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Journal of Virology, January 2006, p. 218-225, Vol. 80, No. 1
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.1.218-225.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

ICP0 Prevents RNase L-Independent rRNA Cleavage in Herpes Simplex Virus Type 1-Infected Cells

Paul T. Sobol1 and Karen L. Mossman1,2*

Departments of Biochemistry and Biomedical Sciences,1 Pathology and Molecular Medicine, Centre for Gene Therapeutics, McMaster University, Hamilton L8N 3Z5, Canada2

Received 14 July 2005/ Accepted 13 October 2005

The classical interferon (IFN)-dependent antiviral response to viral infection involves the regulation of IFN-stimulated genes (ISGs), one being the gene encoding cellular endoribonuclease RNase L, which arrests protein synthesis and induces apoptosis by nonspecifically cleaving rRNA. Recently, the herpes simplex virus type 1 (HSV-1) protein ICP0 has been shown to block the induction of ISGs by subverting the IFN pathway upstream of the 2'-5'-oligoadenylate synthetase (OAS)/RNase L pathway. We report that ICP0 also prevents rRNA degradation at late stages of HSV-1 infection, independent of its E3 ubiquitin ligase activity, and that the resultant rRNA degradation is independent of the classical RNase L antiviral pathway. Moreover, the degradation is independent of the viral RNase vhs and is independent of IFN response factor 3. These studies indicate the existence of another, previously unidentified, RNase that is part of the host antiviral response to viral infection.

* Corresponding author. Mailing address: Department of Pathology & Molecular Medicine, MDCL 5026, 1200 Main Street West, Hamilton, Ontario, Canada L8N 3Z5. Phone: (905) 525-9140. Fax: (905) 522-6750. E-mail: mossk{at}mcmaster.ca.

Journal of Virology, January 2006, p. 218-225, Vol. 80, No. 1
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.1.218-225.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Gu, H., Roizman, B. (2007). Herpes simplex virus-infected cell protein 0 blocks the silencing of viral DNA by dissociating histone deacetylases from the CoREST REST complex. Proc. Natl. Acad. Sci. USA 104: 17134-17139 [Abstract] [Full Text]  


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