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J Gen Virol 76 (1995), 2369-2374; DOI 10.1099/0022-1317-76-9-2369
© 1995 Society for General Microbiology
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The equine herpesvirus 1 gene 63 RING finger protein partially complements Vmw110, its herpes simplex virus type 1 counterpart

Roger Everett*, Anne Orr and Maggie Elliott

MRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, UK

All alpha herpesviruses of known DNA sequence have been found to encode a protein with similarities to immediate early protein Vmw110 (ICP0) of herpes simplex virus type 1 (HSV-1). The conserved portion of this family of proteins is a characteristic zinc binding module, known as a RING finger or C3HC4 domain. Examples of RING finger domains occur in many other proteins of diverse evolutionary origin and function. Recently, the solution structure of the equine herpesvirus 1 (EHV-1) RING finger protein, encoded by gene 63, has been solved. To investigate whether this structure could be considered to be a paradigm of herpesvirus RING domains, we have constructed a recombinant HSV-1 which expresses the EHV-1 gene 63 protein (EHVg63) in place of Vmw110. Comparison of the growth properties of the recombinant with those of wild-type and Vmw110-defective viruses indicates that EHVg63 is able to fulfil partially, but not completely, the roles of Vmw110 during virus growth in tissue culture.

* Author for correspondence. Fax +44 141 3372236. e-mail everett@vir.gla.ac.uk

Received 24 January 1995; accepted 3 May 1995.


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Copyright © 1995 by the Society for General Microbiology.