This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Boutell, C.
Right arrow Articles by Everett, R. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Boutell, C.
Right arrow Articles by Everett, R. D.

 Previous Article  |  Next Article 

Journal of Virology, October 2005, p. 12342-12354, Vol. 79, No. 19
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.19.12342-12354.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Reciprocal Activities between Herpes Simplex Virus Type 1 Regulatory Protein ICP0, a Ubiquitin E3 Ligase, and Ubiquitin-Specific Protease USP7

Chris Boutell, Mary Canning, Anne Orr, and Roger D. Everett*

MRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, Scotland, United Kingdom

Received 21 April 2005/ Accepted 8 July 2005

Herpes simplex virus type 1 (HSV-1) regulatory protein ICP0 stimulates lytic infection and the reactivation of quiescent viral genomes. These roles of ICP0 require its RING finger E3 ubiquitin ligase domain, which induces the degradation of several cellular proteins, including components of promyelocytic leukemia nuclear bodies and centromeres. ICP0 also interacts very strongly with the cellular ubiquitin-specific protease USP7 (also known as HAUSP). We have shown previously that ICP0 induces its own ubiquitination and degradation in a RING finger-dependent manner, and that its interaction with USP7 regulates this process. In the course of these studies we found and report here that ICP0 also targets USP7 for ubiquitination and proteasome-dependent degradation. The reciprocal activities of the two proteins reveal an intriguing situation that poses the question of the balance of the two processes during productive HSV-1 infection. Based on a thorough analysis of the properties of an HSV-1 mutant virus that expresses forms of ICP0 that are unable to bind to USP7, we conclude that USP7-mediated stabilization of ICP0 is dominant over ICP0-induced degradation of USP7 during productive HSV-1 infection. We propose that the biological significance of the ICP0-USP7 interaction may be most pronounced in natural infection situations, in which limited amounts of ICP0 are expressed.

* Corresponding author. Mailing address: MRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, Scotland, United Kingdom. Phone: 44 141 330 3923. Fax: 44 141 337 2236. E-mail: r.everett{at}vir.gla.ac.uk.

Journal of Virology, October 2005, p. 12342-12354, Vol. 79, No. 19
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.19.12342-12354.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Gu, H., Poon, A. P., Roizman, B. (2009). During its nuclear phase the multifunctional regulatory protein ICP0 undergoes proteolytic cleavage characteristic of polyproteins. Proc. Natl. Acad. Sci. USA 106: 19132-19137 [Abstract] [Full Text]  
  • Everett, R. D., Parsy, M.-L., Orr, A. (2009). Analysis of the Functions of Herpes Simplex Virus Type 1 Regulatory Protein ICP0 That Are Critical for Lytic Infection and Derepression of Quiescent Viral Genomes. J. Virol. 83: 4963-4977 [Abstract] [Full Text]  
  • Daubeuf, S., Singh, D., Tan, Y., Liu, H., Federoff, H. J., Bowers, W. J., Tolba, K. (2009). HSV ICP0 recruits USP7 to modulate TLR-mediated innate response. Blood 113: 3264-3275 [Abstract] [Full Text]  
  • Saira, K., Chowdhury, S., Gaudreault, N., da Silva, L., Henderson, G., Doster, A., Jones, C. (2008). The Zinc RING Finger of Bovine Herpesvirus 1-Encoded bICP0 Protein Is Crucial for Viral Replication and Virulence. J. Virol. 82: 12060-12068 [Abstract] [Full Text]  
  • Boutell, C., Everett, R., Hilliard, J., Schaffer, P., Orr, A., Davido, D. (2008). Herpes Simplex Virus Type 1 ICP0 Phosphorylation Mutants Impair the E3 Ubiquitin Ligase Activity of ICP0 in a Cell Type-Dependent Manner. J. Virol. 82: 10647-10656 [Abstract] [Full Text]  
  • Fakioglu, E., Wilson, S. S., Mesquita, P. M. M., Hazrati, E., Cheshenko, N., Blaho, J. A., Herold, B. C. (2008). Herpes Simplex Virus Downregulates Secretory Leukocyte Protease Inhibitor: a Novel Immune Evasion Mechanism. J. Virol. 82: 9337-9344 [Abstract] [Full Text]  
  • Kunec, D., Hanson, L. A., van Haren, S., Nieuwenhuizen, I. F., Burgess, S. C. (2008). An Overlapping Bacterial Artificial Chromosome System That Generates Vectorless Progeny for Channel Catfish Herpesvirus. J. Virol. 82: 3872-3881 [Abstract] [Full Text]  
  • Mouchantaf, R., Azakir, B. A., McPherson, P. S., Millard, S. M., Wood, S. A., Angers, A. (2006). The Ubiquitin Ligase Itch Is Auto-ubiquitylated in Vivo and in Vitro but Is Protected from Degradation by Interacting with the Deubiquitylating Enzyme FAM/USP9X. J. Biol. Chem. 281: 38738-38747 [Abstract] [Full Text]  
  • Geoffroy, M.-C., Chadeuf, G., Orr, A., Salvetti, A., Everett, R. D. (2006). Impact of the Interaction between Herpes Simplex Virus Type 1 Regulatory Protein ICP0 and Ubiquitin-Specific Protease USP7 on Activation of Adeno-Associated Virus Type 2 rep Gene Expression.. J. Virol. 80: 3650-3654 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»