Does herpes simplex virus type 1 UL14 tegument protein regulate intracellular compartmentalization of major tegument protein VP16?
Our findings suggest that a cluster of charged residues within the HSP-like sequence of UL14 is important for the molecular chaperone-like functions of UL14, and this activity is required for the acquisition of functionality of VP16 and UL46. In addition, UL14 likely contributes to maintaining cellular homeostasis following infection, including cytoskeletal organization. However, direct interactions between UL14 and VP16, UL46, or other cellular or viral proteins remain unclear.
These findings provide additional insight into EOC etiology and may serve as novel biomarkers for EOC susceptibility.