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Herpes simplex virus type 1 immediate-early protein Vmw110 (also known as ICP0) has been implicated in the control of the balance between the lytic and latent states, but the precise mechanisms by which it exerts its effects are unknown. Vmw110 includes a characteristic zinc binding domain, termed the C3HC4 domain or RING finger, which is essential for its function. The solution structure of a related herpesvirus RING finger domain suggested that an amphipathic alpha helix might be an important functional component of the RING finger. In this paper, we show that the equivalent region of Vmw110 is important for virus growth in tissue culture and for the normal interaction of Vmw110 with nuclear structures which include the PML protein.

Original publication




Journal article


Journal of virology

Publication Date





7339 - 7344


Medical Research Council Virology Unit, Glasgow, Scotland.


Kidney, Cell Line, Hela Cells, Cell Nucleus, Animals, Horses, Humans, Simplexvirus, Ubiquitin-Protein Ligases, Immediate-Early Proteins, Neoplasm Proteins, Tumor Suppressor Proteins, Nuclear Proteins, Recombinant Proteins, Transcription Factors, Transfection, Mutagenesis, Site-Directed, Virus Latency, Gene Expression Regulation, Viral, Amino Acid Sequence, Protein Structure, Secondary, Zinc Fingers, Kinetics, Point Mutation, Molecular Sequence Data, Cricetinae, Promyelocytic Leukemia Protein