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Related Experiment Videos

Virus-induced permeability transition in mitochondria.

L D Zorova1, B F Krasnikov, A E Kuzminova

  • 1A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia.

FEBS Letters
|February 22, 2000
PubMed
Summary

Tobacco mosaic virus triggers mitochondrial permeability transition in isolated rat liver mitochondria. This virus-induced effect, involving pore opening, was blocked by cyclosporin A, suggesting a role in apoptosis.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Virology

Background:

  • Mitochondria play a crucial role in cellular energy production and apoptosis.
  • The mitochondrial permeability transition pore (MPTP) is a key regulator of mitochondrial function and cell death.
  • Viruses can interact with host cell components, potentially influencing mitochondrial integrity.

Purpose of the Study:

  • To investigate the effect of tobacco mosaic virus (TMV) on isolated rat liver mitochondria.
  • To determine if TMV can induce mitochondrial permeability transition.
  • To explore the potential role of MPTP in virus-induced mitochondrial dysfunction.

Main Methods:

  • Isolated rat liver mitochondria were incubated with TMV suspension.
  • Mitochondrial parameters including oxygen consumption, membrane potential, calcium ion release, and swelling were measured.

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  • Electron microscopy was used to visualize virus-mitochondria interactions.
  • Cyclosporin A was used to assess the involvement of MPTP.

    • Main Results:

    • TMV supplementation induced mitochondrial permeability transition, evidenced by increased oxygen consumption, membrane potential collapse, calcium release, and swelling.
    • Cyclosporin A effectively prevented all TMV-induced mitochondrial changes.
    • EGTA treatment or heat disruption of TMV abolished its effects on mitochondria.
    • Specific viral protein components or disrupted virus supernatant did not affect mitochondrial function.

    Conclusions:

    • Tobacco mosaic virus directly interacts with and disrupts mitochondrial function by opening the MPTP.
    • The observed mitochondrial dysfunction is dependent on the structural integrity of the virus.
    • These findings suggest a potential mechanism for virus-induced apoptosis mediated by MPTP opening.