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Related Experiment Videos

Unfolding affects insect cell permeabilization by Bacillus thuringiensis Cry1C toxin.

G Guihard1, R Laprade, J L Schwartz

  • 1INSERM U533, Hôtel-Dieu, Faculté de Médecine, Nantes, France.

Biochimica Et Biophysica Acta
|November 24, 2001
PubMed
Summary

Bacillus thuringiensis Cry1C toxin permeabilizes insect cells by affecting potassium ion movement. Toxin unfolding reveals its C-terminal half is crucial for this biological insecticide activity.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Insect Toxicology

Background:

  • Bacillus thuringiensis Cry toxins are effective biological insecticides.
  • The precise molecular mechanism of Cry toxin action on insect cells is not fully understood.
  • Understanding Cry toxin interactions is key to developing sustainable pest control strategies.

Purpose of the Study:

  • To investigate the relationship between the conformational state of Cry1C toxin and its ion-channel forming activity.
  • To determine how Cry1C toxin induces potassium ion leakage in Spodoptera frugiperda (Sf9) cells.
  • To elucidate the role of toxin conformation in its biological insecticidal function.

Main Methods:

  • Utilized a fluorescent assay to measure potassium ion movement across Sf9 cell membranes induced by Cry1C toxin.

Related Experiment Videos

  • Employed tryptophan spectroscopy to analyze conformational changes in the Cry1C toxin.
  • Applied guanidinium hydrochloride to induce controlled unfolding of the Cry1C toxin.

    • Main Results:

    • Cry1C toxin, even when its N-terminal half was unfolded by guanidinium hydrochloride, retained its ability to permeabilize Sf9 cells.
    • Complete unfolding of the Cry1C toxin resulted in a loss of its capacity to induce potassium ion leakage.
    • These findings suggest the C-terminal half of the Cry1C toxin is essential for cell permeabilization.

    Conclusions:

    • The permeabilization of Sf9 cells by Cry1C toxin depends on the integrity of its C-terminal half.
    • An initial unfolding step, potentially triggered by the acidic environment of the insect cell, may be necessary for Cry1C toxin activity.
    • This study provides insights into the molecular mechanism of Cry toxin action, crucial for biological insecticide development.