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Dr. Baines is a Professor in the Department of Microbiology and Immunology and has been associated with the department since 1993. He received a bachelor's degree in Microbiology From Kansas State University in 1979 and received the VMD degree from the University of Pennsylvania in 1983. He then received his PhD from Cornell University in 1988 studying the molecular virology of feline coronaviruses. He obtained postdoctoral training at the University of Chicago in the laboratory of Dr. Bernard Roizman studying the molecular virology of herpes simplex virus replication. He has been funded by the NIH since January 1, 1995 to study herpes simplex virus assembly. Research Interests | Graduate Fields | Lab Members | Related Links | Selected References
The major focus of the laboratory is to understand how herpes simplex virus utilizes cellular machinery to optimize its own assembly. The work is divided into two areas. The first area of interest focuses on the process of DNA cleavage and packaging within infected cell nuclei; the process is the target of a novel class of antiviral drugs currently under development. We have discovered that herpesvirus capsids utilize actin to allow capsids to move in a directed fashion in infected cell nuclei. This is done by tracking capsids tagged with green fluorescent protein in living cells by time lapse cofocal microscoopy. These studies should shed light on the roles of actin-dependent motors in the nucleus; such motors have been implicated in intranuclear movement of chromosome remodeling complexes and telomeres, among other structures. A second area concerns envelopment of nucleocapsids at the inner nuclear membrane. We have identified proteins, essential to envelopment of nucleocapsids, that alter the structure of the nucleus, presumably to allow efficient production of virions by facilitating budding at the inner nuclear membrane. The goal of this research is to determine how the HSV proteins alter the nuclear cytoskeleton and mediate nucleocapsid trafficking through the nuclear lamina which forms a fibrous barrier and acts to fortify the structure of the nucleus. This should shed light not only on envelopment of nucleocapsids, but also the functions of the nuclear lamins.
Dr. Baines is a member of the following Graduate Fields:
Elizabeth Wills, a research technical expert in electron microscopy and monoclonal antibody production.
Selected References Yang, K. and J.D. Baines. (2009). Tryptophan residues in the portal protein of herpes simplex virus 1 critical to the interaction with scaffold proteins and incorporation into capsids. J. Virol. 83:11726–11733. Scholtes, L and J.D. Baines. (2009). Effects of major capsid proteins, capsid assembly, and DNA cleavage/packaging on the pUL17/pUL25 complex of herpes simplex virus 1. Journal of Virology. [Editor-Featured article]. Epub October 7, 2009. J. Virol. 83:12725–12737. Scholtes, L, Yang, K., .Li, L.X., and J.D. Baines. (2010). The capsid protein encoded by UL17 of herpes simplex virus 1 interacts with the tegument protein VP13/14. J. Virol. 84:7642-7650. Roberts, K.L., and J.D. Baines. (2010). Myosin Va enhances secretion of herpes simplex virus 1 virions and cell surface expression of viral glycoproteins. J Virol. 84:9889-9896. (Epub June, 2010). Roberts, KL and J.D. Baines. (2011). UL31 of herpes simplex virus is required for optimal viral gene expression. In Press, J. Virol. 85:4947-4953. (Epub March, 2011). |