Edward M. Campbell, Ph.D.
Assistant
Professor
Department
of Cell Biology,
Neurobiology
and Anatomy
1998
University of Illinois,
Champaign-Urbana
B.S. -Life Sciences/Bioengineering
2004
University of Illinois
at Chicago
Ph.D. -Microbiology and Immunology
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| My lab is focused on understanding the interactions
occurring between retroviruses, such as Human Immunodeficiency Virus type-1 (HIV-1) and
cellular restriction factors such as TRIM5a. TRIM5a has been shown to mediate a species specific block to infection,
such that the TRIM5a protein from rhesus macaques potently
inhibits HIV-1 infection, while HIV-1 is able to avoid restriction by TRIM5a protein present in the human population. My work seeks to better
understand the molecular mechanism of restriction mediated by TRIM5a
and other TRIM family proteins. Much of the work in lab features the use of
deconvolution microscopy to directly observe fluorescently labeled
virions infecting target cells. We therefore hope to generate a better understanding of
the biology of restriction by directly observing the interactions occurring between
virions and restriction factors.
There are currently 3 projects in the lab. First, we have identified a region ofa that appears
to mediate the multimerization of TRIM5a into discreet structures termed
cytoplasmic bodies. We seek to understand the
role this multimerization plays in restriction by examining TRIM5 mutants that have lost
the ability to form these structures.. Second, we also are examining the regions of TRIM5
that mediate the binding and clearance of viral complexes during restriction by examining
the kinetics of these events in the context of TRIM5a mutants with specific mutations in
domains thought to be responsible for these activities. Third, we want to develop methods
to fluorescently label other viruses during infection to observe the restriction of those
viruses by TRIM5a
proteins from other species, as well as recently reported antiviral activities possessed
by other TRIM family members. Specifically, we want to develop the ability to
fluorescently label murine leukemia virus particles, to observe the restriction of this
virus by the human version of TRIM5a to better understand and differences in
the restriction mediated by TRIM5a from human forms of the protein. |
Campbell EM, Perez O, Anderson JL, Hope TJ. Visualization
of a proteasome independent intermediate during restriction of HIV-1 by rhesus TRIM5a, J Cell Bio, 2008 Feb
11;180(3):549-61
Campbell EM, Perez O, Melar M, Hope TJ. Labeling HIV-1
virions with two fluorescent proteins allows identification of virions that have
productively entered the target cell. Virology. 2007 April 10;360:286-293 Nov 21
Campbell
EM, Dodding MP, Yap MW, Wu X,
Gallois-Montbrun S, Malim MH, Stoye JP, Hope TJ. Trim5a cytoplasmic bodies are highly dynamic
structures. Mol Biol Cell. 2007, 18(6), 2102-2111
Wu X, Anderson JL, Campbell EM,
Joseph AM, Hope TJ. Proteosome inhibitors uncouple rhesus TRIM5alpha restriction of HIV-1
reverse transcription and infection. PNAS. 2006 May9;103(19):7465-70 |
