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 Ch'ng, T. H.
Right arrow Articles by Enquist, L. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ch'ng, T. H.
Right arrow Articles by Enquist, L. W.

 Previous Article  |  Next Article 

Journal of Virology, July 2005, p. 8835-8846, Vol. 79, No. 14
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.14.8835-8846.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Efficient Axonal Localization of Alphaherpesvirus Structural Proteins in Cultured Sympathetic Neurons Requires Viral Glycoprotein E

T. H. Ch'ng and L. W. Enquist*

Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544

Received 21 February 2005/ Accepted 30 March 2005

Pseudorabies virus (PRV) glycoprotein E (gE) is a type I viral membrane protein that facilitates the anterograde spread of viral infection from the peripheral nervous system to the brain. In animal models, a gE-null mutant infection spreads inefficiently from presynaptic neurons to postsynaptic neurons (anterograde spread of infection). However, the retrograde spread of infection from post- to presynaptic neurons remains unaffected. Here we show that gE is required for wild-type localization of viral structural proteins in axons of infected neurons. During a gE-null PRV infection, a subset of viral glycoproteins, capsids, and tegument proteins enter and localize to the axon inefficiently. This defect is most obvious in the distal axon and growth cones. However, axonal entry and localization of other viral membrane proteins and endogenous cellular proteins remains unaffected. Neurons infected with gE-null mutants produce wild-type levels of viral structural proteins and infectious virions in the cell body. Our results indicate that reduced axonal targeting of viral structural proteins is a compelling explanation for the lack of anterograde spread in neural circuits following infection by a gE-null mutant.

* Corresponding author. Mailing address: Dept. of Molecular Biology, Princeton University, Princeton, NJ 08544. Phone: (609) 258-2415. Fax: (609) 258-1035. E-mail: lenquist{at}molbio.princeton.edu.

Journal of Virology, July 2005, p. 8835-8846, Vol. 79, No. 14
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.14.8835-8846.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Curanovic, D., Enquist, L. W. (2009). Virion-Incorporated Glycoprotein B Mediates Transneuronal Spread of Pseudorabies Virus. J. Virol. 83: 7796-7804 [Abstract] [Full Text]  
  • Lyman, M. G., Kemp, C. D., Taylor, M. P., Enquist, L. W. (2009). Comparison of the Pseudorabies Virus Us9 Protein with Homologs from Other Veterinary and Human Alphaherpesviruses. J. Virol. 83: 6978-6986 [Abstract] [Full Text]  
  • Snyder, A., Polcicova, K., Johnson, D. C. (2008). Herpes Simplex Virus gE/gI and US9 Proteins Promote Transport of both Capsids and Virion Glycoproteins in Neuronal Axons. J. Virol. 82: 10613-10624 [Abstract] [Full Text]  
  • Brittle, E. E., Wang, F., Lubinski, J. M., Bunte, R. M., Friedman, H. M. (2008). A Replication-Competent, Neuronal Spread-Defective, Live Attenuated Herpes Simplex Virus Type 1 Vaccine. J. Virol. 82: 8431-8441 [Abstract] [Full Text]  
  • Shanda, S. K., Wilson, D. W. (2008). UL36p Is Required for Efficient Transport of Membrane-Associated Herpes Simplex Virus Type 1 along Microtubules. J. Virol. 82: 7388-7394 [Abstract] [Full Text]  
  • Lyman, M. G., Feierbach, B., Curanovic, D., Bisher, M., Enquist, L. W. (2007). Pseudorabies Virus Us9 Directs Axonal Sorting of Viral Capsids. J. Virol. 81: 11363-11371 [Abstract] [Full Text]  
  • Snyder, A., Bruun, B., Browne, H. M., Johnson, D. C. (2007). A Herpes Simplex Virus gD-YFP Fusion Glycoprotein Is Transported Separately from Viral Capsids in Neuronal Axons. J. Virol. 81: 8337-8340 [Abstract] [Full Text]  
  • Snyder, A., Wisner, T. W., Johnson, D. C. (2006). Herpes Simplex Virus Capsids Are Transported in Neuronal Axons without an Envelope Containing the Viral Glycoproteins. J. Virol. 80: 11165-11177 [Abstract] [Full Text]  
  • Olsen, L. M., Ch'ng, T. H., Card, J. P., Enquist, L. W. (2006). Role of Pseudorabies Virus Us3 Protein Kinase during Neuronal Infection.. J. Virol. 80: 6387-6398 [Abstract] [Full Text]  
  • Chowdhury, S. I., Mahmood, S., Simon, J., Al-Mubarak, A., Zhou, Y. (2006). The Us9 Gene of Bovine Herpesvirus 1 (BHV-1) Effectively Complements a Us9-Null Strain of BHV-5 for Anterograde Transport, Neurovirulence, and Neuroinvasiveness in a Rabbit Model. J. Virol. 80: 4396-4405 [Abstract] [Full Text]  
  • Saksena, M. M., Wakisaka, H., Tijono, B., Boadle, R. A., Rixon, F., Takahashi, H., Cunningham, A. L. (2006). Herpes simplex virus type 1 accumulation, envelopment, and exit in growth cones and varicosities in mid-distal regions of axons.. J. Virol. 80: 3592-3606 [Abstract] [Full Text]  
  • Wang, F., Tang, W., McGraw, H. M., Bennett, J., Enquist, L. W., Friedman, H. M. (2005). Herpes Simplex Virus Type 1 Glycoprotein E Is Required for Axonal Localization of Capsid, Tegument, and Membrane Glycoproteins. J. Virol. 79: 13362-13372 [Abstract] [Full Text]  
  • Pomeranz, L. E., Reynolds, A. E., Hengartner, C. J. (2005). Molecular Biology of Pseudorabies Virus: Impact on Neurovirology and Veterinary Medicine. Microbiol. Mol. Biol. Rev. 69: 462-500 [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»