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Deubiquitination in virus infection

Holger A Lindner1

  • 1Biotechnology Research Institute, National Research Council of Canada, 6100 Avenue Royalmount, Montreal, Quebec, Canada H4P 2R2. Holger.Lindner@cnrc-nrc.gc.ca

Virology
|February 13, 2007
PubMed

Insights

Viruses manipulate protein ubiquitination and deubiquitination for their benefit. This review explores viral interactions with deubiquitination enzymes and ubiquitin-like sequences, highlighting their role in viral pathogenesis.

Area of Science:

  • Molecular Biology
  • Virology
  • Biochemistry

Background:

  • Post-translational modification by ubiquitin and ubiquitin-like proteins regulates diverse cellular processes.
  • Eukaryotic viruses extensively utilize and manipulate host protein ubiquitination pathways.
  • Deubiquitination is increasingly recognized as a critical viral target.

Purpose of the Study:

  • To review known viral interactions with protein deubiquitination.
  • To discuss viral enzymes exhibiting deubiquitinating activity.
  • To examine the roles of viral ubiquitin-like sequences in viral processes.

Main Methods:

  • Literature review of scientific publications on viral deubiquitination.
  • Analysis of viral enzymes and sequences involved in ubiquitination/deubiquitination.
  • Synthesis of current knowledge on viral manipulation of deubiquitination.

Main Results:

  • Viruses employ various strategies to interfere with host deubiquitination.
  • Several viral enzymes possess deubiquitinating activity, aiding viral replication and immune evasion.
  • Viral ubiquitin-like sequences can mimic host proteins or interfere with ubiquitination pathways.

Conclusions:

  • Viral modulation of deubiquitination is crucial for viral life cycles.
  • Understanding these interactions offers potential targets for antiviral therapies.
  • Further research into viral deubiquitinating enzymes and sequences is warranted.

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