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Journal of Virology, June 2005, p. 7431-7437, Vol. 79, No. 12
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.12.7431-7437.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

The C Terminus of the B5 Receptor for Herpes Simplex Virus Contains a Functional Region Important for Infection

Pilar Perez-Romero and A. Oveta Fuller*

Department of Microbiology and Immunology, 6736 Medical Sciences II, School of Medicine, University of Michigan, Ann Arbor, Michigan 48109-0620

Received 10 May 2004/ Accepted 14 January 2005

The expression of a previously uncharacterized human hfl-B5 cDNA confers susceptibility for herpes simplex virus (HSV) to porcine cells and fulfills criteria as an HSV entry receptor (A. Perez, Q.-X. Li, P. Perez-Romero, G. DeLassus, S. R. Lopez, S. Sutter, N. McLaren, and A. Oveta Fuller, J. Virol. 79:7419-7430, 2005). Heptad repeats found in the B5 C terminus are predicted to form an {alpha}-helix for coiled coil structure. We used mutagenesis and synthetic peptides with wild-type and mutant sequences to examine the function of the heptad repeat motif in HSV binding and entry into porcine cells that express B5 and for infection of naturally susceptible human HEp-2 cells. B5 with point mutations predicted to disrupt the putative C-terminal coiled coil failed to mediate HSV binding and entry into porcine cells. Synthetic peptides that contain the single amino acid changes lose the blocking activity of HSV entry. We concluded that the C terminus of B5 contains a functional region that is important for the B5 receptor to mediate events in HSV entry. Structural evidence that this functional region forms coiled coil structures is under investigation. Blocking of HSV interaction with the C-terminal region of the B5 receptor is a new potential target site to intervene in the virus infection of human cells.

* Corresponding author. Mailing address: 6736 Medical Sciences II, University of Michigan, Ann Arbor, MI 48109-0620. Phone: (734) 647-3830. Fax: (734) 764-3562. E-mail: fullerao{at}umich.edu.

Journal of Virology, June 2005, p. 7431-7437, Vol. 79, No. 12
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.12.7431-7437.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Akkarawongsa, R., Pocaro, N. E., Case, G., Kolb, A. W., Brandt, C. R. (2009). Multiple Peptides Homologous to Herpes Simplex Virus Type 1 Glycoprotein B Inhibit Viral Infection. Antimicrob. Agents Chemother. 53: 987-996 [Abstract] [Full Text]  
  • Jenssen, H., Hamill, P., Hancock, R. E. W. (2006). Peptide Antimicrobial Agents. Clin. Microbiol. Rev. 19: 491-511 [Abstract] [Full Text]  
  • Perez, A., Li, Q.-X., Perez-Romero, P., DeLassus, G., Lopez, S. R., Sutter, S., McLaren, N., Fuller, A. O. (2005). A New Class of Receptor for Herpes Simplex Virus Has Heptad Repeat Motifs That Are Common to Membrane Fusion Proteins. J. Virol. 79: 7419-7430 [Abstract] [Full Text]  


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