Activation of the Nipah Virus Fusion Protein in MDCK Cells Is Mediated by Cathepsin B within the Endosome-Recycling Compartment

Diederich S, Sauerhering L, Weis M, Altmeppen H, Schaschke N, Reinheckel T, Erbar S, Maisner A (2012)
Journal of Virology 86(7): 3736-3745.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Diederich, Sandra; Sauerhering, Lucie; Weis, Michael; Altmeppen, Hermann; Schaschke, NorbertUniBi; Reinheckel, Thomas; Erbar, Stephanie; Maisner, Andrea
Abstract / Bemerkung
Proteolytic activation of the fusion protein of the highly pathogenic Nipah virus (NiV F) is a prerequisite for the production of infectious particles and for virus spread via cell-to-cell fusion. Unlike other paramyxoviral fusion proteins, functional NiV F activation requires endocytosis and pH-dependent cleavage at a monobasic cleavage site by endosomal proteases. Using prototype Vero cells, cathepsin L was previously identified to be a cleavage enzyme. Compared to Vero cells, MDCK cells showed substantially higher F cleavage rates in both NiV-infected and NiV F-transfected cells. Surprisingly, this could not be explained either by an increased F endocytosis rate or by elevated cathepsin L activities. On the contrary, MDCK cells did not display any detectable cathepsin L activity. Though we could confirm cathepsin L to be responsible for F activation in Vero cells, inhibitor studies revealed that in MDCK cells, cathepsin B was required for F-protein cleavage and productive replication of pathogenic NiV. Supporting the idea of an efficient F cleavage in early and recycling endosomes of MDCK cells, endocytosed F proteins and cathepsin B colocalized markedly with the endosomal marker proteins early endosomal antigen 1 (EEA-1), Rab4, and Rab11, while NiV F trafficking through late endosomal compartments was not needed for F activation. In summary, this study shows for the first time that endosomal cathepsin B can play a functional role in the activation of highly pathogenic NiV.
Journal of Virology
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Diederich S, Sauerhering L, Weis M, et al. Activation of the Nipah Virus Fusion Protein in MDCK Cells Is Mediated by Cathepsin B within the Endosome-Recycling Compartment. Journal of Virology. 2012;86(7):3736-3745.
Diederich, S., Sauerhering, L., Weis, M., Altmeppen, H., Schaschke, N., Reinheckel, T., Erbar, S., et al. (2012). Activation of the Nipah Virus Fusion Protein in MDCK Cells Is Mediated by Cathepsin B within the Endosome-Recycling Compartment. Journal of Virology, 86(7), 3736-3745. doi:10.1128/JVI.06628.11
Diederich, Sandra, Sauerhering, Lucie, Weis, Michael, Altmeppen, Hermann, Schaschke, Norbert, Reinheckel, Thomas, Erbar, Stephanie, and Maisner, Andrea. 2012. “Activation of the Nipah Virus Fusion Protein in MDCK Cells Is Mediated by Cathepsin B within the Endosome-Recycling Compartment”. Journal of Virology 86 (7): 3736-3745.
Diederich, S., Sauerhering, L., Weis, M., Altmeppen, H., Schaschke, N., Reinheckel, T., Erbar, S., and Maisner, A. (2012). Activation of the Nipah Virus Fusion Protein in MDCK Cells Is Mediated by Cathepsin B within the Endosome-Recycling Compartment. Journal of Virology 86, 3736-3745.
Diederich, S., et al., 2012. Activation of the Nipah Virus Fusion Protein in MDCK Cells Is Mediated by Cathepsin B within the Endosome-Recycling Compartment. Journal of Virology, 86(7), p 3736-3745.
S. Diederich, et al., “Activation of the Nipah Virus Fusion Protein in MDCK Cells Is Mediated by Cathepsin B within the Endosome-Recycling Compartment”, Journal of Virology, vol. 86, 2012, pp. 3736-3745.
Diederich, S., Sauerhering, L., Weis, M., Altmeppen, H., Schaschke, N., Reinheckel, T., Erbar, S., Maisner, A.: Activation of the Nipah Virus Fusion Protein in MDCK Cells Is Mediated by Cathepsin B within the Endosome-Recycling Compartment. Journal of Virology. 86, 3736-3745 (2012).
Diederich, Sandra, Sauerhering, Lucie, Weis, Michael, Altmeppen, Hermann, Schaschke, Norbert, Reinheckel, Thomas, Erbar, Stephanie, and Maisner, Andrea. “Activation of the Nipah Virus Fusion Protein in MDCK Cells Is Mediated by Cathepsin B within the Endosome-Recycling Compartment”. Journal of Virology 86.7 (2012): 3736-3745.

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