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Deubiquitinating function of adenovirus proteinase
Maxim Y Balakirev1, Michel Jaquinod, Arthur L Haas
1Institut de Biologie Structurale, Grenoble 38027. Département de Biologie Moléculaire et Structurale, CEA, Grenoble 38054, France. maxbala@ibs.fr
Journal of Virology
|May 22, 2002
Summary
Adenovirus infection increases host cell deubiquitinating activity. The adenovirus L3 23K proteinase (Avp) deubiquitinates cellular proteins, highlighting the role of ubiquitin pathways in viral infections.
Area of Science:
- Virology
- Molecular Biology
- Biochemistry
Background:
- Viruses often synthesize proteins that mimic cellular functions to disrupt host processes.
- Ubiquitin pathways play a critical role in regulating cellular functions.
Purpose of the Study:
- To investigate the effect of adenovirus infection on host cell deubiquitinating activity.
- To identify the viral protein responsible for this activity and characterize its function.
Main Methods:
- Affinity chromatography using ubiquitin aldehyde (Ubal) to identify deubiquitinating proteases.
- In vivo and in vitro assays to analyze the deubiquitinating activity of adenovirus L3 23K proteinase (Avp).
- Structural modeling of the Ubal-Avp interaction.
Main Results:
- Adenovirus infection leads to increased deubiquitinating activity in host cells.
- Adenovirus L3 23K proteinase (Avp) was identified as a key enzyme responsible for this activity.
- Avp was shown to deubiquitinate various cellular proteins in vivo and in vitro.
- Structural analysis revealed similarities between Avp and other ubiquitin hydrolases.
Conclusions:
- Adenovirus utilizes its L3 23K proteinase (Avp) to deubiquitinate cellular proteins, potentially as an advantageous invasion strategy.
- These findings underscore the significance of ubiquitin pathways in the context of viral infections.