Abstract
The virion protein, Vmw65, of herpes simplex virus selectively induces the transcription of the virus immediate–early genes and is required for normal virus replication and for virulence in animal models. Vmw65 operates by interacting with a host cell transcription factor (Oct-1) and analysis of the structure/function relationship within Vmw65 has facilitated the design of a peptide, corresponding to a local domain of the protein, which interferes with the Vmw65–Oct-1 interaction. The selective interference of protein–protein interactions involved in gene regulation may provide a suitable target for the inhibition of virus replication.
