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Journal of Virology, March 2005, p. 3865-3872, Vol. 79, No. 6
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.6.3865-3872.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Endocytosis of the Nipah Virus Glycoproteins

Carola Vogt, Markus Eickmann, Sandra Diederich, Markus Moll,{dagger} and Andrea Maisner*

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

Received 16 August 2004/ Accepted 12 November 2004

Nipah virus (NiV), a highly pathogenic member of the family Paramyxoviridae, encodes the surface glycoproteins F and G. Since internalization of the NiV envelope proteins from the cell surface might be of functional importance for viral pathogenesis either by regulating cytopathogenicity or by modulating recognition of infected cells by the immune system, we analyzed the endocytosis of the NiV F and G proteins. Interestingly, we found both glycoproteins to be internalized in infected and transfected cells. As endocytosis is normally mediated by tyrosine- or dileucine-dependent signals in the cytoplasmic tails of transmembrane proteins, all potential internalization signals in the NiV glycoproteins were mutated. Whereas the G protein appeared to be constitutively internalized with the bulk flow during membrane turnover, uptake of the F protein was found to be signal mediated. F endocytosis clearly depended on a membrane-proximal YXX{Phi} motif and was found to be of functional importance for the biological activity of the protein.

* 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, March 2005, p. 3865-3872, Vol. 79, No. 6
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.6.3865-3872.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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