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 Previous Article

Journal of Virology, September 2006, p. 9341-9345, Vol. 80, No. 18
0022-538X/06/$08.00+0     doi:10.1128/JVI.01008-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

The Virion Host Shutoff Protein (UL41) of Herpes Simplex Virus 1 Is an Endoribonuclease with a Substrate Specificity Similar to That of RNase A

Brunella Taddeo and Bernard Roizman*

The Marjorie B. Kovler Viral Oncology Laboratories, The University of Chicago, Chicago, Illinois 60637

Received 16 May 2006/ Accepted 30 June 2006

Earlier, our laboratory reported that purified glutathione S-transferase-virion host shutoff (GST-vhs) protein exhibited endoribonucleolytic activity in in vitro assays using as substrates in vitro-transcribed regions of IEX-1 mRNA. Here, we report that studies of the cleavage patterns of synthetic RNA oligonucleotides defined the activity of GST-vhs as being similar to that of RNase A. Thus, GST-vhs cleaved the RNA at the 3' end of single-stranded cytidine and uridine residues. Since the GST-mvhs nuclease-defective mutant protein failed to cleave the synthetic RNAs, the results unambiguously attribute the activity to vhs.

* Corresponding author. Mailing address: The Marjorie Kovler Viral Oncology Laboratories, The University of Chicago, 910 East 58th Street, Chicago, IL 60637. Phone: (773) 702-1898. Fax: (773) 702-1631. E-mail: Bernard.Roizman{at}bsd.uchicago.edu.

Journal of Virology, September 2006, p. 9341-9345, Vol. 80, No. 18
0022-538X/06/$08.00+0     doi:10.1128/JVI.01008-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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