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USP7 manipulation by viral proteins

Anna Bojagora1, Vivian Saridakis1

  • 1Department of Biology, York University, Toronto, Canada.

Virus Research
|July 1, 2020
PubMed

Insights

Viruses manipulate Ubiquitin Specific Protease 7 (USP7), a key enzyme regulating cellular processes. This review details how viral proteins hijack USP7 for their own survival and replication.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Virology

Background:

  • Ubiquitin Specific Protease 7 (USP7) is a crucial deubiquitinating enzyme (DUB) involved in diverse cellular functions.
  • USP7 is the primary DUB implicated in viral infections, interacting with numerous viral proteins.
  • Viruses have evolved strategies to exploit host cellular machinery, including USP7, for their benefit.

Purpose of the Study:

  • To review the latest research on viral manipulation of USP7.
  • To elucidate the mechanisms by which viruses usurp USP7 function.
  • To highlight the significance of USP7 in host-pathogen interactions.

Main Methods:

  • Literature review of recent studies on USP7 and viral interactions.
  • Analysis of identified viral proteins that target USP7.
  • Examination of the functional consequences of USP7 manipulation by viruses.

Main Results:

  • Multiple viral proteins have been identified that specifically target and interact with USP7.
  • Viruses utilize USP7 to promote their replication and survival within the host.
  • Understanding these interactions provides insights into viral pathogenesis.

Conclusions:

  • USP7 is a critical node for viral exploitation of host cell processes.
  • Targeting USP7-viral protein interactions presents potential therapeutic avenues.
  • Further research is needed to fully understand the complex interplay between viruses and USP7.
Keywords:
EBNA1ICP0USP7Ubiquitinp53vIRF1

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