Assistant Professor

Contact Information:
Email: jkamil@lsuhsc.edu
Office Phone:   318-675-5771
Laboratory Phone:  318-675-5773
Office Fax:  318-675-5764

Education/Training:

Postdoctoral Study, Harvard Medical School

Postdoctoral Study, Cornell University

Ph.D., Microbiology, 2003, University of California, Davis

B.A., General Biology, 1997, Cornell University

Major Research Interests:  Human cytomegalovirus replication, viral cyclin-dependent kinase mimicry, virus-cell interactions

Human cytomegalovirus (HCMV) is a widespread pathogen that infects most of the human population. Although HCMV infection is typically asymptomatic in healthy people, HCMV causes severe disease in people with compromised immune systems.  HCMV is also the most common viral infection present at childbirth, and frequently causes congenital defects.  HCMV encodes a protein kinase, UL97, which is clinically important as the viral gene product that activates ganciclovir, a viral DNA synthesis inhibitor.  UL97 is also the target of maribavir, a new drug currently under investigation, which directly inhibits UL97.  Our research has helped establish that UL97 is required for at least two processes during viral replication: (i) to inactivate the retinoblastoma tumor suppressor protein (pRb), and (ii) to promote disassembly of the nuclear lamina by phosphorylating lamin A/C.   Inactivation of pRb appears to be required for efficient viral DNA synthesis, while phosphorylation of lamin A/C is hypothesized to be important for escape of newly assembled virus particles from the nucleus.  Interestingly, infections lacking UL97 activity (either due to drug inhibition or genetic ablation of the UL97 gene) can result in mild to extremely severe defects in production of infectious virus particles.  The degree of these defects depends on the HCMV strain being studied, the cell type being infected, and the culture conditions being used.  The goal of our research is to better understand the cellular and viral factors that govern these UL97-dependent replication defects.  We hope that our findings will help clinicians make better use of UL97 as a target for increasingly effective antiviral drug therapies.

Representative Publications:

Kamil JP and DM Coen. 2007. Human cytomegalovirus protein kinase UL97 forms a complex with the tegument phosphoprotein pp65. J Virol 81:10659-10668.

Hume AJ, Finkel JS, Kamil JP, Coen DM, Culbertson MR, and RF Kalejta. 2008. Phosphorylation of retinoblastoma protein by viral protein with cyclin-dependent kinase function. Science 320: 797-799.

Hamirally S*, Kamil JP*, Ndassa-Colday Y, Lin AJ, Jahng WJ, Baek, MC, Noton S, Simpson-Holley M, Silva LA, Knipe DM, Golan DE, Marto JA, and DM Coen. 2009. Viral mimicry of cdc2/cyclin-dependent kinase 1 mediates disruption of nuclear lamina during human cytomegalovirus nuclear egress. PLoS Pathogens 5 (1): e1000275. *contributed equally

Kamil JP, Hume AJ, Jurak I, Münger K, Kalejta RF, and DM Coen. 2009. Human papillomavirus E7 inactivator of retinoblastoma family proteins complements human cytomegalovirus lacking UL97 protein kinase. Proc Natl Acad Sci, 106 (39): 16823-16828.

All Publications: PubMed