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 Gonzalez-Dunia, D.
Right arrow Articles by de la Torre, J. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gonzalez-Dunia, D.
Right arrow Articles by de la Torre, J. C.

 Previous Article  |  Next Article 

J Virol, January 1998, p. 783-788, Vol. 72, No. 1
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Mechanism of Borna Disease Virus Entry into Cellsdagger

Daniel Gonzalez-Dunia, Beatrice Cubitt, and Juan Carlos de la Torre*

Division of Virology, Department of Neuropharmacology, The Scripps Research Institute, La Jolla, California 92037

Received 6 August 1997/Accepted 8 October 1997

We have investigated the entry pathway of Borna disease virus (BDV). Virus entry was assessed by detecting early viral replication and transcription. Lysosomotropic agents (ammonium chloride, chloroquine, and amantadine), as well as energy depletion, prevented BDV infection, indicating that BDV enters host cells by endocytosis and requires an acidic intracellular compartment to allow membrane fusion and initiate infection. Consistent with this hypothesis, we observed that BDV-infected cells form extensive syncytia upon low-pH treatment. Entry of enveloped viruses into animal cells usually requires the membrane-fusing activity of viral surface glycoproteins (GPs). BDV GP is expressed as two products of 84 and 43 kDa (GP-84 and GP-43, respectively). We show here that only GP-43 is present at the surface of BDV-infected cells and therefore is likely the viral polypeptide responsible for triggering fusion events. We also present evidence that GP-43, which corresponds to the C terminus of GP-84, is generated by cleavage of GP-84 by the cellular protease furin. Hence, we propose that BDV GP-84 is involved in attachment to the cell surface receptor whereas its furin-cleaved product, GP-43, is involved in pH-dependent fusion after internalization of the virion by endocytosis.

* Corresponding author. Mailing address: Division of Virology, Department of Neuropharmacology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037. Phone: (619) 784-9462. Fax: (619) 784-9981. E-mail: juanct{at}scripps.edu.

dagger Publication 11049-NP from the Scripps Research Institute.




This article has been cited by other articles:

  • Clemente, R., de Parseval, A., Perez, M., de la Torre, J. C. (2009). Borna Disease Virus Requires Cholesterol in both Cellular Membrane and Viral Envelope for Efficient Cell Entry. J. Virol. 83: 2655-2662 [Abstract] [Full Text]  
  • Perez, M., Clemente, R., Robison, C. S., Jeetendra, E., Jayakar, H. R., Whitt, M. A., de la Torre, J. C. (2007). Generation and Characterization of a Recombinant Vesicular Stomatitis Virus Expressing the Glycoprotein of Borna Disease Virus. J. Virol. 81: 5527-5536 [Abstract] [Full Text]  
  • Clemente, R., de la Torre, J. C. (2007). Cell-to-Cell Spread of Borna Disease Virus Proceeds in the Absence of the Virus Primary Receptor and Furin-Mediated Processing of the Virus Surface Glycoprotein. J. Virol. 81: 5968-5977 [Abstract] [Full Text]  
  • Misinzo, G., Meerts, P., Bublot, M., Mast, J., Weingartl, H. M., Nauwynck, H. J. (2005). Binding and entry characteristics of porcine circovirus 2 in cells of the porcine monocytic line 3D4/31. J. Gen. Virol. 86: 2057-2068 [Abstract] [Full Text]  
  • Bajramovic, J. J., Munter, S., Syan, S., Nehrbass, U., Brahic, M., Gonzalez-Dunia, D. (2003). Borna Disease Virus Glycoprotein Is Required for Viral Dissemination in Neurons. J. Virol. 77: 12222-12231 [Abstract] [Full Text]  
  • Geib, T., Sauder, C., Venturelli, S., Hassler, C., Staeheli, P., Schwemmle, M. (2003). Selective Virus Resistance Conferred by Expression of Borna Disease Virus Nucleocapsid Components. J. Virol. 77: 4283-4290 [Abstract] [Full Text]  
  • Vahlenkamp, T. W., Konrath, A., Weber, M., Muller, H. (2002). Persistence of Borna Disease Virus in Naturally Infected Sheep. J. Virol. 76: 9735-9743 [Abstract] [Full Text]  
  • Nishino, Y., Kobasa, D., Rubin, S. A., Pletnikov, M. V., Carbone, K. M. (2002). Enhanced Neurovirulence of Borna Disease Virus Variants Associated with Nucleotide Changes in the Glycoprotein and L Polymerase Genes. J. Virol. 76: 8650-8658 [Abstract] [Full Text]  
  • Perez, M., Watanabe, M., Whitt, M. A., de la Torre, J. C. (2001). N-Terminal Domain of Borna Disease Virus G (p56) Protein Is Sufficient for Virus Receptor Recognition and Cell Entry. J. Virol. 75: 7078-7085 [Abstract] [Full Text]  
  • Planz, O., Pleschka, S., Ludwig, S. (2001). MEK-Specific Inhibitor U0126 Blocks Spread of Borna Disease Virus in Cultured Cells. J. Virol. 75: 4871-4877 [Abstract] [Full Text]  
  • Jordan, I., Briese, T., Averett, D. R., Lipkin, W. I. (1999). Inhibition of Borna Disease Virus Replication by Ribavirin. J. Virol. 73: 7903-7906 [Abstract] [Full Text]  
  • Planz, O., Stitz, L. (1999). Borna Disease Virus Nucleoprotein (p40) Is a Major Target for CD8+-T-Cell-Mediated Immune Response. J. Virol. 73: 1715-1718 [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»