Stephen Rice

Assistant Professor

Microbiology, Medical School

Email: ricex019@umn.edu
Phone: (612) 626-4183

Education

Ph.D., University of Utah, 1985

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

• Fraser, K and S.A. Rice. 2005. Herpes simplex virus type 1 infection leads to loss of serine-2 phosphorylation on the carboxyl-terminal domain of RNA polymerase II. J. Virol. 79:11323-11334. 77:9872-9884.
• Perkins, K.D., J. Gregonis, S. Borge, and S.A. Rice. 2003. Transactivation of a viral target gene by herpes simplex virus ICP27 is post-transcriptional and does not require the endogenous promoter or polyadenylation site. J. Virol. 77:9872-9884.
• Koffa, M.D., J. Kean, G. Zachos, S. Rice and J.B. Clements. 2003. CK2 protein kinase is stimulated and redistributed by herpes simplex virus ICP27 protein. J. Virol. 77:4315-4325.
• Lengyel, J., C. Guy, V. Leong, S. Borge, and S.A. Rice. 2002. Mapping of functional regions in the amino-terminal portion of the herpes simplex virus ICP27 regulatory protein: importance of the leucine-rich nuclear export signal and RGG box RNA-binding domain. J. Virol. 76:11866-79.
• Aubert, M., S.A. Rice, and J. Blaho. 2001. Accumulation of herpes simplex virus type 1 early and leaky-late proteins correlates with apoptosis prevention in infected human HEp-2 cells. J Virol. 75:1013-1030.
• Ellison, K.S, S.A. Rice, R. Verity and J.R. Smiley. 2000. Processing of alpha-globin and ICP0 mRNA in cells infected with HSV-1 ICP27 mutants. J. Virol. 74:7307-19.
• Bunnell, S.M., and S.A. Rice. 2000. The conserved carboxyl-terminal half of herpes simplex virus type 1 regulatory protein ICP27 is dispensable for viral growth in the presence of compensatory mutations. J. Virol. 74:7362-7374.
• Long, M., V. Leong, P. Schaffer, C. Spencer, and S. Rice. (1999) ICP22 and the UL13 protein kinase are both required for herpes simplex virus-induced modification of the large subunit of RNA polymerase II. J. Virol. 73:5593-5604.
• Mears, W., and S.A. Rice. (1998) The herpes simplex virus regulatory protein ICP27 shuttles between the nucleus and cytoplasm. Virology 242:128-137.