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 Kolesnikova, L.
Right arrow Articles by Becker, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kolesnikova, L.
Right arrow Articles by Becker, S.

 Previous Article  |  Next Article 

Journal of Virology, November 2004, p. 12277-12287, Vol. 78, No. 22
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.22.12277-12287.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Multivesicular Bodies as a Platform for Formation of the Marburg Virus Envelope

Larissa Kolesnikova, Beate Berghöfer, Sandra Bamberg, and Stephan Becker*

Institut für Virologie der Philips-Universität Marburg, Marburg, Germany

Received 29 April 2004/ Accepted 30 June 2004

The Marburg virus (MARV) envelope consists of a lipid membrane and two major proteins, the matrix protein VP40 and the glycoprotein GP. Both proteins use different intracellular transport pathways: GP utilizes the exocytotic pathway, while VP40 is transported through the retrograde late endosomal pathway. It is currently unknown where the proteins combine to form the viral envelope. In the present study, we identified the intracellular site where the two major envelope proteins of MARV come together as peripheral multivesicular bodies (MVBs). Upon coexpression with VP40, GP is redistributed from the trans-Golgi network into the VP40-containing MVBs. Ultrastructural analysis of MVBs suggested that they provide the platform for the formation of membrane structures that bud as virus-like particles from the cell surface. The virus-like particles contain both VP40 and GP. Single expression of GP also resulted in the release of particles, which are round or pleomorphic. Single expression of VP40 led to the release of filamentous structures that closely resemble viral particles and contain traces of endosomal marker proteins. This finding indicated a central role of VP40 in the formation of the filamentous structure of MARV particles, which is similar to the role of the related Ebola virusVP40. In MARV-infected cells, VP40 and GP are colocalized in peripheral MVBs as well. Moreover, intracellular budding of progeny virions into MVBs was frequently detected. Taken together, these results demonstrate an intracellular intersection between GP and VP40 pathways and suggest a crucial role of the late endosomal compartment for the formation of the viral envelope.


* Corresponding author. Mailing address: Institut für Virologie der Philipps-Universität Marburg, Robert-Koch-Strasse 17, D-35037 Marburg, Germany. Phone: 6421-2865433. Fax: 6421-2865482. E-mail: becker{at}staff.uni-marburg.de.


Journal of Virology, November 2004, p. 12277-12287, Vol. 78, No. 22
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.22.12277-12287.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Kolesnikova, L., Strecker, T., Morita, E., Zielecki, F., Mittler, E., Crump, C., Becker, S. (2009). Vacuolar Protein Sorting Pathway Contributes to the Release of Marburg Virus. J. Virol. 83: 2327-2337 [Abstract] [Full Text]  
  • Ribeiro, D., Foresti, O., Denecke, J., Wellink, J., Goldbach, R., Kormelink, R. J. M. (2008). Tomato spotted wilt virus glycoproteins induce the formation of endoplasmic reticulum- and Golgi-derived pleomorphic membrane structures in plant cells. J. Gen. Virol. 89: 1811-1818 [Abstract] [Full Text]  
  • Ushijima, Y., Koshizuka, T., Goshima, F., Kimura, H., Nishiyama, Y. (2008). Herpes Simplex Virus Type 2 UL56 Interacts with the Ubiquitin Ligase Nedd4 and Increases Its Ubiquitination. J. Virol. 82: 5220-5233 [Abstract] [Full Text]  
  • Watanabe, T., Sorensen, E. M., Naito, A., Schott, M., Kim, S., Ahlquist, P. (2007). Involvement of host cellular multivesicular body functions in hepatitis B virus budding. Proc. Natl. Acad. Sci. USA 104: 10205-10210 [Abstract] [Full Text]  
  • Urata, S., Noda, T., Kawaoka, Y., Morikawa, S., Yokosawa, H., Yasuda, J. (2007). Interaction of Tsg101 with Marburg Virus VP40 Depends on the PPPY Motif, but Not the PT/SAP Motif as in the Case of Ebola Virus, and Tsg101 Plays a Critical Role in the Budding of Marburg Virus-Like Particles Induced by VP40, NP, and GP. J. Virol. 81: 4895-4899 [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]  
  • Pohl, C., Duprex, W. P., Krohne, G., Rima, B. K., Schneider-Schaulies, S. (2007). Measles virus M and F proteins associate with detergent-resistant membrane fractions and promote formation of virus-like particles. J. Gen. Virol. 88: 1243-1250 [Abstract] [Full Text]  
  • Kuhn, J. H., Radoshitzky, S. R., Guth, A. C., Warfield, K. L., Li, W., Vincent, M. J., Towner, J. S., Nichol, S. T., Bavari, S., Choe, H., Aman, M. J., Farzan, M. (2006). Conserved Receptor-binding Domains of Lake Victoria Marburgvirus and Zaire Ebolavirus Bind a Common Receptor. J. Biol. Chem. 281: 15951-15958 [Abstract] [Full Text]  
  • Moller, P., Pariente, N., Klenk, H.-D., Becker, S. (2005). Homo-Oligomerization of Marburgvirus VP35 Is Essential for Its Function in Replication and Transcription. J. Virol. 79: 14876-14886 [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]  
  • Zimmer, G., Bossow, S., Kolesnikova, L., Hinz, M., Neubert, W. J., Herrler, G. (2005). A Chimeric Respiratory Syncytial Virus Fusion Protein Functionally Replaces the F and HN Glycoproteins in Recombinant Sendai Virus. J. Virol. 79: 10467-10477 [Abstract] [Full Text]