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
Right arrow Citation Map
Services
Right arrow E-mail this article to a friend
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 Sänger, C.
Right arrow Articles by Becker, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sänger, C.
Right arrow Articles by Becker, S.

 Previous Article  |  Next Article 

Journal of Virology, February 2001, p. 1274-1283, Vol. 75, No. 3
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.3.1274-1283.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Sorting of Marburg Virus Surface Protein and Virus Release Take Place at Opposite Surfaces of Infected Polarized Epithelial Cells

Christian Sänger,1 Elke Mühlberger,1 Elena Ryabchikova,2 Larissa Kolesnikova,1,2 Hans-Dieter Klenk,1 and Stephan Becker1,*

Institut für Virologie, Philipps-Universität Marburg, D-35037 Marburg, Germany,1 and State Research Center of Virology and Biotechnology "Vector" Institute of Molecular Biology, Laboratory of Ultrastructure and Pathomorphology, 633159 Koltsovo, Novosibirsk Region, Russia2

Received 2 August 2000/Accepted 25 October 2000

Marburg virus, a filovirus, causes severe hemorrhagic fever with hitherto poorly understood molecular pathogenesis. We have investigated here the vectorial transport of the surface protein GP of Marburg virus in polarized epithelial cells. To this end, we established an MDCKII cell line that was able to express GP permanently (MDCK-GP). The functional integrity of GP expressed in these cells was analyzed using vesicular stomatitis virus pseudotypes. Further experiments revealed that GP is transported in MDCK-GP cells mainly to the apical membrane and is released exclusively into the culture medium facing the apical membrane. When MDCKII cells were infected with Marburg virus, the majority of GP was also transported to the apical membrane, suggesting that the protein contains an autonomous apical transport signal. Release of infectious progeny virions, however, took place exclusively at the basolateral membrane of the cells. Thus, vectorial budding of Marburg virus is presumably determined by factors other than the surface protein.

* Corresponding author. Mailing address: Institut für Virologie der Philipps-Universität Marburg, Robert-Koch-Strasse 17, D-35037 Marburg, Germany. Phone: 49 (06421) 286-5433. Fax: 49 (06421) 286-5482. E-mail: becker{at}mailer.uni-marburg.de.

Journal of Virology, February 2001, p. 1274-1283, Vol. 75, No. 3
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.3.1274-1283.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Batonick, M., Oomens, A. G. P., Wertz, G. W. (2008). Human Respiratory Syncytial Virus Glycoproteins Are Not Required for Apical Targeting and Release from Polarized Epithelial Cells. J. Virol. 82: 8664-8672 [Abstract] [Full Text]  
  • Runkler, N., Dietzel, E., Moll, M., Klenk, H.-D., Maisner, A. (2008). Glycoprotein targeting signals influence the distribution of measles virus envelope proteins and virus spread in lymphocytes. J. Gen. Virol. 89: 687-696 [Abstract] [Full Text]  
  • Mittler, E., Kolesnikova, L., Strecker, T., Garten, W., Becker, S. (2007). Role of the Transmembrane Domain of Marburg Virus Surface Protein GP in Assembly of the Viral Envelope. J. Virol. 81: 3942-3948 [Abstract] [Full Text]  
  • Bamberg, S., Kolesnikova, L., Moller, P., Klenk, H.-D., Becker, S. (2005). VP24 of Marburg Virus Influences Formation of Infectious Particles. J. Virol. 79: 13421-13433 [Abstract] [Full Text]  
  • Kolesnikova, L., Berghofer, B., Bamberg, S., Becker, S. (2004). Multivesicular Bodies as a Platform for Formation of the Marburg Virus Envelope. J. Virol. 78: 12277-12287 [Abstract] [Full Text]  
  • Schwegmann-Wessels, C., Al-Falah, M., Escors, D., Wang, Z., Zimmer, G., Deng, H., Enjuanes, L., Naim, H. Y., Herrler, G. (2004). A Novel Sorting Signal for Intracellular Localization Is Present in the S Protein of a Porcine Coronavirus but Absent from Severe Acute Respiratory Syndrome-associated Coronavirus. J. Biol. Chem. 279: 43661-43666 [Abstract] [Full Text]  
  • Zimmer, G., Zimmer, K.-P., Trotz, I., Herrler, G. (2002). Vesicular Stomatitis Virus Glycoprotein Does Not Determine the Site of Virus Release in Polarized Epithelial Cells. J. Virol. 76: 4103-4107 [Abstract] [Full Text]  
  • Mora, R., Rodriguez-Boulan, E., Palese, P., Garcia-Sastre, A. (2002). Apical Budding of a Recombinant Influenza A Virus Expressing a Hemagglutinin Protein with a Basolateral Localization Signal. J. Virol. 76: 3544-3553 [Abstract] [Full Text]  
  • Kolesnikova, L., Bugany, H., Klenk, H.-D., Becker, S. (2002). VP40, the Matrix Protein of Marburg Virus, Is Associated with Membranes of the Late Endosomal Compartment. J. Virol. 76: 1825-1838 [Abstract] [Full Text]  


Copyright © 2010 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»