RNase L activity does not contribute to host RNA degradation induced by herpes simplex virus infection.
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.
Smith
Tracy J
TJ
Departments of Ophthalmology and Visual Sciences, Washington University School of Medicine, Box 8096, 660 S. Euclid Avenue, St Louis, MO 63110, USA.
Silverman
Robert H
RH
Department of Cancer Biology, Cleveland Clinic Foundation, Cleveland, OH 44195, USA.
Leib
David A
DA
Departments of Molecular Microbiology, Washington University School of Medicine, Box 8096, 660 S. Euclid Avenue, St Louis, MO 63110, USA.|Departments of Ophthalmology and Visual Sciences, Washington University School of Medicine, Box 8096, 660 S. Euclid Avenue, St Louis, MO 63110, USA.
D000818:Animals; D002478:Cells, Cultured; D002522:Chlorocebus aethiops; D004722:Endoribonucleases / Q000172:deficiency / Q000235:genetics / Q000502:physiology*; D005347:Fibroblasts; D006561:Herpes Simplex / Q000378:metabolism*; D051379:Mice; D012333:RNA, Messenger / Q000378:metabolism*; D018139:Simplexvirus / Q000201:enzymology*; D014709:Vero Cells
D012333:RNA, Messenger; D004722:Endoribonucleases; C031956:2-5A-dependent ribonuclease