Major Department



College of Liberal Arts & Sciences


BS (Bachelor of Science)

Session and Year of Graduation

Fall 2017

Honors Major Advisor

Linda McCarter

Thesis Mentor

Richard Roller


Following reactivation from latency herpesviruses utilize the conserved ability of cell-to-cell spread to evade the host immune response, mediating disease and viral shedding. The UL51 protein of herpes simplex virus 1 is a conserved tegument protein that functions in cytoplasmic assembly and secondary envelopment. Partial deletions of UL51 are associated with strong cell-to-cell spread defects. UL51 has no known enzymatic ability suggesting its function in cell-to-cell spread is likely dependent on specific interactions with other proteins. It has been shown to form complexes with UL7, the gE/gI complex and itself. However, it is unknown whether the self-interaction is a direct interaction or an interaction mediated by another component. A co-immunoprecipitation assay using plasmid expression of differentially tagged UL51 proteins demonstrates that the UL51 protein does not require other viral proteins for self-interaction. Using UL51 truncations coinciding with regions of conservation we began mapping regions important for self-interaction through co-immunoprecipitation and co-localization assays. We expect that determining the mechanism of interaction that UL51 has with itself will lead to the development of ways to determine the significance of the self-interactions for cell-to-cell spread, viral assembly or both.

Total Pages

23 pages


Copyright © 2017 Samantha Ryken