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 Saad, A.
Right arrow Articles by Rixon, F. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Saad, A.
Right arrow Articles by Rixon, F. J.

 Previous Article  |  Next Article 

Journal of Virology, August 1999, p. 6821-6830, Vol. 73, No. 8
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Roles of Triplex and Scaffolding Proteins in Herpes Simplex Virus Type 1 Capsid Formation Suggested by Structures of Recombinant Particles

Ali Saad,1 Z. Hong Zhou,2 Joanita Jakana,1 Wah Chiu,1,* and Frazer J. Rixon3

Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine,1 and Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School,2 Houston, Texas 77030, and Medical Research Council Virology Unit, Institute of Virology, Glasgow G11 5JR, Scotland3

Received 9 February 1999/Accepted 16 April 1999

Typical herpes simplex virus (HSV) capsids contain seven proteins that form a T=16 icosahedron of 1,250-Å diameter. Infection of cells with recombinant baculoviruses expressing two of these proteins, VP5 (which forms the pentons and hexons in typical HSV capsids) and VP19C (a component of the triplexes that connect adjacent capsomeres), results in the formation of spherical particles of 880-Å diameter. Electron cryomicroscopy and computer reconstruction revealed that these particles possess a T=7 icosahedral symmetry, having 12 pentons and 60 hexons. Among the characteristic structural features of the particle are the skewed appearance of the hexons and the presence of intercapsomeric mass densities connecting the middle domain of one hexon subunit to the lower domain of a subunit in the adjacent hexon. We interpret these connecting masses as being formed by VP19C. Comparison of the connecting masses with the triplexes, which occupy equivalent positions in the T=16 capsid, reveals the probable locations of the single VP19C and two VP23 molecules that make up the triplex. Their arrangement suggests that the two triplex proteins have different roles in controlling intercapsomeric interactions and capsid stability. The nature of these particles and of other aberrant forms made in the absence of scaffold demonstrates the conformational adaptability of the capsid proteins and illustrates how VP23 and the scaffolding protein modulate the nature of the VP5-VP19C network to ensure assembly of the functional T=16 capsid.

* Corresponding author. Mailing address: Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030. Phone: (713) 798-6985. Fax: (713) 796-9438. E-mail: wah{at}bcm.tmc.edu.

Journal of Virology, August 1999, p. 6821-6830, Vol. 73, No. 8
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Liashkovich, I., Hafezi, W., Kuhn, J. E., Oberleithner, H., Kramer, A., Shahin, V. (2008). Exceptional mechanical and structural stability of HSV-1 unveiled with fluid atomic force microscopy. J. Cell Sci. 121: 2287-2292 [Abstract] [Full Text]  
  • Hernandez, R., Paredes, A., Brown, D. T. (2008). Sindbis Virus Conformational Changes Induced by a Neutralizing Anti-E1 Monoclonal Antibody. J. Virol. 82: 5750-5760 [Abstract] [Full Text]  
  • de Oliveira, A. P., Glauser, D. L., Laimbacher, A. S., Strasser, R., Schraner, E. M., Wild, P., Ziegler, U., Breakefield, X. O., Ackermann, M., Fraefel, C. (2008). Live Visualization of Herpes Simplex Virus Type 1 Compartment Dynamics. J. Virol. 82: 4974-4990 [Abstract] [Full Text]  
  • Adamson, W. E., McNab, D., Preston, V. G., Rixon, F. J. (2006). Mutational Analysis of the Herpes Simplex Virus Triplex Protein VP19C. J. Virol. 80: 1537-1548 [Abstract] [Full Text]  
  • Okoye, M. E., Sexton, G. L., Huang, E., McCaffery, J. M., Desai, P. (2006). Functional Analysis of the Triplex Proteins (VP19C and VP23) of Herpes Simplex Virus Type 1. J. Virol. 80: 929-940 [Abstract] [Full Text]  
  • Shahin, V., Hafezi, W., Oberleithner, H., Ludwig, Y., Windoffer, B., Schillers, H., Kuhn, J. E. (2006). The genome of HSV-1 translocates through the nuclear pore as a condensed rod-like structure. J. Cell Sci. 119: 23-30 [Abstract] [Full Text]  
  • Gilcrease, E. B., Winn-Stapley, D. A., Hewitt, F. C., Joss, L., Casjens, S. R. (2005). Nucleotide Sequence of the Head Assembly Gene Cluster of Bacteriophage L and Decoration Protein Characterization. J. Bacteriol. 187: 2050-2057 [Abstract] [Full Text]  
  • Yu, X.-K., O'Connor, C. M., Atanasov, I., Damania, B., Kedes, D. H., Zhou, Z. H. (2003). Three-Dimensional Structures of the A, B, and C Capsids of Rhesus Monkey Rhadinovirus: Insights into Gammaherpesvirus Capsid Assembly, Maturation, and DNA Packaging. J. Virol. 77: 13182-13193 [Abstract] [Full Text]  
  • McClelland, D. A., Aitken, J. D., Bhella, D., McNab, D., Mitchell, J., Kelly, S. M., Price, N. C., Rixon, F. J. (2002). pH Reduction as a Trigger for Dissociation of Herpes Simplex Virus Type 1 Scaffolds. J. Virol. 76: 7407-7417 [Abstract] [Full Text]  
  • Preston, V. G., McDougall, I. M. (2002). Regions of the Herpes Simplex Virus Scaffolding Protein That Are Important for Intermolecular Self-Interaction. J. Virol. 76: 673-687 [Abstract] [Full Text]  
  • Chen, D.-H., Jakana, J., McNab, D., Mitchell, J., Zhou, Z. H., Dougherty, M., Chiu, W., Rixon, F. J. (2001). The Pattern of Tegument-Capsid Interaction in the Herpes Simplex Virus Type 1 Virion Is Not Influenced by the Small Hexon-Associated Protein VP26. J. Virol. 75: 11863-11867 [Abstract] [Full Text]  
  • Paredes, A., Alwell-Warda, K., Weaver, S. C., Chiu, W., Watowich, S. J. (2001). Venezuelan Equine Encephalomyelitis Virus Structure and Its Divergence from Old World Alphaviruses. J. Virol. 75: 9532-9537 [Abstract] [Full Text]  
  • Trus, B. L., Heymann, J. B., Nealon, K., Cheng, N., Newcomb, W. W., Brown, J. C., Kedes, D. H., Steven, A. C. (2001). Capsid Structure of Kaposi's Sarcoma-Associated Herpesvirus, a Gammaherpesvirus, Compared to Those of an Alphaherpesvirus, Herpes Simplex Virus Type 1, and a Betaherpesvirus, Cytomegalovirus. J. Virol. 75: 2879-2890 [Abstract] [Full Text]  
  • Wu, L., Lo, P., Yu, X., Stoops, J. K., Forghani, B., Zhou, Z. H. (2000). Three-Dimensional Structure of the Human Herpesvirus 8 Capsid. J. Virol. 74: 9646-9654 [Abstract] [Full Text]  
  • Sheaffer, A. K., Newcomb, W. W., Brown, J. C., Gao, M., Weller, S. K., Tenney, D. J. (2000). Evidence for Controlled Incorporation of Herpes Simplex Virus Type 1 UL26 Protease into Capsids. J. Virol. 74: 6838-6848 [Abstract] [Full Text]  
  • Zhou, Z. H., Dougherty, M., Jakana, J., He, J., Rixon, F. J., Chiu, W. (2000). Seeing the Herpesvirus Capsid at 8.5 Å . Science 288: 877-880 [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»