This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Newcomb, W. W.
Right arrow Articles by Brown, J. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Newcomb, W. W.
Right arrow Articles by Brown, J. C.

 Previous Article

Journal of Virology, October 2002, p. 10084-10088, Vol. 76, No. 19
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.19.10084-10088.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Inhibition of Herpes Simplex Virus Replication by WAY-150138: Assembly of Capsids Depleted of the Portal and Terminase Proteins Involved in DNA Encapsidation

William W. Newcomb and Jay C. Brown*

Department of Microbiology and Cancer Center, University of Virginia Health System, Charlottesville, Virginia 22908

Received 18 April 2002/ Accepted 24 June 2002

Studies were carried out to examine the mechanism of action of WAY-150138, a member of a novel group of thiourea compounds recently shown to inhibit replication of herpes simplex virus type 1 (HSV-1). Previous studies have shown that the drug acts by preventing DNA encapsidation and that resistant mutants map to UL6, the gene encoding the protein subunit of the portal complex through which DNA enters the capsid. We tested the idea that WAY-150138 acts by preventing the incorporation of DNA-packaging proteins into capsids as they are assembled. Capsids were isolated from HSV-1-infected, drug-treated cells and examined by Western immunoblotting for the presence of two packaging proteins, the portal subunit (UL6) and a candidate terminase subunit (UL15). The results showed that both proteins were depleted in the capsids, suggesting that WAY-150138 antagonizes DNA encapsidation by depriving capsids of packaging proteins during the assembly process.

* Corresponding author. Mailing address: Department of Microbiology, University of Virginia Health System, Box 800734, Charlottesville, VA 22908. Phone: (434) 924-1814. Fax: (434) 982-1071. E-mail: JCB2G{at}VIRGINIA.EDU.

Journal of Virology, October 2002, p. 10084-10088, Vol. 76, No. 19
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.19.10084-10088.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Yang, K., Homa, F., Baines, J. D. (2007). Putative Terminase Subunits of Herpes Simplex Virus 1 Form a Complex in the Cytoplasm and Interact with Portal Protein in the Nucleus. J. Virol. 81: 6419-6433 [Abstract] [Full Text]  
  • Pesola, J. M., Coen, D. M. (2007). In vivo fitness and virulence of a drug-resistant herpes simplex virus 1 mutant. J. Gen. Virol. 88: 1410-1414 [Abstract] [Full Text]  
  • Pesola, J. M., Zhu, J., Knipe, D. M., Coen, D. M. (2005). Herpes Simplex Virus 1 Immediate-Early and Early Gene Expression during Reactivation from Latency under Conditions That Prevent Infectious Virus Production. J. Virol. 79: 14516-14525 [Abstract] [Full Text]  
  • Newcomb, W. W., Homa, F. L., Brown, J. C. (2005). Involvement of the Portal at an Early Step in Herpes Simplex Virus Capsid Assembly. J. Virol. 79: 10540-10546 [Abstract] [Full Text]  
  • Singer, G. P., Newcomb, W. W., Thomsen, D. R., Homa, F. L., Brown, J. C. (2005). Identification of a Region in the Herpes Simplex Virus Scaffolding Protein Required for Interaction with the Portal. J. Virol. 79: 132-139 [Abstract] [Full Text]  
  • Newcomb, W. W., Thomsen, D. R., Homa, F. L., Brown, J. C. (2003). Assembly of the Herpes Simplex Virus Capsid: Identification of Soluble Scaffold-Portal Complexes and Their Role in Formation of Portal-Containing Capsids. J. Virol. 77: 9862-9871 [Abstract] [Full Text]  
  • White, C. A., Stow, N. D., Patel, A. H., Hughes, M., Preston, V. G. (2003). Herpes Simplex Virus Type 1 Portal Protein UL6 Interacts with the Putative Terminase Subunits UL15 and UL28. J. Virol. 77: 6351-6358 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»