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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, 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.

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

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