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Journal of Virology, July 2008, p. 6778-6781, Vol. 82, No. 13
0022-538X/08/$08.00+0     doi:10.1128/JVI.00473-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Amino Acids 143 to 150 of the Herpes Simplex Virus Type 1 Scaffold Protein Are Required for the Formation of Portal-Containing Capsids{triangledown}

Jamie B. Huffman,1 William W. Newcomb,2 Jay C. Brown,2 and Fred L. Homa1*

Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261,1 Department of Microbiology and Cancer Center, University of Virginia Health System, Charlottesville, Virginia 229082

Received 4 March 2008/ Accepted 7 April 2008

The herpes simplex virus type 1 (HSV-1) portal is composed of a dodecamer of UL6 protein molecules whose incorporation into the capsid is mediated by interaction with the HSV-1 UL26.5 scaffold protein. Previous results with an in vitro capsid assembly assay demonstrated that nine amino acids (amino acids 143 to 151) of the UL26.5 protein are required for its interaction with UL6 and for incorporation of the portal complex into capsids. In the present study an HSV-1 mutant, bvFH411, was isolated and contained a deletion that removed the codons for UL26.5 amino acids 143 to 150. The mutant virus failed to produce infectious virus in noncomplementing cells, and only B capsids that contained only minor amounts of portal protein were made. These data corroborate our previous in vitro studies and demonstrate that amino acids 143 to 150 of UL26.5 are required for the formation of portal-containing HSV-1 capsids.

* Corresponding author. Mailing address: Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, W1256 Biomedical Science Tower, Pittsburgh, PA 15261. Phone: (412) 648-8788. Fax: (412) 624-1401. E-mail: flhoma{at}pitt.edu

{triangledown} Published ahead of print on 16 April 2008.

Journal of Virology, July 2008, p. 6778-6781, Vol. 82, No. 13
0022-538X/08/$08.00+0     doi:10.1128/JVI.00473-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Yang, K., Baines, J. D. (2009). Tryptophan Residues in the Portal Protein of Herpes Simplex Virus 1 Critical to the Interaction with Scaffold Proteins and Incorporation of the Portal into Capsids. J. Virol. 83: 11726-11733 [Abstract] [Full Text]  
  • Yang, K., Baines, J. D. (2009). Proline and Tyrosine Residues in Scaffold Proteins of Herpes Simplex Virus 1 Critical to the Interaction with Portal Protein and Its Incorporation into Capsids. J. Virol. 83: 8076-8081 [Abstract] [Full Text]  
  • Yang, K., Wills, E., Baines, J. D. (2009). The Putative Leucine Zipper of the UL6-Encoded Portal Protein of Herpes Simplex Virus 1 Is Necessary for Interaction with pUL15 and pUL28 and Their Association with Capsids. J. Virol. 83: 4557-4564 [Abstract] [Full Text]  


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