclusions:

    • Tetanolysin specifically targets and binds to cholesterol in the Mycoplasma capricolum cell membrane.
    • This interaction leads to cell lysis and alters membrane physical properties.
    • The findings suggest a model where tetanolysin shields membrane cholesterol from phospholipids.