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Journal of Virology, February 1999, p. 1704-1707, Vol. 73, No. 2
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Physical and Functional Interactions between the Herpes Simplex Virus UL15 and UL28 DNA Cleavage and Packaging Proteins

Kim M. Koslowski,1 Patti R. Shaver,1 James T. Casey II,1 Todd Wilson,2 Gregory Yamanaka,2 Amy K. Sheaffer,2 Daniel J. Tenney,2 and Nels E. Pederson1,*

Department of Microbiology and Immunology, East Carolina University School of Medicine, Greenville, North Carolina 27858,1 and Department of Virology, Bristol-Myers Squibb Pharmaceutical Research Institute, Wallingford, Connecticut 064922

Received 2 July 1998/Accepted 27 October 1998

Herpes simplex virus (HSV) DNA is cleaved from concatemers and packaged into capsids in infected cell nuclei. This process requires seven viral proteins, including UL15 and UL28. UL15 expressed alone displays a nuclear localization, while UL28 remains cytoplasmic. Coexpression with UL15 enables UL28 to enter nuclei, suggesting an interaction between the two proteins. Additionally, UL28 copurified with UL15 from HSV-infected cells after ion-exchange and DNA affinity chromatography, and the complex sedimented as a 1:1 heterodimer upon sucrose gradient centrifugation. These findings are evidence of a physical interaction of UL15 and UL28 and a functional role for UL15 in directing UL28 to the nucleus.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, Brody Medical Sciences Building, East Carolina University School of Medicine, 600 Moye Blvd., Greenville, NC 27858-4354. Phone: (252) 816-2706. Fax: (252) 816-3104. E-mail: pederson{at}brody.med.ecu.edu.

Journal of Virology, February 1999, p. 1704-1707, Vol. 73, No. 2
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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