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 Pomeranz, L. E.
Right arrow Articles by Blaho, J. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pomeranz, L. E.
Right arrow Articles by Blaho, J. A.

 Previous Article  |  Next Article 

Journal of Virology, November 2000, p. 10041-10054, Vol. 74, No. 21
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Assembly of Infectious Herpes Simplex Virus Type 1 Virions in the Absence of Full-Length VP22

Lisa E. Pomeranz and John A. Blaho*

Department of Microbiology, Mount Sinai School of Medicine, New York, New York 10029

Received 9 May 2000/Accepted 27 July 2000

VP22, the 301-amino-acid phosphoprotein product of the herpes simplex virus type 1 (HSV-1) UL49 gene, is incorporated into the tegument during virus assembly. We previously showed that highly modified forms of VP22 are restricted to infected cell nuclei (L. E. Pomeranz and J. A. Blaho, J. Virol. 73:6769-6781, 1999). VP22 packaged into infectious virions appears undermodified, and nuclear- and virion-associated forms are easily differentiated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (J. A. Blaho, C. Mitchell, and B. Roizman, J. Biol. Chem. 269:17401-17410, 1994). As VP22 packaging-associated undermodification is unique among HSV-1 tegument proteins, we sought to determine the role of VP22 during viral replication. We now show the following. (i) VP22 modification occurs in the absence of other viral factors in cell lines which stably express its gene. (ii) RF177, a recombinant HSV-1 strain generated for this study, synthesizes only the amino-terminal 212 amino acids of VP22 (Delta 212). (iii) Delta 212 localizes to the nucleus and incorporates into virions during RF177 infection of Vero cells. Thus, the carboxy-terminal region is not required for nuclear localization of VP22. (iv) RF177 synthesizes the tegument proteins VP13/14, VP16, and VHS (virus host shutoff) and incorporates them into infectious virions as efficiently as wild-type virus. However, (v) the loss of VP22 in RF177 virus particles is compensated for by a redistribution of minor virion components. (vi) Mature RF177 virions are identical to wild-type particles based on electron microscopic analyses. (vii) Single-step growth kinetics of RF177 in Vero cells are essentially identical to those of wild-type virus. (viii) RF177 plaque size is reduced by nearly 40% compared to wild-type virus. Based on these results, we conclude that VP22 is not required for tegument formation, virion assembly/maturation, or productive HSV-1 replication, while the presence of full-length VP22 in the tegument is needed for efficient virus spread in Vero cell monolayers.

* Corresponding author. Mailing address: Department of Microbiology, Mount Sinai School of Medicine, One Gustave L. Levy Place, New York, NY 10029-6574. Phone: (212) 241-7319. Fax: (212) 534-1684. E-mail: john.blaho{at}mssm.edu.

Journal of Virology, November 2000, p. 10041-10054, Vol. 74, No. 21
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Duffy, C., Mbong, E. F., Baines, J. D. (2009). VP22 of Herpes Simplex Virus 1 Promotes Protein Synthesis at Late Times in Infection and Accumulation of a Subset of Viral mRNAs at Early Times in Infection. J. Virol. 83: 1009-1017 [Abstract] [Full Text]  
  • Che, X., Reichelt, M., Sommer, M. H., Rajamani, J., Zerboni, L., Arvin, A. M. (2008). Functions of the ORF9-to-ORF12 Gene Cluster in Varicella-Zoster Virus Replication and in the Pathogenesis of Skin Infection. J. Virol. 82: 5825-5834 [Abstract] [Full Text]  
  • Sciortino, M. T., Taddeo, B., Giuffre-Cuculletto, M., Medici, M. A., Mastino, A., Roizman, B. (2007). Replication-Competent Herpes Simplex Virus 1 Isolates Selected from Cells Transfected with a Bacterial Artificial Chromosome DNA Lacking Only the UL49 Gene Vary with Respect to the Defect in the UL41 Gene Encoding Host Shutoff RNase. J. Virol. 81: 10924-10932 [Abstract] [Full Text]  
  • Che, X., Berarducci, B., Sommer, M., Ruyechan, W. T., Arvin, A. M. (2007). The Ubiquitous Cellular Transcriptional Factor USF Targets the Varicella-Zoster Virus Open Reading Frame 10 Promoter and Determines Virulence in Human Skin Xenografts in SCIDhu Mice In Vivo. J. Virol. 81: 3229-3239 [Abstract] [Full Text]  
  • Duffy, C., LaVail, J. H., Tauscher, A. N., Wills, E. G., Blaho, J. A., Baines, J. D. (2006). Characterization of a UL49-Null Mutant: VP22 of Herpes Simplex Virus Type 1 Facilitates Viral Spread in Cultured Cells and the Mouse Cornea.. J. Virol. 80: 8664-8675 [Abstract] [Full Text]  
  • Hafezi, W., Bernard, E., Cook, R., Elliott, G. (2005). Herpes Simplex Virus Tegument Protein VP22 Contains an Internal VP16 Interaction Domain and a C-Terminal Domain That Are Both Required for VP22 Assembly into the Virus Particle. J. Virol. 79: 13082-13093 [Abstract] [Full Text]  
  • Mouzakitis, G., McLauchlan, J., Barreca, C., Kueltzo, L., O'Hare, P. (2005). Characterization of VP22 in Herpes Simplex Virus-Infected Cells. J. Virol. 79: 12185-12198 [Abstract] [Full Text]  
  • Vittone, V., Diefenbach, E., Triffett, D., Douglas, M. W., Cunningham, A. L., Diefenbach, R. J. (2005). Determination of Interactions between Tegument Proteins of Herpes Simplex Virus Type 1. J. Virol. 79: 9566-9571 [Abstract] [Full Text]  
  • Nozawa, N., Kawaguchi, Y., Tanaka, M., Kato, A., Kato, A., Kimura, H., Nishiyama, Y. (2005). Herpes Simplex Virus Type 1 UL51 Protein Is Involved in Maturation and Egress of Virus Particles. J. Virol. 79: 6947-6956 [Abstract] [Full Text]  
  • Zhu, J., Qiu, Z., Wiese, C., Ishii, Y., Friedrichsen, J., Rajashekara, G., Splitter, G. A. (2005). Nuclear and Mitochondrial Localization Signals Overlap within Bovine Herpesvirus 1 Tegument Protein VP22. J. Biol. Chem. 280: 16038-16044 [Abstract] [Full Text]  
  • Yedowitz, J. C., Kotsakis, A., Schlegel, E. F. M., Blaho, J. A. (2005). Nuclear Localizations of the Herpes Simplex Virus Type 1 Tegument Proteins VP13/14, vhs, and VP16 Precede VP22-Dependent Microtubule Reorganization and VP22 Nuclear Import. J. Virol. 79: 4730-4743 [Abstract] [Full Text]  
  • Fuchs, W., Granzow, H., Mettenleiter, T. C. (2003). A Pseudorabies Virus Recombinant Simultaneously Lacking the Major Tegument Proteins Encoded by the UL46, UL47, UL48, and UL49 Genes Is Viable in Cultured Cells. J. Virol. 77: 12891-12900 [Abstract] [Full Text]  
  • Farnsworth, A., Goldsmith, K., Johnson, D. C. (2003). Herpes Simplex Virus Glycoproteins gD and gE/gI Serve Essential but Redundant Functions during Acquisition of the Virion Envelope in the Cytoplasm. J. Virol. 77: 8481-8494 [Abstract] [Full Text]  
  • Goodkin, M. L., Ting, A. T., Blaho, J. A. (2003). NF-{kappa}B Is Required for Apoptosis Prevention during Herpes Simplex Virus Type 1 Infection. J. Virol. 77: 7261-7280 [Abstract] [Full Text]  
  • Brignati, M. J., Loomis, J. S., Wills, J. W., Courtney, R. J. (2003). Membrane Association of VP22, a Herpes Simplex Virus Type 1 Tegument Protein. J. Virol. 77: 4888-4898 [Abstract] [Full Text]  
  • Lyman, M. G., Demmin, G. L., Banfield, B. W. (2002). The Attenuated Pseudorabies Virus Strain Bartha Fails To Package the Tegument Proteins Us3 and VP22. J. Virol. 77: 1403-1414 [Abstract] [Full Text]  
  • Kopp, M., Klupp, B. G., Granzow, H., Fuchs, W., Mettenleiter, T. C. (2002). Identification and Characterization of the Pseudorabies Virus Tegument Proteins UL46 and UL47: Role for UL47 in Virion Morphogenesis in the Cytoplasm. J. Virol. 76: 8820-8833 [Abstract] [Full Text]  
  • Fuchs, W., Klupp, B. G., Granzow, H., Hengartner, C., Brack, A., Mundt, A., Enquist, L. W., Mettenleiter, T. C. (2002). Physical Interaction between Envelope Glycoproteins E and M of Pseudorabies Virus and the Major Tegument Protein UL49. J. Virol. 76: 8208-8217 [Abstract] [Full Text]  
  • Fuchs, W., Granzow, H., Klupp, B. G., Kopp, M., Mettenleiter, T. C. (2002). The UL48 Tegument Protein of Pseudorabies Virus Is Critical for Intracytoplasmic Assembly of Infectious Virions. J. Virol. 76: 6729-6742 [Abstract] [Full Text]  
  • van Leeuwen, H., Elliott, G., O'Hare, P. (2002). Evidence of a Role for Nonmuscle Myosin II in Herpes Simplex Virus Type 1 Egress. J. Virol. 76: 3471-3481 [Abstract] [Full Text]  
  • Mettenleiter, T. C. (2002). Herpesvirus Assembly and Egress. J. Virol. 76: 1537-1547 [Full Text]  
  • Dorange, F., Tischer, B. K., Vautherot, J.-F., Osterrieder, N. (2002). Characterization of Marek's Disease Virus Serotype 1 (MDV-1) Deletion Mutants That Lack UL46 to UL49 Genes: MDV-1 UL49, Encoding VP22, Is Indispensable for Virus Growth. J. Virol. 76: 1959-1970 [Abstract] [Full Text]  
  • del Rio, T., Werner, H. C., Enquist, L. W. (2002). The Pseudorabies Virus VP22 Homologue (UL49) Is Dispensable for Virus Growth In Vitro and Has No Effect on Virulence and Neuronal Spread in Rodents. J. Virol. 76: 774-782 [Abstract] [Full Text]  
  • Geiss, B. J., Tavis, J. E., Metzger, L. M., Leib, D. A., Morrison, L. A. (2001). Temporal Regulation of Herpes Simplex Virus Type 2 VP22 Expression and Phosphorylation. J. Virol. 75: 10721-10729 [Abstract] [Full Text]  
  • Ren, X., Harms, J. S., Splitter, G. A. (2001). Tyrosine Phosphorylation of Bovine Herpesvirus 1 Tegument Protein VP22 Correlates with the Incorporation of VP22 into Virions. J. Virol. 75: 9010-9017 [Abstract] [Full Text]  
  • Kotsakis, A., Pomeranz, L. E., Blouin, A., Blaho, J. A. (2001). Microtubule Reorganization during Herpes Simplex Virus Type 1 Infection Facilitates the Nuclear Localization of VP22, a Major Virion Tegument Protein. J. Virol. 75: 8697-8711 [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»