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

 Previous Article  |  Next Article 

Journal of Virology, May 2001, p. 4744-4751, Vol. 75, No. 10
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.10.4744-4751.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

N-Glycans of F Protein Differentially Affect Fusion Activity of Human Respiratory Syncytial Virus

Gert Zimmer, Ina Trotz, and Georg Herrler*

Institut für Virologie, Tierärztliche Hochschule Hannover, D-30559 Hannover, Germany

Received 12 December 2000/Accepted 23 February 2001

The human respiratory syncytial virus (Long strain) fusion protein contains six potential N-glycosylation sites: N27, N70, N116, N120, N126, and N500. Site-directed mutagenesis of these positions revealed that the mature fusion protein contains three N-linked oligosaccharides, attached to N27, N70, and N500. By introducing these mutations into the F gene in different combinations, four more mutants were generated. All mutants, including a triple mutant devoid of any N-linked oligosaccharide, were efficiently transported to the plasma membrane, as determined by flow cytometry and cell surface biotinylation. None of the glycosylation mutations interfered with proteolytic activation of the fusion protein. Despite similar levels of cell surface expression, the glycosylation mutants affected fusion activity in different ways. While the N27Q mutation did not have an effect on syncytium formation, loss of the N70-glycan caused a fusion activity increase of 40%. Elimination of both N-glycans (N27/70Q mutant) reduced the fusion activity by about 50%. A more pronounced reduction of the fusion activity of about 90% was observed with the mutants N500Q, N27/500Q, and N70/500Q. Almost no fusion activity was detected with the triple mutant N27/70/500Q. These data indicate that N-glycosylation of the F2 subunit at N27 and N70 is of minor importance for the fusion activity of the F protein. The single N-glycan of the F1 subunit attached to N500, however, is required for efficient syncytium formation.

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

Journal of Virology, May 2001, p. 4744-4751, Vol. 75, No. 10
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.10.4744-4751.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Schwegmann-Wessels, C., Glende, J., Ren, X., Qu, X., Deng, H., Enjuanes, L., Herrler, G. (2009). Comparison of vesicular stomatitis virus pseudotyped with the S proteins from a porcine and a human coronavirus. J. Gen. Virol. 90: 1724-1729 [Abstract] [Full Text]  
  • Rawling, J., Garcia-Barreno, B., Melero, J. A. (2008). Insertion of the Two Cleavage Sites of the Respiratory Syncytial Virus Fusion Protein in Sendai Virus Fusion Protein Leads to Enhanced Cell-Cell Fusion and a Decreased Dependency on the HN Attachment Protein for Activity. J. Virol. 82: 5986-5998 [Abstract] [Full Text]  
  • 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]  
  • Long, G., Pan, X., Vlak, J. M. (2007). Absence of N-linked glycans from the F2 subunit of the major baculovirus envelope fusion protein F enhances fusogenicity. J. Gen. Virol. 88: 441-449 [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]  
  • 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]  
  • 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]  
  • 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., Kaufmann, A., Maisner, A. (2004). Influence of N-Glycans on Processing and Biological Activity of the Nipah Virus Fusion Protein. J. Virol. 78: 7274-7278 [Abstract] [Full Text]  
  • Kohl, W., Zimmer, G., Greiser-Wilke, I., Haas, L., Moennig, V., Herrler, G. (2004). The surface glycoprotein E2 of bovine viral diarrhoea virus contains an intracellular localization signal. J. Gen. Virol. 85: 1101-1111 [Abstract] [Full Text]  
  • Schwegmann-Wessels, C., Zimmer, G., Schroder, B., Breves, G., Herrler, G. (2003). Binding of Transmissible Gastroenteritis Coronavirus to Brush Border Membrane Sialoglycoproteins. J. Virol. 77: 11846-11848 [Abstract] [Full Text]  
  • von Messling, V., Cattaneo, R. (2003). N-Linked Glycans with Similar Location in the Fusion Protein Head Modulate Paramyxovirus Fusion. J. Virol. 77: 10202-10212 [Abstract] [Full Text]  
  • Schlender, J., Zimmer, G., Herrler, G., Conzelmann, K.-K. (2003). Respiratory Syncytial Virus (RSV) Fusion Protein Subunit F2, Not Attachment Protein G, Determines the Specificity of RSV Infection. J. Virol. 77: 4609-4616 [Abstract] [Full Text]  
  • Zimmer, G., Conzelmann, K.-K., Herrler, G. (2002). Cleavage at the Furin Consensus Sequence RAR/KR109 and Presence of the Intervening Peptide of the Respiratory Syncytial Virus Fusion Protein Are Dispensable for Virus Replication in Cell Culture. J. Virol. 76: 9218-9224 [Abstract] [Full Text]  
  • Rixon, H. W. McL., Brown, C., Brown, G., Sugrue, R. J. (2002). Multiple glycosylated forms of the respiratory syncytial virus fusion protein are expressed in virus-infected cells. J. Gen. Virol. 83: 61-66 [Abstract] [Full Text]  
  • Zimmer, G., Budz, L., Herrler, G. (2001). Proteolytic Activation of Respiratory Syncytial Virus Fusion Protein. CLEAVAGE AT TWO FURIN CONSENSUS SEQUENCES. J. Biol. Chem. 276: 31642-31650 [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»