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 Moll, M.
Right arrow Articles by Maisner, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Moll, M.
Right arrow Articles by Maisner, A.

 Previous Article  |  Next Article 

Journal of Virology, July 2004, p. 7274-7278, Vol. 78, No. 13
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.13.7274-7278.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Influence of N-Glycans on Processing and Biological Activity of the Nipah Virus Fusion Protein

Markus Moll,{dagger} Andreas Kaufmann, and Andrea Maisner*

Institute of Virology, Philipps University of Marburg, Marburg, Germany

Received 17 December 2003/ Accepted 1 March 2004

Nipah virus (NiV), a new member of the Paramyxoviridae, codes for a fusion (F) protein with five potential N-glycosylation sites. Because glycans are known to be important structural components affecting the conformation and function of viral glycoproteins, we analyzed the effect of the deletion of N-linked oligosaccharides on cell surface transport, proteolytic cleavage, and the biological activity of the NiV F protein. Each of the five potential glycosylation sites was removed either individually or in combination, revealing that four sites are actually utilized (g2 and g3 in the F2 subunit and g4 and g5 in the F1 subunit). While the removal of g2 and/or g3 had no or little effect on cleavage, surface transport, and fusion activity, the elimination of g4 or g5 reduced the surface expression by more than 80%. Similar to a mutant lacking all N-glycans, g4 deletion mutants in which the potential glycosylation site was destroyed by introducing a glycine residue were neither cleaved nor transported to the cell surface and consequently were not able to mediate cell-to-cell fusion. This finding indicates that in the absence of g4, the amino acid sequence around position 414 is important for folding and transport.


* Corresponding author. Mailing address: Institut für Virologie, Robert-Koch-Str. 17, 35037 Marburg, Germany. Phone: 49 6421 2865146. Fax: 49 6421 2868962. E-mail: maisner{at}staff.uni-marburg.de.

{dagger} Present address: Center for Infectious Medicine, Karolinska Institute, Stockholm, Sweden.


Journal of Virology, July 2004, p. 7274-7278, Vol. 78, No. 13
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.13.7274-7278.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Malik, T., Wolbert, C., Mauldin, J., Sauder, C., Carbone, K. M., Rubin, S. A. (2007). Functional consequences of attenuating mutations in the haemagglutinin neuraminidase, fusion and polymerase proteins of a wild-type mumps virus strain. J. Gen. Virol. 88: 2533-2541 [Abstract] [Full Text]  
  • Vigerust, D. J., Ulett, K. B., Boyd, K. L., Madsen, J., Hawgood, S., McCullers, J. A. (2007). N-Linked Glycosylation Attenuates H3N2 Influenza Viruses. J. Virol. 81: 8593-8600 [Abstract] [Full Text]  
  • Aguilar, H. C., Matreyek, K. A., Choi, D. Y., Filone, C. M., Young, S., Lee, B. (2007). Polybasic KKR Motif in the Cytoplasmic Tail of Nipah Virus Fusion Protein Modulates Membrane Fusion by Inside-Out Signaling. J. Virol. 81: 4520-4532 [Abstract] [Full Text]  
  • Schowalter, R. M., Smith, S. E., Dutch, R. E. (2006). Characterization of Human Metapneumovirus F Protein-Promoted Membrane Fusion: Critical Roles for Proteolytic Processing and Low pH. J. Virol. 80: 10931-10941 [Abstract] [Full Text]  
  • Aguilar, H. C., Matreyek, K. A., Filone, C. M., Hashimi, S. T., Levroney, E. L., Negrete, O. A., Bertolotti-Ciarlet, A., Choi, D. Y., McHardy, I., Fulcher, J. A., Su, S. V., Wolf, M. C., Kohatsu, L., Baum, L. G., Lee, B. (2006). N-Glycans on Nipah Virus Fusion Protein Protect against Neutralization but Reduce Membrane Fusion and Viral Entry.. J. Virol. 80: 4878-4889 [Abstract] [Full Text]  
  • Diederich, S., Moll, M., Klenk, H.-D., Maisner, A. (2005). The Nipah Virus Fusion Protein Is Cleaved within the Endosomal Compartment. J. Biol. Chem. 280: 29899-29903 [Abstract] [Full Text]  
  • Carter, J. R., Pager, C. T., Fowler, S. D., Dutch, R. E. (2005). Role of N-Linked Glycosylation of the Hendra Virus Fusion Protein. J. Virol. 79: 7922-7925 [Abstract] [Full Text]  
  • Vogt, C., Eickmann, M., Diederich, S., Moll, M., Maisner, A. (2005). Endocytosis of the Nipah Virus Glycoproteins. J. Virol. 79: 3865-3872 [Abstract] [Full Text]