| Name: |
| Kurt Gustin |
| Title: |
| Assistant Professor |
| Degree: |
| Ph.D., 1998, University of Michigan, Ann Arbor |
| Phone: |
| (208) 885-7525 |
| Fax: |
| (208) 885-7036 |
| Email: |
| kgustin@uidaho.edu |
| Lab/Office Location: |
| Ag Biotech, Room 305 |
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| Research Interests: |
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Picornaviruses are prevalent human pathogens and cause diseases ranging from the common cold, to jaundice, myocarditis and
paralysis. Included in this family are poliovirus, rhinovirus, hepatitis A virus, coxsackievirus, echovirus and others. My goals are
to understand, at a molecular level, the host-pathogen interactions that occur during picornavirus infection. In addition to
enhancing our understanding of picornavirus molecular biology and pathogenesis, my research plan is designed to provide insights
into the mechanisms underlying such basic cellular processes as signal transduction, regulation of gene expression and
nucleo-cytoplasmic trafficking. To achieve these goals I utilize a multidisciplinary approach that incorporates cell biology,
molecular biology, genetics, biochemistry and functional genomics.
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| Poliovirus Type 1 |
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During poliovirus and rhinovirus infection a number of host nuclear proteins relocalize from the nucleus to the cytoplasm. Recently,
we demonstrated that both poliovirus and rhinovirus infection cause a dramatic inhibition of nuclear import coincident with the
cytoplasmic accumulation of host nuclear proteins. We have also shown that two components of the nuclear pore complex (NPC), Nup153
and p62, are degraded during infection, thus providing a potential mechanism to account for the observed inhibition of nuclear
import. Inhibition of nuclear import is predicted to result in the cytoplasmic accumulation of a number of nuclear proteins that
normally function in RNA biogenesis and transport, activities that an RNA virus replicating in the cytoplasm might find
advantageous. Additionally, many anti-viral responses involve the transport of cytoplasmic signaling molecules, such as NFkB and
STATs into the nucleus. Inhibition of nuclear import may thus provide an attenuated anti-viral response and lead to a more
productive replicative cycle in vivo.
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Changes to the NPC and transport pathways caused by poliovirus infection. X indicates transport pathway disrupted or Nup
degraded. Question marks indicate that the status of these Nups in the NPC has not been determined. NE: nuclear
envelope.
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Currently, the major focus of the lab is to determine the role that inhibition of nucleo-cytoplasmic trafficking plays in viral
replication and pathogenesis and the impact of this inhibition on the host cell. A major effort is underway to identify the viral
factors responsible for the inhibition of nuclear import and degradation of NPC components that occurs during poliovirus and
rhinovirus infection. To better understand the consequences of viral infection on nucleo-cytoplasmic trafficking and NPC
composition, a second project focuses on characterizing the status of specific trafficking pathways and NPC components in infected
cells. Yet another project is aimed at determining if picornaviruses attenuate the host anti-viral response by examining the ability
of infected cells to mediate signal transduction from the cytoplasm to the nucleus. If you think you would be interested in working
in the lab on one of these diverse projects please feel free to drop by my office or contact me by phone or email.
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Intracellular localization ofEGFP-NLS molecules in uninfected and poliovirus-infected cells. HeLa cells stably
expressing EGFP-NLS fusion proteins were mock-infected or infected with poliovirus as indicated. Cells were processed
and examined by fluorescent microscopy at 4.5 hours after infection. EGFP fluorescence was visualized using a FITC
filter. DNA: Hoechst-stained nuclei were examined with a UV filter. Merged: shows the FITC and Hoechst images merged.
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| Selected Publications: |
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Gustin, K. E. and Peter Sarnow. 2002 Inhibition of Nuclear Import and Alteration of Nuclear Pore Complex Composition by Rhinovirus. J. Virology 72:8787-8796.
Gustin, K. E. and Peter Sarnow. 2001. Effects of Poliovirus Infection on Nucleo-cytoplasmic Trafficking and Nuclear Pore Complex Composition. EMBO J 20:240-249.
Gustin, K. E. and Robert D. Burk. 2000. PCR-Directed Linker Scanning Mutagenesis. Methods in Molecular Biology 130:85-90.
Gustin, K. E. and Michael J. Imperiale. 1998. Encapsidation of Viral DNA Requires the Adenovirus L1 52/55 kDa Protein. J. Virology 72:7860-7870.
Gustin, K. E., Lutz, P., and Michael J. Imperiale. 1996. Interaction of the Adenovirus L1 52/55 kDa Protein with the IVa2 Gene Product During Infection. J. Virology 70:6463-6467.
Gustin, K. E. and Robert D. Burk. 1993. A Rapid Method for Generating Linker Scanning Mutants Utilizing PCR. Biotechniques 14:22-23.
Gustin, K., Shapiro, M., Lee, W., and Robert D. Burk. 1993. Characterization of the Role of Individual Protein Binding Motifs within the Hepatitis B Virus Enhancer I on X Promoter Activity Using Linker Scanning Mutagenesis. Virology 193:653-660.
Gupta, S., Chowdhury, N. R., Jagtiani, R., Gustin, K., Aragona, E., Shafritz, D. A., Chowdhury, J. R., and Robert D. Burk. 1990. A Novel System for Transplantation of Isolated Hepatocytes Utilizing HBsAg-Producing Transgenic Donor Cells. Transplantation 50:472-475.
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