 |
Stephen Rice, Ph.D.
Associate Professor
Department of Microbiology
University of Utah, 1985, Ph.D.
ricex019@umn.edu
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
|
