The ability of herpes simplex virus type 1 immediate-early protein Vmw110 to bind to a ubiquitin-specific protease contributes to its roles in the activation of gene expression and stimulation of virus replication

Herpes simplex virus type 1 immediate-early protein Vmw110 stimulates the o nset of virus infection and is required for efficient reactivation from lat ency. In transfection assays, Vmw110 is a potent activator of gene expressi on, but its mode of action has yet to be determined. Previous work has show n that Vmw110 localizes to specific intranuclear structures known as ND10, PML bodies, or PODs and causes the disruption of these domains. The ability of Vmw110 to disrupt ND10 correlates with its biological activities in inf ected and transfected cells. It has also been found that Vmw110 binds stron gly and specifically to a ubiquitin-specific protease known as HAUSP, itsel f a component of a subset of ND10, In this study we have investigated the r ole of HAUSP in Vmw110 activity; single amino acid residues of Vmw110 requi red for the interaction were identified, and the effects of mutation of the se residues in infected and transfected cells were then assayed. The result s indicate that the ability to bind to HAUSP contributes to the functional activities of Vmw110.