Date of Award




Document Type


Degree Name

Doctor of Philosophy (PhD)


Department of Biomedical Sciences

Content Description

1 online resource (xi, 139 pages) : PDF file, illustrations (some color)

Dissertation/Thesis Chair

April D Burch

Committee Members

Paul Masters, Kathleen McDonough, Scott Tenenbaum, Joseph Wade


HSV-1, microRNA, miRNA, Proteasome, VICE, Herpes simplex virus, Non-coding RNA, Viroids

Subject Categories

Microbiology | Virology


Herpes Simplex Virus Type 1 (HSV-1) is a human pathogen that is estimated to have infected 60-80% of the population worldwide, causing oral lesions, encephalitis, and blindness. Infection results in life-long latency of the virus, with periods of reactivation and symptomatic disease. Early in infection, HSV-1 induces the formation of replication compartments and VICE (virus induced chaperone enriched) domains within the nucleus. Adjacent to VICE domains, we observed foci which contained Mss1, a cellular protein normally associated with the proteasome. Mss1 belongs to the AAA-ATPase family of proteins, which have been shown to function in DNA repair, transcription, translation, and the stress response. In ECP19 cells, which are naturally reduced in Mss1 protein and mRNA levels, HSV-1 does not replicate. Based on Mss1's accessory functions and observed localization, we sought to determine if Mss1 played a role in HSV-1 infection. Addition of Mss1 to non-permissive ECP19 cells which have endogenously lower levels of Mss1 did not alter HSV-1 replication. Furthermore, siRNA knockdown of Mss1 in normally permissive cells did not alter HSV-1 replication. These results indicated that Mss1 was likely a dispensable accessory factor incorporated to VICE domains during HSV-1 replication.

Included in

Virology Commons