This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Melanson, V. R. Articles by Iorio, R. M. Search for Related Content PubMed PubMed Citation Articles by Melanson, V. R. Articles by Iorio, R. M.

 Previous Article  |  Next Article 

Journal of Virology, December 2004, p. 13053-13061, Vol. 78, No. 23
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.23.13053-13061.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Amino Acid Substitutions in the F-Specific Domain in the Stalk of the Newcastle Disease Virus HN Protein Modulate Fusion and Interfere with Its Interaction with the F Protein

Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, Massachusetts

Received 12 May 2004/ Accepted 18 June 2004

The hemagglutinin-neuraminidase (HN) protein of Newcastle disease virus mediates attachment to sialic acid receptors, as well as cleavage of the same moiety. HN also interacts with the other viral glycoprotein, the fusion (F) protein, to promote membrane fusion. The ectodomain of the HN spike consists of a stalk and a terminal globular head. The most conserved part of the stalk consists of two heptad repeats separated by a nonhelical intervening region (residues 89 to 95). Several amino acid substitutions for a completely conserved proline residue in this region not only impair fusion and the HN-F interaction but also decrease neuraminidase activity in the globular domain, suggesting that the substitutions may alter HN structure. Substitutions for L94 also interfere with fusion and the HN-F interaction but have no significant effect on any other HN function. Amino acid substitutions at other positions in the intervening region also modulate only fusion. In all cases, diminished fusion correlates with a decreased ability of the mutated HN protein to interact with F at the cell surface. These findings indicate that the intervening region is critical to the role of HN in the promotion of fusion and may be directly involved in its interaction with the homologous F protein.

This article has been cited by other articles:

• Bishop, K. A., Hickey, A. C., Khetawat, D., Patch, J. R., Bossart, K. N., Zhu, Z., Wang, L.-F., Dimitrov, D. S., Broder, C. C. (2008). Residues in the Stalk Domain of the Hendra Virus G Glycoprotein Modulate Conformational Changes Associated with Receptor Binding. J. Virol. 82: 11398-11409 [Abstract] [Full Text]  
• Mahon, P. J., Mirza, A. M., Musich, T. A., Iorio, R. M. (2008). Engineered Intermonomeric Disulfide Bonds in the Globular Domain of Newcastle Disease Virus Hemagglutinin-Neuraminidase Protein: Implications for the Mechanism of Fusion Promotion. J. Virol. 82: 10386-10396 [Abstract] [Full Text]  
• Corey, E. A., Iorio, R. M. (2007). Mutations in the Stalk of the Measles Virus Hemagglutinin Protein Decrease Fusion but Do Not Interfere with Virus-Specific Interaction with the Homologous Fusion Protein. J. Virol. 81: 9900-9910 [Abstract] [Full Text]  
• Melanson, V. R., Iorio, R. M. (2006). Addition of N-Glycans in the Stalk of the Newcastle Disease Virus HN Protein Blocks Its Interaction with the F Protein and Prevents Fusion. J. Virol. 80: 623-633 [Abstract] [Full Text]