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 Zeilfelder, U.
Right arrow Articles by Bosch, V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zeilfelder, U.
Right arrow Articles by Bosch, V.

 Previous Article

Journal of Virology, January 2001, p. 548-555, Vol. 75, No. 1
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.1.548-555.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Properties of Wild-Type, C-Terminally Truncated, and Chimeric Maedi-Visna Virus Glycoprotein and Putative Pseudotyping of Retroviral Vector Particles

Udo Zeilfelder and Valerie Bosch*

Forschungsschwerpunkt Angewandte Tumorvirologie, Deutsches Krebsforschungszentrum, D-69120 Heidelberg, Germany

Received 7 February 2000/Accepted 6 October 2000

We have characterized the properties of the maedi-visna virus (MVV) glycoprotein, which has a long cytoplasmic C-terminal domain, and of a panel of C-terminally truncated and C-terminally chimeric MVV-Env constructs. Cells expressing wild-type MVV glycoprotein form syncytia with target cells from many different species and tissues, demonstrating that the MVV-Env cellular receptor is widely distributed. Similar to the situation with other lentiviral glycoproteins, truncation of the C-terminal domain of MVV-Env significantly increases its membrane fusion capacity. However, despite their presence in a fusogenic form at the cell surface, neither the wild-type nor any of the C-terminally modified MVV-Env constructs, these latter lacking sterically inhibitory C termini, were able to successfully pseudotype murine leukemia virus- or human immunodeficiency virus-derived vector particles.

* Corresponding author. Mailing address: Forschungsschwerpunkt Angewandte Tumorvirologie, F0200, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 242, D-69120 Heidelberg, Germany. Phone: (49)-6221-424948. Fax: (49)-6221-424932. E-mail: v.bosch{at}dkfz-heidelberg.de.

Journal of Virology, January 2001, p. 548-555, Vol. 75, No. 1
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.1.548-555.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Murakami, T., Ablan, S., Freed, E. O., Tanaka, Y. (2004). Regulation of Human Immunodeficiency Virus Type 1 Env-Mediated Membrane Fusion by Viral Protease Activity. J. Virol. 78: 1026-1031 [Abstract] [Full Text]  
  • Sinn, P. L., Hickey, M. A., Staber, P. D., Dylla, D. E., Jeffers, S. A., Davidson, B. L., Sanders, D. A., McCray, P. B. Jr. (2003). Lentivirus Vectors Pseudotyped with Filoviral Envelope Glycoproteins Transduce Airway Epithelia from the Apical Surface Independently of Folate Receptor Alpha. J. Virol. 77: 5902-5910 [Abstract] [Full Text]  
  • Edwards, T. G., Wyss, S., Reeves, J. D., Zolla-Pazner, S., Hoxie, J. A., Doms, R. W., Baribaud, F. (2002). Truncation of the Cytoplasmic Domain Induces Exposure of Conserved Regions in the Ectodomain of Human Immunodeficiency Virus Type 1 Envelope Protein. J. Virol. 76: 2683-2691 [Abstract] [Full Text]  
  • Bruett, L., Clements, J. E. (2001). Functional Murine Leukemia Virus Vectors Pseudotyped with the Visna Virus Envelope Show Expanded Visna Virus Cell Tropism. J. Virol. 75: 11464-11473 [Abstract] [Full Text]  
  • Hotzel, I., Cheevers, W. P. (2001). Host Range of Small-Ruminant Lentivirus Cytopathic Variants Determined with a Selectable Caprine Arthritis- Encephalitis Virus Pseudotype System. J. Virol. 75: 7384-7391 [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»