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Alireza Gholami1, Raïd Kassis, Eléonore Real

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The matrix protein of Mokola virus (MOK) targets mitochondria, disrupting function and causing neuronal apoptosis. This interaction with cytochrome c oxidase subunit I offers a novel mechanism for energy depletion in virus-induced cell death.

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Area of Science:

  • Virology
  • Cell Biology
  • Neuroscience

Background:

  • Lyssaviruses are neurotropic viruses known to cause neuronal apoptosis.
  • The precise molecular mechanisms by which lyssavirus matrix proteins induce apoptosis remain largely unknown.
  • Previous studies suggest matrix proteins of certain lyssaviruses contribute to neuronal cell death.

Purpose of the Study:

  • To elucidate the molecular mechanism by which the Mokola virus (MOK) matrix protein (M-MOK) induces neuronal apoptosis.
  • To identify the specific viral protein regions and cellular targets involved in M-MOK-mediated apoptosis.
  • To compare the apoptotic mechanisms of low-pathogenicity M-MOK with high-pathogenicity lyssavirus matrix proteins.

Main Methods:

  • Analysis of truncated M-MOK mutants to map functional domains.
  • Yeast two-hybrid assays and coimmunoprecipitation to identify protein interactions.
  • Confocal microscopy to assess mitochondrial morphology and protein localization.
  • Measurement of cytochrome c oxidase (CcO) activity and assessment of cytochrome c release.

Main Results:

  • M-MOK targets mitochondria, disrupts morphology, and induces apoptosis via caspase-9 activation.
  • The region between residues 46 and 110 of M-MOK is crucial for mitochondrial targeting and apoptosis induction.
  • M-MOK physically associates with cytochrome c oxidase (CcO) subunit I, reducing CcO activity.
  • Specific mutations in M-MOK (K77R, N81E) mimicking M-THA reduce apoptosis and restore CcO activity, while reverse mutations in M-THA induce M-MOK-like effects.

Conclusions:

  • Mokola virus matrix protein induces apoptosis through mitochondrial targeting and disruption of the respiratory chain.
  • Interaction with CcO subunit I and subsequent energy depletion is a novel mechanism for lyssavirus-induced apoptosis.
  • Specific amino acid residues (77 and 81) dictate the pathogenic potential and apoptotic mechanism of lyssavirus matrix proteins.