Association of two membrane proteins encoded by herpes simplex virus type 2, UL11 and UL56.

Herpes simplex virus (HSV) acquires envelope by budding into trans-Golgi network (TGN)-derived vesicles. Previous studies showed that the UL11 gene product enables efficient virion envelopment and export from infected cells and is incorporated into virions as tegument protein. At its N-terminus, UL11 is dually acylated by myristoic and palmitoic acids. Fatty acylation of UL11 provides both membrane binding strength and Golgi-targeting specificity. We show here that UL11 interacts with UL56 protein, a tail-anchored type II membrane protein encoded by HSV, which associated with the Golgi apparatus and cytoplasmic vesicles. We previously showed that UL56 is involved in vesicular transport in infected cells. The UL11-UL56 complex localized to the perinuclear region of the cytoplasm in infected cells. Fatty acylation of UL11 was important for the formation of the UL11-UL56 protein complex. Taken together, our results identify a novel interaction between two HSV proteins facilitated by mutual interactions with Golgi-derived vesicles.