University of Minnesota
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MICaB Faculty

Steve Rice
Stephen Rice, Ph.D.

Associate Professor

Department of Microbiology

University of Utah, 1985, Ph.D.

612-626-4183: office
612-624-9934: lab

Research Interests:

Herpes simplex virus gene expression

The infection of mammalian cells with herpes simplex virus type 1 (HSV-1) results in dramatic alterations to the host cell nucleus, so that viral genes are expressed at high levels, while cellular genes are nearly completely suppressed. This genetic subversion is accomplished by a small set of HSV-1 regulatory proteins, which are amenable to biochemical and genetic analysis. Currently, our laboratory is studying two of these proteins, ICP27 and ICP22. ICP27 is conserved in all known herpesviruses and is absolutely essential for HSV-1 late gene expression. Although its mechanism of action is unknown, a variety of evidence suggests that it is an unusual type of gene regulator which affects pre-mRNA processing and transport. Consistent with its suspected post-transcriptional role, we have shown that ICP27 is an RNA-binding protein that continuously shuttles between the nucleus and cytoplasm. We are also studying ICP22, an HSV-1 protein which is required for viral growth in some cell lines. We have found that HSV-1 infection alters the phosphorylation of the large subunit of RNA polymerase II, and that this effect requires ICP22. Our current goal is to delineate the molecular pathway by which ICP22 alters RNA polymerase II and to understand the functional significance of this change.


Selected Recent Publications:

  • Sedlackova, L., K.D. Perkins, J. Lengyel, A.K. Strain, V.L. van Santen, and S. A. Rice. 2008. Herpes simplex virus type 1 ICP27 regulates expression of a variant, secreted form of glycoprotein C by an intron retention mechanism. J. Virol. 82:7443-55.
  • Sedlackova, L. and S.A. Rice. 2008. Herpes simplex virus immediate-early protein ICP27 is required for the efficient virion incorporation of ICP0 and ICP4. J. Virol. 82:268-77.
  • Fraser, K. and S.A. Rice.2007. Herpes simplex virus immediate-early protein ICP22 triggers loss of serine 2-phosphorylated RNA polymerase II. J. Virol. 81:5091-5101.
  • Hargett, D., S.A. Rice, and S. L. Bachenheimer. 2006. Herpes simplex virus type 1 ICP27-dependent activation of NF-kappaB. J. Virol. 80:105665-78.
  • Orlando, J.S., J.W. Balliet, A.S. Kushnir, T.L. Astor, M. Kosz-Vnenchak, S.A. Rice, D.M. Knipe, and P.A. Schaffer. 2006. ICP22 is required for wild-type composition and infectivity of herpes simplex virus type 1 virions. J. Virol. 80:9381-90.
  • Lengyel, J., A. Strain, K. Perkins, and S.A. Rice. 2006. ICP27-dependent resistance of herpes simplex virus type 1 to leptomycin B is associated with enhanced nuclear localization of ICP0 and ICP4. Virology, 352:368-79.
  • Rice, S.A. and K.A. Fraser. 2006. The modification of cellular RNA polymerase II by HSV-1 infection. In Alpha Herpesviruses: Molecular and Cellular Biology. Caister Academic Press.
  • Fraser, K.A. and S.A. Rice.2005. Herpes simplex type 1 infection leads to loss of serine-2 phosphorylation on the carboxyl-terminal domain of RNA polymerase II. J. Virol., 79:11323-34.


Last update: July 21, 2008