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Journal of Virology, June 2003, p. 6351-6358, Vol. 77, No. 11
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.11.6351-6358.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Herpes Simplex Virus Type 1 Portal Protein UL6 Interacts with the Putative Terminase Subunits UL15 and UL28

Colleen A. White,{dagger} Nigel D. Stow, Arvind H. Patel, Michelle Hughes, and Valerie G. Preston*

MRC Virology Unit, Institute of Virology, Glasgow G11 5JR, United Kingdom

Received 15 October 2002/ Accepted 12 March 2003

The herpes simplex virus type 1 (HSV-1) UL6, UL15, and UL28 proteins are essential for cleavage of replicated concatemeric viral DNA into unit length genomes and their packaging into a preformed icosahedral capsid known as the procapsid. The capsid-associated UL6 DNA-packaging protein is located at a single vertex and is thought to form the portal through which the genome enters the procapsid. The UL15 protein interacts with the UL28 protein, and both are strong candidates for subunits of the viral terminase, a key component of the molecular motor that drives the DNA into the capsid. To investigate the association of the UL6 protein with the UL15 and UL28 proteins, the three proteins were produced in large amounts in insect cells with the baculovirus expression system. Interactions between UL6 and UL28 and between UL6 and UL15 were identified by an immunoprecipitation assay. These results were confirmed by transiently expressing wild-type and mutant proteins in mammalian cells and monitoring their distribution by immunofluorescence. In cells expressing the single proteins, UL6 and UL15 were concentrated in the nuclei whereas UL28 was found in the cytoplasm. When the UL6 and UL28 proteins were coexpressed, UL28 was redistributed to the nuclei, where it colocalized with UL6. In cells producing either of two cytoplasmic UL6 mutant proteins and a functional epitope-tagged form of UL15, the UL15 protein was concentrated with the mutant UL6 protein in the cytoplasm. These observed interactions of UL6 with UL15 and UL28 are likely to be of major importance in establishing a functional DNA-packaging complex at the portal vertex of the HSV-1 capsid.

* Corresponding author. Mailing address: MRC Virology Unit, Institute of Virology, Church St., Glasgow G11 5JR, United Kingdom. Phone: 44 141 330 4025. Fax: 44 141 337 2236. E-mail: v.preston{at}vir.gla.ac.uk.

{dagger} Present address: Development Laboratory, Excell Biotech, Livingston EH53 0TG, United Kingdom.

Journal of Virology, June 2003, p. 6351-6358, Vol. 77, No. 11
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.11.6351-6358.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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