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Journal of Virology, February 2006, p. 1588-1591, Vol. 80, No. 3
0022-538X/06/$08.00+0 doi:10.1128/JVI.80.3.1588-1591.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Richard W. P. Smith,1,
Gavin S. Wilkie,2,
Poonam Malik,1,
Nicola K. Gray,2,3* and
J. Barklie Clements1
Division of Virology, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G11 5JR, Scotland, United Kingdom,1 MRC Human Genetics Unit, Western General Hospital, Edinburgh EH4 2XU, Scotland, United Kingdom,2 School of Molecular and Clinical Medicine, 3rd Floor Outpatients Department, Western General Hospital, University of Edinburgh, Edinburgh, Scotland EH4 2XU, United Kingdom3
Received 10 July 2005/ Accepted 11 November 2005
Herpes simplex virus type 1 (HSV-1) ICP27 protein is an essential regulator of viral gene expression with roles at various levels of RNA metabolism in the nucleus. Using the tethered function assay, we showed a cytoplasmic activity for ICP27 in directly enhancing mRNA translation in vivo in the absence of other viral factors. The region of ICP27 required for translational stimulation maps to the C terminus. Furthermore, in infected cells, ICP27 is associated with polyribosomes, indicating a function in translation during the lytic cycle.
This work is dedicated to the memory of J. Barklie Clements, who was co-corresponding author and died during revision of the manuscript. We dedicate this article to Barklie for his long-standing contribution to the herpesvirus field and for being a wonderful person and a great scientist. He will be sadly missed by all of us in his group, his friends, and his colleagues for his enthusiasm, encouragement, and support.
These authors contributed equally to this work.
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