Jeremy P. Kamil, Ph.D.

Assistant Professor

Contact Information:
Email: Office Phone:   318-675-5771
Laboratory Phone:  318-675-5773
Office Fax:  318-675-5764


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 or immature immune systems. Our research is focused on two questions: (i) How does the virus regulate its genes during infection? and (ii) How does HCMV regulate its tropism for the diverse array of cell types it encounters during natural infection?  Pertinent to the first question, we have a longstanding interest in a viral protein kinase encoded by HCMV, UL97, which is named after the open reading frame that encodes it. One role of UL97 is to inactivate the retinoblastoma tumor suppressor protein (pRb), which is a key regulator of cellular genes. Among several exciting projects concerning gene expression, we are investigating whether pRb is recruited to viral chromatin to regulate viral genes.  Moreover, in collaboration with two other laboratories, we are also examining a fascinating connection we recently discovered between UL97 and a cluster of viral genes that regulate HCMV latency.  With regard to the second question, our studies of HCMV cell tropism were initiated following a discovery in our lab that a viral gene called UL148 strongly influences the ability of HCMV to infect epithelial cells.  Follow up studies revealed that the encoded protein, UL148, resides in the endoplasmic reticulum and promotes efficient maturation of a viral glycoprotein complex, gH/gL/gO, that is necessary for infection of cell types, such as fibroblasts, which the virus infects by fusing at the plasma membrane.  A second gH/gL complex, gH/gL/UL128-131 is also found on HCMV virions, and is crucial for infection of cell types in which the virus requires endocytosis, and hence, fusion of the virion with endosomal membranes for infection.  Although several other herpesviruses employ alternate gH/gL complexes to regulate their membrane fusion machinery, UL148 appears to be the first example of a virally-encoded factor that regulates the relative abundance of the two alternate complexes. 

Representative Publications:


Li G, Nguyen CC, Ryckman BJ, Britt WJ, and JP Kamil. 2015. A Viral Regulator of Glycoprotein Complexes Contributes To Human Cytomegalovirus Cell Tropism. Proc. Natl. Acad. Sci., U S A. 112: 4471-4476


Li G, Rak M, Nguyen CC, Umashankar M, Goodrum FD, and JP Kamil. 2014. An Epistatic Relationship Between the Viral Protein Kinase UL97 and the UL133-UL138 Latency Locus During the Human Cytomegalovirus Lytic Cycle. J. Virol. 88: 6047-6060.

Wang D, Li G, Schauflinger M, Nguyen CC, Hall ED, Yurochko AD, von Einem, J. and JP Kamil. 2013. The ULb' region of the human cytomegalovirus genome confers an increased requirement for the viral protein kinase UL97. J. Virol. 87: 6359-6376.

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., U S A. 106: 16823-16828.

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.

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



All Publications: PubMed