This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow An erratum has been published
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 Lenz, O.
Right arrow Articles by Garten, W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lenz, O.
Right arrow Articles by Garten, W.

 Previous Article  |  Next Article 

Journal of Virology, December 2000, p. 11418-11421, Vol. 74, No. 23
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Identification of a Novel Consensus Sequence at the Cleavage Site of the Lassa Virus Glycoprotein

Oliver Lenz,1 Jan ter Meulen,2 Heinz Feldmann,3 Hans-Dieter Klenk,1 and Wolfgang Garten1,*

Institut für Virologie, D-35037 Marburg,1 and Bernhard-Nocht-Institut für Tropenmedizin, D-20359 Hamburg,2 Germany, and Health Canada, Laboratory Centre for Disease Control, Winnipeg, Manitoba R3E3R2, Canada3

Received 19 June 2000/Accepted 6 September 2000

The Lassa virus glycoprotein consists of an amino-terminal and a carboxy-terminal cleavage fragment designated GP-1 and GP-2, respectively, that are derived by proteolysis from the precursor GP-C. The membrane-anchored GP-2 obtained from purified virions of the Josiah strain revealed the N-terminal tripeptide GTF262 when analyzed by Edman degradation. Upstream of this site, GP-C contains the tetrapeptide sequence RRLL259, which is conserved in all Lassa virus isolates published to date. Systematic mutational analysis of vector-expressed GP-C revealed that the motif R-X (L/I/V)-L259 (where X stands for L, I, or V) is essential for cleavage of the peptide bond between leucine259 and glycine260. This cleavage motif is homologous to the consensus sequence recognized by a novel class of cellular endoproteases which have so far not been implicated in the processing of viral glycoproteins.

* Corresponding author. Mailing address: Institut für Virologie, Robert-Koch-Strasse 17, D-35037 Marburg, Germany. Phone: 49-6421-286-5145. Fax: 49-6421-286-8962. E-mail: garten{at}mailer.uni-marburg.de.

Journal of Virology, December 2000, p. 11418-11421, Vol. 74, No. 23
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • York, J., Nunberg, J. H. (2009). Intersubunit Interactions Modulate pH-Induced Activation of Membrane Fusion by the Junin Virus Envelope Glycoprotein GPC. J. Virol. 83: 4121-4126 [Abstract] [Full Text]  
  • Cosset, F.-L., Marianneau, P., Verney, G., Gallais, F., Tordo, N., Pecheur, E.-I., ter Meulen, J., Deubel, V., Bartosch, B. (2009). Characterization of Lassa Virus Cell Entry and Neutralization with Lassa Virus Pseudoparticles. J. Virol. 83: 3228-3237 [Abstract] [Full Text]  
  • Rojek, J. M., Lee, A. M., Nguyen, N., Spiropoulou, C. F., Kunz, S. (2008). Site 1 Protease Is Required for Proteolytic Processing of the Glycoproteins of the South American Hemorrhagic Fever Viruses Junin, Machupo, and Guanarito. J. Virol. 82: 6045-6051 [Abstract] [Full Text]  
  • Agnihothram, S. S., York, J., Trahey, M., Nunberg, J. H. (2007). Bitopic Membrane Topology of the Stable Signal Peptide in the Tripartite Junin Virus GP-C Envelope Glycoprotein Complex. J. Virol. 81: 4331-4337 [Abstract] [Full Text]  
  • York, J., Nunberg, J. H. (2006). Role of the Stable Signal Peptide of Junin Arenavirus Envelope Glycoprotein in pH-Dependent Membrane Fusion.. J. Virol. 80: 7775-7780 [Abstract] [Full Text]  
  • Agnihothram, S. S., York, J., Nunberg, J. H. (2006). Role of the stable signal Peptide and cytoplasmic domain of g2 in regulating intracellular transport of the junin virus envelope glycoprotein complex.. J. Virol. 80: 5189-5198 [Abstract] [Full Text]  
  • Boesen, A., Sundar, K., Coico, R. (2005). Lassa Fever Virus Peptides Predicted by Computational Analysis Induce Epitope-Specific Cytotoxic-T-Lymphocyte Responses in HLA-A2.1 Transgenic Mice. CVI 12: 1223-1230 [Abstract] [Full Text]  
  • Le Fourn, V., Ferrand, M., Franc, J.-L. (2005). Endoproteolytic Cleavage of Human Thyroperoxidase: ROLE OF THE PROPEPTIDE IN THE PROTEIN FOLDING PROCESS. J. Biol. Chem. 280: 4568-4577 [Abstract] [Full Text]  
  • Pannetier, D., Faure, C., Georges-Courbot, M.-C., Deubel, V., Baize, S. (2004). Human Macrophages, but Not Dendritic Cells, Are Activated and Produce Alpha/Beta Interferons in Response to Mopeia Virus Infection. J. Virol. 78: 10516-10524 [Abstract] [Full Text]  
  • Pager, C. T., Wurth, M. A., Dutch, R. E. (2004). Subcellular Localization and Calcium and pH Requirements for Proteolytic Processing of the Hendra Virus Fusion Protein. J. Virol. 78: 9154-9163 [Abstract] [Full Text]  
  • Eichler, R., Lenz, O., Strecker, T., Eickmann, M., Klenk, H.-D., Garten, W. (2004). Lassa Virus Glycoprotein Signal Peptide Displays a Novel Topology with an Extended Endoplasmic Reticulum Luminal Region. J. Biol. Chem. 279: 12293-12299 [Abstract] [Full Text]  
  • Strecker, T., Eichler, R., Meulen, J. t., Weissenhorn, W., Dieter Klenk, H., Garten, W., Lenz, O. (2003). Lassa Virus Z Protein Is a Matrix Protein Sufficient for the Release of Virus-Like Particles. J. Virol. 77: 10700-10705 [Abstract] [Full Text]  
  • Vincent, M. J., Sanchez, A. J., Erickson, B. R., Basak, A., Chretien, M., Seidah, N. G., Nichol, S. T. (2003). Crimean-Congo Hemorrhagic Fever Virus Glycoprotein Proteolytic Processing by Subtilase SKI-1. J. Virol. 77: 8640-8649 [Abstract] [Full Text]  
  • Beyer, W. R., Popplau, D., Garten, W., von Laer, D., Lenz, O. (2003). Endoproteolytic Processing of the Lymphocytic Choriomeningitis Virus Glycoprotein by the Subtilase SKI-1/S1P. J. Virol. 77: 2866-2872 [Abstract] [Full Text]  
  • Sanchez, A. J., Vincent, M. J., Nichol, S. T. (2002). Characterization of the Glycoproteins of Crimean-Congo Hemorrhagic Fever Virus. J. Virol. 76: 7263-7275 [Abstract] [Full Text]  
  • Spiropoulou, C. F., Kunz, S., Rollin, P. E., Campbell, K. P., Oldstone, M. B. A. (2002). New World Arenavirus Clade C, but Not Clade A and B Viruses, Utilizes {alpha}-Dystroglycan as Its Major Receptor. J. Virol. 76: 5140-5146 [Abstract] [Full Text]  
  • Elagoz, A., Benjannet, S., Mammarbassi, A., Wickham, L., Seidah, N. G. (2002). Biosynthesis and Cellular Trafficking of the Convertase SKI-1/S1P. ECTODOMAIN SHEDDING REQUIRES SKI-1 ACTIVITY. J. Biol. Chem. 277: 11265-11275 [Abstract] [Full Text]  
  • Lenz, O., ter Meulen, J., Klenk, H.-D., Seidah, N. G., Garten, W. (2001). The Lassa virus glycoprotein precursor GP-C is proteolytically processed by subtilase SKI-1/S1P. Proc. Natl. Acad. Sci. USA 10.1073/pnas.221447598v1 [Abstract] [Full Text]  
  • Lenz, O., ter Meulen, J., Klenk, H.-D., Seidah, N. G., Garten, W. (2001). The Lassa virus glycoprotein precursor GP-C is proteolytically processed by subtilase SKI-1/S1P. Proc. Natl. Acad. Sci. USA 98: 12701-12705 [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»