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In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
Published on: July 25, 2019
Deubiquitination in virus infection.
1Biotechnology Research Institute, National Research Council of Canada, 6100 Avenue Royalmount, Montreal, Quebec, Canada H4P 2R2. Holger.Lindner@cnrc-nrc.gc.ca
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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