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Journal of Virology, January 1999, p. 417-426, Vol. 73, No. 1
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

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

Roger D. Everett,* Michayla Meredith,dagger and Anne Orr

MRC Virology Unit, Glasgow G11 5JR, Scotland, United Kingdom

Received 22 June 1998/Accepted 8 October 1998

Herpes simplex virus type 1 immediate-early protein Vmw110 stimulates the onset of virus infection and is required for efficient reactivation from latency. In transfection assays, Vmw110 is a potent activator of gene expression, but its mode of action has yet to be determined. Previous work has shown 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 infected and transfected cells. It has also been found that Vmw110 binds strongly and specifically to a ubiquitin-specific protease known as HAUSP, itself a component of a subset of ND10. In this study we have investigated the role of HAUSP in Vmw110 activity; single amino acid residues of Vmw110 required for the interaction were identified, and the effects of mutation of these residues in infected and transfected cells were then assayed. The results indicate that the ability to bind to HAUSP contributes to the functional activities of Vmw110.

* Corresponding author. Mailing address: MRC Virology Unit, Institute of Virology, Church St., Glasgow, Scotland G11 5JR, United Kingdom. Phone: 141 330 3923. Fax: 141 337 2236. E-mail: r.everett{at}vir.gla.ac.uk.

dagger Present address: Department of Biochemistry, University of Dundee, Dundee DD1 5EH, Scotland.

Journal of Virology, January 1999, p. 417-426, Vol. 73, No. 1
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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