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Journal of Virology, March 2006, p. 2309-2317, Vol. 80, No. 5
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.5.2309-2317.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Structural Characterization of the UL25 DNA-Packaging Protein from Herpes Simplex Virus Type 1

Brian R. Bowman,1,{dagger} Robert L. Welschhans,1 Hariharan Jayaram,1,{ddagger} Nigel D. Stow,2 Valerie G. Preston,2 and Florante A. Quiocho1*

Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030,1 MRC Virology Unit, Institute of Virology, Glasgow G11 5JR, United Kingdom2

Received 25 October 2005/ Accepted 8 December 2005

Herpesviruses replicate their double stranded DNA genomes as high-molecular-weight concatemers which are subsequently cleaved into unit-length genomes by a complex mechanism that is tightly coupled to DNA insertion into a preformed capsid structure, the procapsid. The herpes simplex virus type 1 UL25 protein is incorporated into the capsid during DNA packaging, and previous studies of a null mutant have demonstrated that its function is essential at the late stages of the head-filling process, either to allow packaging to proceed to completion or for retention of the viral genome within the capsid. We have expressed and purified an N-terminally truncated form of the 580-residue UL25 protein and have determined the crystallographic structure of the region corresponding to amino acids 134 to 580 at 2.1-Å resolution. This structure, the first for any herpesvirus protein involved in processing and packaging of viral DNA, reveals a novel fold, a distinctive electrostatic distribution, and a unique "flexible" architecture in which numerous flexible loops emanate from a stable core. Evolutionary trace analysis of UL25 and its homologues in other herpesviruses was used to locate potentially important amino acids on the surface of the protein, leading to the identification of four putative docking regions for protein partners.

* Corresponding author. Mailing address: Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030. Phone: (713) 798-6565. Fax: (713) 798-8516. E-mail: faq{at}bcm.tmc.edu.

{dagger} Present address: Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138.

{ddagger} Present address: Howard Hughes Medical Institute and Department of Biochemistry, Brandeis University, Waltham, MA 02454.

Journal of Virology, March 2006, p. 2309-2317, Vol. 80, No. 5
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.5.2309-2317.2006
Copyright © 2006, 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]  
  • Preston, V. G., Murray, J., Preston, C. M., McDougall, I. M., Stow, N. D. (2008). The UL25 Gene Product of Herpes Simplex Virus Type 1 Is Involved in Uncoating of the Viral Genome. J. Virol. 82: 6654-6666 [Abstract] [Full Text]  
  • Newcomb, W. W., Homa, F. L., Brown, J. C. (2006). Herpes Simplex Virus Capsid Structure: DNA Packaging Protein UL25 Is Located on the External Surface of the Capsid near the Vertices.. J. Virol. 80: 6286-6294 [Abstract] [Full Text]  


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