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J Gen Virol 84 (2003), 925-928; DOI 10.1099/vir.0.18695-0

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© 2003 Society for General Microbiology

Short Communication

RNase L activity does not contribute to host RNA degradation induced by herpes simplex virus infection

Tracy J. Smith1, Robert H. Silverman3 and David A. Leib1,2

1 Departments of Ophthalmology and Visual Sciences, Washington University School of Medicine, Box 8096, 660 S. Euclid Avenue, St Louis, MO 63110, USA
2 Departments of Molecular Microbiology, Washington University School of Medicine, Box 8096, 660 S. Euclid Avenue, St Louis, MO 63110, USA
3 Department of Cancer Biology, Cleveland Clinic Foundation, Cleveland, OH 44195, USA

Correspondence
David Leib
Leib{at}vision.wustl.edu

In early herpes simplex virus (HSV) infection, the virion host shutoff (vhs) protein mediates the degradation of mRNA and subsequent shutoff of host protein synthesis. It is unclear whether vhs acts alone or in concert with virus-induced cellular factors for this activity. This paper examines whether RNase L, a virally induced endoribonuclease, contributes to HSV-induced mRNA decay. Results showed that RNA degradation was comparable in wild-type and RNase L-/- cells, demonstrating that HSV-mediated RNA degradation is independent of RNase L activity. Furthermore, the data show that HSV-1 does not significantly induce RNase L activity in murine embryo fibroblasts.




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