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Journal of Virology, July 2008, p. 6654-6666, Vol. 82, No. 13
0022-538X/08/$08.00+0     doi:10.1128/JVI.00257-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

The UL25 Gene Product of Herpes Simplex Virus Type 1 Is Involved in Uncoating of the Viral Genome{triangledown}

Valerie G. Preston,* Jill Murray, Christopher M. Preston, Iris M. McDougall, and Nigel D. Stow

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

Received 5 February 2008/ Accepted 21 April 2008

Studies on the herpes simplex virus type 1 UL25-null mutant KUL25NS have shown that the capsid-associated UL25 protein is required at a late stage in the encapsidation of viral DNA. Our previous work on UL25 with the UL25 temperature-sensitive (ts) mutant ts1204 also implicated UL25 in a role at very early times in the virus growth cycle, possibly at the stage of penetration of the host cell. We have reexamined this mutant and discovered that it had an additional ts mutation elsewhere in the genome. The ts1204 UL25 mutation was transferred into wild-type (wt) virus DNA, and the UL25 mutant ts1249 was isolated and characterized to clarify the function of UL25 at the initial stages of virus infection. Indirect immunofluorescence assays and in situ hybridization analysis of virus-infected cells revealed that the mutant ts1249 was not impaired in penetration of the host cell but had an uncoating defect at the nonpermissive temperature. When ts1249-infected cells were incubated initially at the permissive temperature to allow uncoating of the viral genome and subsequently transferred to the restrictive temperature, a DNA-packaging defect was evident. The results suggested that ts1249, like KUL25NS, had a block at a late stage of DNA packaging and that the packaged genome was shorter than the full-length genome. Examination of ts1249 capsids produced at the nonpermissive temperature revealed that, in comparison with wt capsids, they contained reduced amounts of UL25 protein, thereby providing a possible explanation for the failure of ts1249 to package full-length viral DNA.

* Corresponding author. Mailing address: MRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, United Kingdom. Phone: 44 141 330 4019. Fax: 44 141 337 2236. E-mail: v.preston{at}mrcvu.gla.ac.uk

{triangledown} Published ahead of print on 30 April 2008.

Journal of Virology, July 2008, p. 6654-6666, Vol. 82, No. 13
0022-538X/08/$08.00+0     doi:10.1128/JVI.00257-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Pasdeloup, D., Blondel, D., Isidro, A. L., Rixon, F. J. (2009). Herpesvirus Capsid Association with the Nuclear Pore Complex and Viral DNA Release Involve the Nucleoporin CAN/Nup214 and the Capsid Protein pUL25. J. Virol. 83: 6610-6623 [Abstract] [Full Text]  
  • Cockrell, S. K., Sanchez, M. E., Erazo, A., Homa, F. L. (2009). Role of the UL25 Protein in Herpes Simplex Virus DNA Encapsidation. J. Virol. 83: 47-57 [Abstract] [Full Text]  


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