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 Maisner, A.
Right arrow Articles by Herrler, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Maisner, A.
Right arrow Articles by Herrler, G.

 Previous Article  |  Next Article 

J Virol, June 1998, p. 5276-5278, Vol. 72, No. 6
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Polarized Budding of Measles Virus Is Not Determined by Viral Surface Glycoproteins

A. Maisner,1 H.-D. Klenk,1 and G. Herrler1,2,*

Institut für Virologie, Philipps-Universität Marburg, 35037 Marburg,1 and Institut für Virologie, Tierärztliche Hochschule Hannover, 30559 Hannover,2 Germany

Received 19 December 1997/Accepted 10 March 1998

For viruses that mature by a budding process, the envelope glycoproteins are considered the major determinants for the site of virus release from polarized epithelial cells. Viruses are usually released from that membrane domain where the viral surface glycoproteins are transported to. We here report that measles virus has developed a different maturation strategy. Measles virus was found to be released from the apical membrane domain of polarized epithelial cells, though the surface glycoproteins H and F were transported in a nonpolarized fashion and to the basolateral membrane domain, respectively.


* Corresponding author. Mailing address: Institut für Virologie, Tierärztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany. Phone: 49-511-953-8857. Fax: 49-511-953-8898. E-mail: herrler{at}viro.tiho-hannover.de.


J Virol, June 1998, p. 5276-5278, Vol. 72, No. 6
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Runkler, N., Dietzel, E., Carsillo, M., Niewiesk, S., Maisner, A. (2009). Sorting signals in the measles virus wild-type glycoproteins differently influence virus spread in polarized epithelia and lymphocytes. J. Gen. Virol. 90: 2474-2482 [Abstract] [Full Text]  
  • 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]  
  • 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]  
  • Moll, M., Pfeuffer, J., Klenk, H.-D., Niewiesk, S., Maisner, A. (2004). Polarized glycoprotein targeting affects the spread of measles virus in vitro and in vivo. J. Gen. Virol. 85: 1019-1027 [Abstract] [Full Text]  
  • Moll, M., Klenk, H.-D., Maisner, A. (2002). Importance of the Cytoplasmic Tails of the Measles Virus Glycoproteins for Fusogenic Activity and the Generation of Recombinant Measles Viruses. J. Virol. 76: 7174-7186 [Abstract] [Full Text]  
  • Ehrengruber, M. U., Ehler, E., Billeter, M. A., Naim, H. Y. (2002). Measles Virus Spreads in Rat Hippocampal Neurons by Cell-to-Cell Contact and in a Polarized Fashion. J. Virol. 76: 5720-5728 [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]  
  • Sinn, P. L., Williams, G., Vongpunsawad, S., Cattaneo, R., McCray, P. B. Jr. (2002). Measles Virus Preferentially Transduces the Basolateral Surface of Well-Differentiated Human Airway Epithelia. J. Virol. 76: 2403-2409 [Abstract] [Full Text]  
  • von Messling, V., Zimmer, G., Herrler, G., Haas, L., Cattaneo, R. (2001). The Hemagglutinin of Canine Distemper Virus Determines Tropism and Cytopathogenicity. J. Virol. 75: 6418-6427 [Abstract] [Full Text]  
  • Sänger, C., Mühlberger, E., Ryabchikova, E., Kolesnikova, L., Klenk, H.-D., Becker, S. (2001). Sorting of Marburg Virus Surface Protein and Virus Release Take Place at Opposite Surfaces of Infected Polarized Epithelial Cells. J. Virol. 75: 1274-1283 [Abstract] [Full Text]  
  • Maisner, A., Mrkic, B., Herrler, G., Moll, M., Billeter, M. A., Cattaneo, R., Klenk, H.-D. (2000). Recombinant measles virus requiring an exogenous protease for activation of infectivity. J. Gen. Virol. 81: 441-449 [Abstract] [Full Text]  
  • Manié, S. N., Debreyne, S., Vincent, S., Gerlier, D. (2000). Measles Virus Structural Components Are Enriched into Lipid Raft Microdomains: a Potential Cellular Location for Virus Assembly. J. Virol. 74: 305-311 [Abstract] [Full Text]  
  • Moll, M., Klenk, H.-D., Herrler, G., Maisner, A. (2001). A Single Amino Acid Change in the Cytoplasmic Domains of Measles Virus Glycoproteins H and F Alters Targeting, Endocytosis, and Cell Fusion in Polarized Madin-Darby Canine Kidney Cells. J. Biol. Chem. 276: 17887-17894 [Abstract] [Full Text]