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 Carter, J. R.
Right arrow Articles by Dutch, R. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Carter, J. R.
Right arrow Articles by Dutch, R. E.

 Previous Article  |  Next Article 

Journal of Virology, June 2005, p. 7922-7925, Vol. 79, No. 12
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.12.7922-7925.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Role of N-Linked Glycosylation of the Hendra Virus Fusion Protein

James Richard Carter, Cara Theresia Pager, Stephen Derrick Fowler, and Rebecca Ellis Dutch*

Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky 40536-0298

Received 2 December 2004/ Accepted 8 February 2005

The Hendra virus fusion (F) protein contains five potential sites for N-linked glycosylation in the ectodomain. Examination of F protein mutants with single asparagine-to-alanine mutations indicated that two sites in the F2 subunit (N67 and N99) and two sites in the F1 subunit (N414 and N464) normally undergo N-linked glycosylation. While N-linked modification at N414 is critical for protein folding and transport, F proteins lacking carbohydrates at N67, N99, or N464 remained fusogenically active. As N464 lies within heptad repeat B, these results contrast with those seen for several paramyxovirus F proteins.

* Corresponding Author: Department of Molecular and Cellular Biochemistry University of Kentucky, 800 Rose Street, UKMC MN606 Lexington, KY 40536-0298. Phone: (859) 323-1795. Fax: (859) 323-1037. E-mail:rdutc2{at}uky.edu.

Journal of Virology, June 2005, p. 7922-7925, Vol. 79, No. 12
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.12.7922-7925.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • 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]  
  • Gardner, A. E., Dutch, R. E. (2007). A Conserved Region in the F2 Subunit of Paramyxovirus Fusion Proteins Is Involved In Fusion Regulation. J. Virol. 81: 8303-8314 [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]  
  • Meulendyke, K. A., Wurth, M. A., McCann, R. O., Dutch, R. E. (2005). Endocytosis Plays a Critical Role in Proteolytic Processing of the Hendra Virus Fusion Protein. J. Virol. 79: 12643-12649 [Abstract] [Full Text]  
  • Pager, C. T., Dutch, R. E. (2005). Cathepsin L Is Involved in Proteolytic Processing of the Hendra Virus Fusion Protein. J. Virol. 79: 12714-12720 [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»