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 Henriksson, P.
Right arrow Articles by Bosch, V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Henriksson, P.
Right arrow Articles by Bosch, V.

 Previous Article  |  Next Article 

Journal of Virology, November 1999, p. 9294-9302, Vol. 73, No. 11
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Incorporation of Wild-Type and C-Terminally Truncated Human Epidermal Growth Factor Receptor into Human Immunodeficiency Virus-Like Particles: Insight into the Processes Governing Glycoprotein Incorporation into Retroviral Particles

Peter Henriksson, Tanya Pfeiffer, Hanswalter Zentgraf, Alexandra Alke, and Valerie Bosch*

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

Received 8 March 1999/Accepted 26 July 1999

Previous results have indicated that incorporation of surface glycoprotein into retroviral particles is not a specific process and that many heterologous viral and cellular glycoproteins can be incorporated as long as they do not have long cytoplasmic C-terminal regions which were presumed to be sterically inhibitory. In this study, this concept has been directly examined by analyzing the incorporation of the wild-type human epidermal growth factor receptor (Wt-EGFR) and of a C-terminally truncated mutant of Wt-EGFR (Tr-EGFR) into human immunodeficiency virus (HIV)-like particles. Incorporation was directly analyzed at the protein level and by immunogold labelling of enriched HIV-like particles. In agreement with the above concept, Tr-EGFR, with only 7 C-terminal amino acids (aa), was efficiently incorporated into HIV-like particles. Incorporation of the Wt-EGFR species, with 542 C-terminal cytoplasmic aa, was reduced by a factor of about 5 in comparison to that of the Tr-EGFR species. However, the Wt-EGFR species was still very significantly present in the HIV-like particles. A series of control experiments verified that this represents genuine incorporation of Wt-EGFR into the membrane of HIV-like particles. These observations allow further speculation as to the processes governing glycoprotein incorporation into retroviral particles and indicate that the internal virus structure of HIV (in particular the matrix layer [MA]) can accommodate much larger heterologous cytoplasmic domains in incorporated glycoproteins than previously assumed.

* Corresponding author. Mailing address: Forschungsschwerpunkt Angewandte Tumorvirologie, F0200, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 242, D-69120 Heidelberg, Germany. Phone: (0)6221-424948. Fax: (0)6221-424932. E-mail: v.bosch{at}dkfz-heidelberg.de.

Journal of Virology, November 1999, p. 9294-9302, Vol. 73, No. 11
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Jorgenson, R. L., Vogt, V. M., Johnson, M. C. (2009). Foreign Glycoproteins Can Be Actively Recruited to Virus Assembly Sites during Pseudotyping. J. Virol. 83: 4060-4067 [Abstract] [Full Text]  
  • Beausejour, Y., Tremblay, M. J. (2004). Interaction between the Cytoplasmic Domain of ICAM-1 and Pr55Gag Leads to Acquisition of Host ICAM-1 by Human Immunodeficiency Virus Type 1. J. Virol. 78: 11916-11925 [Abstract] [Full Text]  
  • Bosch, V., Kramer, B., Pfeiffer, T., Starck, L., Steinhauer, D. A. (2001). Inhibition of release of lentivirus particles with incorporated human influenza virus haemagglutinin by binding to sialic acid-containing cellular receptors. J. Gen. Virol. 82: 2485-2494 [Abstract] [Full Text]  
  • Zeilfelder, U., Bosch, V. (2001). Properties of Wild-Type, C-Terminally Truncated, and Chimeric Maedi-Visna Virus Glycoprotein and Putative Pseudotyping of Retroviral Vector Particles. J. Virol. 75: 548-555 [Abstract] [Full Text]  
  • Yap, M. W., Kingsman, S. M., Kingsman, A. J. (2000). Effects of stoichiometry of retroviral components on virus production. J. Gen. Virol. 81: 2195-2202 [Abstract] [Full Text]  
  • Hoffman, T. L., Canziani, G., Jia, L., Rucker, J., Doms, R. W. (2000). A biosensor assay for studying ligand-membrane receptor interactions: Binding of antibodies and HIV-1 Env to chemokine receptors. Proc. Natl. Acad. Sci. USA 97: 11215-11220 [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»