|Department:||Veterinary Microbiology & Pathology|
|Credentials:||1996 - Ph.D., University of Pennsylvania; Microbiology and Virology|
|Mailing Address:||Veterinary Microbiology & Pathology|
Paul G. Allen School for Global Animal Health
Washington State University
PO Box 647040
Pullman, WA 99164-7040
Infectious diseases, virus entry, herpes simplex virus, sexually transmitted diseases, virus-cell interaction
Dr. Nicola has more than 15 years of experience studying the cell biology of herpes simplex virus glycoproteins and entry, and is perhaps best known for revealing that herpes viruses utilize low pH, endocytic pathways to enter and infect biologically relevant cells. This finding conflicted with the long-held dogma that herpes viruses were a paradigm for viruses that enter solely by direct fusion with the plasma membrane. However, over a short period of time, these findings were integrated into the field, and it was recognized that other herpes viruses including human cytomegalovirus, Kaposi’s sarcoma herpes virus and varicella zoster virus utilize similar pathways. In addition to pH-triggered entry, the Nicola lab also investigates the proteasome-dependent delivery of HSV capsids to the nucleus during entry. We utilize a combination of cellular, molecular, biochemical, and microscopic approaches to delineate the step-by-step itinerary of the incoming virus. A better understanding of how herpes simplex virus interacts with the cell will identify novel targets for intervention.
Komala Sari T, Pritchard SM, Cunha CW, Wudiri GA, Laws EI, Aguilar HC, Taus NS and AV Nicola. 2013. "Contributions of herpes simplex virus 1 envelope proteins to viral entry by endocytosis." Journal of Virology 87: 13922-13926.
Pritchard SM, Cunha CW, and AV Nicola. 2013. "Analysis of herpes simplex virion tegument ICP4 derived from infected cells and ICP4-complementing cells." PLoS ONE 8 (8):e70889.
Dollery SJ, CC Wright, et al. (2011). "Low-pH-dependent changes in the conformation and oligomeric state of the prefusion form of herpes simplex virus glycoprotein B are separable from fusion activitiy." Journal of Virology 85(19):9964-9973.
Delboy MG and AV Nicola (2011). "A pre-immediate-early role for teument ICP0 in the proteasome-dependent entry of herpes simplex virus." Journal of Virology 85(12):5910-5918.
Siekavizza-Robles CR, SJ Dollery, et al. (2010). "Reversible conformational change in herpes simplex virus glycoprotein B with fusion-from-without activity is triggered by mildly acidic pH." Virology journal 7:352.
Dollery SJ, MG Delboy, et al. (2010). "Low pH-induced conformational change in herpes simplex virus glycoprotein B." Journal of Virology 84(8):3759-3766.
Dollery SJ, KD Lane, et al. (2010) "Role of the UL45 protein in herpes simplex virus entry via low pH-dependent endocytosis and its relationship to the conformation and function of glycoprotein B."
Delboy MG, CR Siekavizza-Robles, et al. (2010). "Herpes simplex virus tegument ICP0 is capsid associated, and its E3 ubiquitin ligase domain is important for incorporation into virions." Journal of Virology 84(3):1637-1640.