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New EMBO members' review: viral and bacterial proteins regulating apoptosis at the mitochondrial level

P Boya1, B Roques, G Kroemer

  • 1Centre National de la Recherche Scientifique, UMR 1599, Institut Gustave Roussy, Pavillon de Recherche 1, 39 rue Camille-Desmoulins F-94805 Villejuif, France.

The EMBO Journal
|August 14, 2001
PubMed

Insights

Pathogens can manipulate host cell death (apoptosis) by targeting mitochondrial membrane permeabilization (MMP). Some pathogen proteins interact with VDAC or ANT, potentially using host mechanisms to control MMP.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Immunology

Background:

  • Mitochondrial membrane permeabilization (MMP) is a key event in apoptosis.
  • Intracellular pathogens can modulate host cell apoptosis at the mitochondrial level.
  • Pathogen-encoded proteins target mitochondrial membranes to induce or inhibit MMP.

Purpose of the Study:

  • To investigate how pathogen-encoded proteins regulate host mitochondrial apoptosis.
  • To explore the mechanisms by which pathogen proteins interact with mitochondrial components.
  • To understand the role of Bcl-2 homology and VDAC/ANT interactions in pathogen-mediated MMP.

Main Methods:

  • Analysis of pathogen-encoded mitochondrion-targeted proteins.
  • Investigation of interactions with voltage-dependent anion channel (VDAC) and adenine nucleotide translocator (ANT).
  • Examination of amino acid sequence homology to Bcl-2-like proteins and VDAC/porin.

Main Results:

  • Pathogen proteins targeting mitochondria can induce or inhibit MMP.
  • Some pathogen proteins lack Bcl-2 homology but interact with VDAC or ANT.
  • ANT-targeted proteins may utilize short cationic binding domains for membrane insertion.

Conclusions:

  • Pathogen-mediated MMP regulation involves targeting mitochondrial proteins.
  • Interactions with VDAC and ANT are key mechanisms for pathogen control of apoptosis.
  • ANT-targeted proteins might exploit host intrinsic MMP control pathways.

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