This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Ellison, K. S. Articles by Smiley, J. R. Search for Related Content PubMed PubMed Citation Articles by Ellison, K. S. Articles by Smiley, J. R.

 Previous Article  |  Next Article 

Journal of Virology, April 2005, p. 4120-4131, Vol. 79, No. 7
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.7.4120-4131.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Control of VP16 Translation by the Herpes Simplex Virus Type 1 Immediate-Early Protein ICP27

Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta, Canada

Received 30 September 2004/ Accepted 18 November 2004

Herpes simplex virus (HSV) ICP27 is an essential and multifunctional regulator of gene expression that modulates the synthesis and maturation of viral and cellular mRNAs. Processes that are affected by ICP27 include transcription, pre-mRNA splicing, polyadenylation, and nuclear RNA export. We have examined how ICP27 influences the expression of the essential HSV tegument protein and transactivator of immediate-early gene expression VP16. We monitored the effects of ICP27 on the levels, nuclear export, and polyribosomal association of VP16 mRNA and on the amount and stability of VP16 protein. Deletion of ICP27 reduced the levels of VP16 mRNA without altering its nuclear export or the stability of the encoded protein. However, the translational yield of the VP16 mRNA produced in the absence of ICP27 was reduced 9- to 80-fold relative to that for wild-type infection, suggesting a defect in translation. In the absence of ICP27, the majority of cytoplasmic VP16 mRNA was not associated with actively translating polyribosomes but instead cosedimented with 40S ribosomal subunits, indicating that the translational defect is likely at the level of initiation. These effects were mRNA specific, as polyribosomal analysis of two cellular transcripts (glyceraldehyde-3-phosphate dehydrogenase and ß-actin) and two early HSV transcripts (thymidine kinase and ICP8) indicated that ICP27 is not required for efficient translation of these mRNAs. Thus, we have uncovered a novel mRNA-specific translational regulatory function of ICP27.

This article has been cited by other articles:

• Sedlackova, L., Perkins, K. D., Lengyel, J., Strain, A. K., van Santen, V. L., Rice, S. A. (2008). Herpes Simplex Virus Type 1 ICP27 Regulates Expression of a Variant, Secreted Form of Glycoprotein C by an Intron Retention Mechanism. J. Virol. 82: 7443-7455 [Abstract] [Full Text]  
• Fontaine-Rodriguez, E. C., Knipe, D. M. (2008). Herpes Simplex Virus ICP27 Increases Translation of a Subset of Viral Late mRNAs. J. Virol. 82: 3538-3545 [Abstract] [Full Text]  
• Bryant, K. F., Coen, D. M. (2008). Inhibition of Translation by a Short Element in the 5' Leader of the Herpes Simplex Virus 1 DNA Polymerase Transcript. J. Virol. 82: 77-85 [Abstract] [Full Text]  
• Corcoran, J. A., Hsu, W.-L., Smiley, J. R. (2006). Herpes Simplex Virus ICP27 Is Required for Virus-Induced Stabilization of the ARE-Containing IEX-1 mRNA Encoded by the Human IER3 Gene. J. Virol. 80: 9720-9729 [Abstract] [Full Text]  
• Sanchez, V., Spector, D. H. (2006). Cyclin-Dependent Kinase Activity Is Required for Efficient Expression and Posttranslational Modification of Human Cytomegalovirus Proteins and for Production of Extracellular Particles.. J. Virol. 80: 5886-5896 [Abstract] [Full Text]  
• Dai-Ju, J. Q., Li, L., Johnson, L. A., Sandri-Goldin, R. M. (2006). ICP27 Interacts with the C-Terminal Domain of RNA Polymerase II and Facilitates Its Recruitment to Herpes Simplex Virus 1 Transcription Sites, Where It Undergoes Proteasomal Degradation during Infection.. J. Virol. 80: 3567-3581 [Abstract] [Full Text]  
• Larralde, O., Smith, R. W. P., Wilkie, G. S., Malik, P., Gray, N. K., Clements, J. B. (2006). Direct Stimulation of Translation by the Multifunctional Herpesvirus ICP27 Protein. J. Virol. 80: 1588-1591 [Abstract] [Full Text]  
• Schwartz, J. A., Brittle, E. E., Reynolds, A. E., Enquist, L. W., Silverstein, S. J. (2006). UL54-Null Pseudorabies Virus Is Attenuated in Mice but Productively Infects Cells in Culture. J. Virol. 80: 769-784 [Abstract] [Full Text]