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Ub surprised: viral ovarian tumor domain proteases remove ubiquitin and ISG15 conjugates

Meztli D Arguello1, John Hiscott

  • 1Lady Davis Institute for Medical Research, Jewish General Hospital, Montreal H3T 1E2, Canada.

Cell Host & Microbe
|December 15, 2007
PubMed

Insights

Viral proteases of nairoviruses and arteriviruses possess ovarian tumor domains that remove ubiquitin and ISG15. This action inhibits antiviral immunity, boosting viral replication and offering new therapeutic targets.

Area of Science:

  • Molecular biology
  • Virology
  • Immunology

Background:

  • Ubiquitin conjugation regulates critical cellular pathways, including antiviral immunity signaling.
  • The ubiquitin-like protein ISG15 is essential for antiviral responses against specific viruses.

Discussion:

  • Frias-Staheli and colleagues identified ovarian tumor domain-containing sequences within viral proteases of nairoviruses and arteriviruses.
  • These domains function as deubiquitinases and deISGylases, removing ubiquitin and ISG15 modifications from host proteins.

Key Insights:

  • The viral deubiquitinase/deISGylase activity inhibits the host's antiviral response mediated by ISG15.
  • This inhibition enhances viral replication by subverting a key component of innate immunity.

Outlook:

  • Understanding these viral evasion mechanisms can inform the development of novel antiviral strategies.
  • Targeting these viral protease domains may represent a promising therapeutic approach against nairoviruses and arteriviruses.

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