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Dr. Gershburg


Edward Gershburg
Associate Professor
phone: 217.545.1139

Dr. Gershburg is an associate professor in the Department of Medical Microbiology, Immunology and Cell Biology at SIU School of Medicine and a member of the SIU Simmons Cancer Institute. Dr. Gershburg is a member of the American Society for Microbiology, International Association for Research on Epstein-Barr virus and Associated Diseases, and International Society of Antiviral Research.

Education and Training:
1998 - 2005 Postdoctoral training, Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC

1998 Ph.D. in Virology, Tel Aviv University, Ramat Aviv, Israel

1992 M.S. in Microbiology, St. Petersburg State University, St. Petersburg, Russia

Academic appointments:
2005 - 2007 Research Assistant Professor; Department of Microbiology and Immunology, University of North Carolina at Chapel Hill, Chapel Hill, NC
2007 - Assistant Professor; Department of Medical Microbiology, Immunology and Cell Biology; Simmons Cancer Institute; Southern Illinois University School of Medicine, Springfield, IL                                                                                                       2013 - Associate Professor; Department of Medical Microbiology, Immunology and Cell Biology; Simmons Cancer Institute; Southern Illinois University School of Medicine, Springfield, IL

Research Focus –
Biology and pathogenesis of the human herpesvirus, Epstein-Barr virus (EBV)

Epstein-Barr Virus (EBV) is one of the eight human herpesviruses and an important opportunistic pathogen. EBV is now recognized as a causative agent in most cases of infectious mononucleosis, and is detectable in over 90% of the population worldwide. EBV is also associated with the development of several malignancies of lymphoid and epithelial origin, including Burkitt’s lymphoma, post-transplantation lymphoproliferative disorders (PTLD), Hodgkin’s disease, AIDS-related lymphomas, NK/T cell lymphoma, and nasopharyngeal carcinoma. EBV has a biphasic infection cycle consisting of a latent and a lytic, replicative phase. Latency is characterized by limited gene expression, lack of virion production, and is responsible for immortalization of infected cells. Hence, the oncogenic properties of EBV are historically associated with latent infection. In contrast, most viral genes are expressed during the lytic cycle, which results in assembly and release of infectious virus particles. Viral genes expressed in the lytic phase are rarely expressed in EBV-associated tumors, with the notable exception of lymphoproliferative diseases in the immunosuppressed host, in which they may play a pathogenic role; lytic infection also plays a role in establishing latency and facilitates virus spread. Consistent presence of the EBV in the aforementioned diseases and its role in their development offers a unique opportunity for design of highly-specific, virus-targeting therapies.
The major focus of the research in this laboratory is to understand the role in viral infection and identify the targets of the virally-encoded protein kinase (EBV-PK), an EBV BGLF4 gene product. We have previously shown that this protein kinase is essential for the EBV replication, and is a potential target for antiviral therapies. Two current projects in the laboratory are: (I) biochemical analyses of the EBV-PK enzymology and structure aimed to develop specific inhibitors with an antiviral potential; and (II) studies of EBV BKRF4 protein, which is one of the substrates of the EBV-PK, and its homologues in other herpesviruses.

Selected Publications

Goswami R, Gershburg S, Satorius A, Gershburg, E. (2012) Protein kinase inhibitors that inhibit induction of lytic program and replication of Epstein-Barr virus. Antiviral Res. 96(3):296-304. doi: 10.1016/j.antiviral.2012.09.021. [Epub ahead of print]

Halford, W. P., Püschel, R., Gershburg, E., Wilber, A., Gershburg, S., and B. Rakowski (2011) A live-attenuated HSV-2 ICP0- virus elicits 10 to 100 times greater protection against genital herpes than a glycoprotein D subunit vaccine. PLoS ONE, 11;6(3):e17748.

Gershburg, S., Murphy, L., Marschall, M. and E. Gershburg (2010) Mutagenesis of the Epstein-Barr virus (EBV)-encoded protein kinase reveals motifs required for activity and localization. Biochem J., 431(2):227-235. Epub. 2010 Aug 12.

Meng, Q., Hagemeier, S. R., Fingeroth, J. D., Gershburg, E., Pagano, J. S. and S. C. Kenney (2010) The EBV-encoded protein kinase, EBV-PK, but not the thymidine kinase (EBV-TK), is required for ganciclovir and acyclovir inhibition of lytic viral production. J. Virol., 84(9):4534-42.

Liu M, Rakowski B, Gershburg E, Weisend CM, Lucas O, et al. (2010) ICP0 Antagonizes ICP4-Dependent Silencing of the Herpes Simplex Virus ICP0 Gene. PLoS ONE 5(1): e8837. doi:10.1371/journal.pone.0008837

Wang F.Z., Roy D., Gershburg E., Whitehurst C.B. Dittmer D.P., Pagano J.S. (2009) Maribavir inhibits epstein-barr virus transcription in addition to viral DNA replication. J Virol. Dec;83(23):12108-17. Epub 2009 Sep 16.

Whitehurst CB, Ning S, Bentz GL, Dufour F, Gershburg E, Shackelford J, Langelier Y, Pagano JS (2009) The Epstein-Barr virus (EBV) deubiquitinating enzyme BPLF1 reduces EBV ribonucleotide reductase activity. J Virol. 83(9):4345-53. Epub 2009 Feb 25.

Gershburg, E. and J. S. Pagano (2008) Conserved herpesvirus protein kinases. Biochim Biophys Acta 1784(1):203-12. Epub 2007 Aug 16.

Gershburg, E., Raffa, S., Torrisi, M. R. and J. S. Pagano (2007) Epstein-Barr virus-encoded protein kinase (BGLF4) is essential for production of infectious virus. J. Virol. 81(10): 5407-5412.

Gershburg, E. and J. S. Pagano (2005) Treatment of Epstein-Barr Virus (EBV) infections. J Antimicrob Chemother. 56(2):277-81. Epub 2005 Jul 8.

Yue, W., Gershburg, E. and J. S. Pagano. (2005) Epstein-Barr Virus protein kinase phosphorylates EBNA2 and suppresses EBNA2 transactivation of LMP1 promoter. J. Virol. 79(9):5880-5885.

Gershburg, E., M. Marschall, K. Hong and J. S. Pagano (2004) Expression and localization of Epstein-Barr Virus encoded protein kinase. J Virol., 78(22):12140-12146.