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Journal of Virology, November 2008, p. 10946-10952, Vol. 82, No. 21
0022-538X/08/$08.00+0     doi:10.1128/JVI.01403-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Characterization of a CRM1-Dependent Nuclear Export Signal in the C Terminus of Herpes Simplex Virus Type 1 Tegument Protein UL47{triangledown}

Paul Williams, Janneke Verhagen,{dagger} and Gillian Elliott*

Department of Virology, Faculty of Medicine, Imperial College London, London, United Kingdom

Received 7 July 2008/ Accepted 13 August 2008

The herpes simplex virus type 1 tegument protein known as VP13/14, or hUL47, localizes to the nucleus and binds RNA. Using fluorescence loss in photobleaching analysis, we show that hUL47 undergoes nucleocytoplasmic shuttling during infection. We identify the hUL47 nuclear export signal (NES) as a C-terminal 10-residue hydrophobic peptide and measure its efficiency relative to that of the classical human immunodeficiency virus type 1 Rev NES. Finally, we show that the hUL47 NES is sensitive to the inhibitor of CRM1-mediated nuclear export leptomycin B. Hence, hUL47 joins a growing list of virus-encoded RNA-binding proteins that use CRM1 to exit the nucleus.

* Corresponding author. Mailing address: Department of Virology, Faculty of Medicine, Imperial College London, St. Mary's Campus, Norfolk Place, London W2 1PG, United Kingdom. Phone: 44 207 594 5037. Fax: 44 207 594 3973. E-mail: g.elliott{at}imperial.ac.uk

{triangledown} Published ahead of print on 20 August 2008.

{dagger} Present address: Aaron Diamond AIDS Research Center, 455 First Avenue, New York, NY 10016.

Journal of Virology, November 2008, p. 10946-10952, Vol. 82, No. 21
0022-538X/08/$08.00+0     doi:10.1128/JVI.01403-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



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