This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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 Moll, M.
Right arrow Articles by Maisner, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Moll, M.
Right arrow Articles by Maisner, A.

 Previous Article  |  Next Article 

Journal of Virology, September 2004, p. 9705-9712, Vol. 78, No. 18
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.18.9705-9712.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Ubiquitous Activation of the Nipah Virus Fusion Protein Does Not Require a Basic Amino Acid at the Cleavage Site

Markus Moll,{dagger} Sandra Diederich,1 Hans-Dieter Klenk,1 Markus Czub,2 and Andrea Maisner1*

Institute of Virology, Philipps University of Marburg, Marburg, Germany,1 Special Pathogens Program, Canadian Science Centre for Human and Animal Health, Winnipeg, Canada2

Received 10 February 2004/ Accepted 5 May 2004

Nipah virus (NiV), a highly pathogenic paramyxovirus, causes a systemic infection in vivo and is able to replicate in cultured cells of many species and organs. Such pantropic paramyxoviruses generally encode fusion (F) proteins with multibasic cleavage sites activated by furin or other ubiquitous intracellular host cell proteases. In contrast, NiV has an F protein with a single arginine (R109) at the cleavage site, as is the case with paramyxoviruses that are activated by trypsin-like proteases only present in specific cells or tissues and therefore only cause localized infections. Unlike these viruses, cleavage of the NiV F protein is ubiquitous and does not require the addition of exogenous proteases in cell culture. To determine the importance of the amino acid sequence at the NiV F protein cleavage site for ubiquitous activation, we generated NiV F proteins with mutations around R109. Surprisingly, neither the exchange of amino acids upstream of R109 nor replacement of the basic residue itself interfered with F cleavage. Thus, R109 is not essential for F cleavage and activation. Our data demonstrate that NiV F-protein activation depends on a novel type of proteolytic cleavage that has not yet been described for any other paramyxovirus F protein. NiV F activation is mediated by a ubiquitous protease that requires neither a monobasic nor a multibasic cleavage site and therefore differs from the furin- or trypsin-like proteases known to activate other ortho- and paramyxovirus fusion proteins.

* 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, September 2004, p. 9705-9712, Vol. 78, No. 18
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.18.9705-9712.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Biacchesi, S., Pham, Q. N., Skiadopoulos, M. H., Murphy, B. R., Collins, P. L., Buchholz, U. J. (2006). Modification of the Trypsin-Dependent Cleavage Activation Site of the Human Metapneumovirus Fusion Protein To Be Trypsin Independent Does Not Increase Replication or Spread in Rodents or Nonhuman Primates.. J. Virol. 80: 5798-5806 [Abstract] [Full Text]  
  • Meulendyke, K. A., Wurth, M. A., McCann, R. O., Dutch, R. E. (2005). Endocytosis Plays a Critical Role in Proteolytic Processing of the Hendra Virus Fusion Protein. J. Virol. 79: 12643-12649 [Abstract] [Full Text]  
  • Pager, C. T., Dutch, R. E. (2005). Cathepsin L Is Involved in Proteolytic Processing of the Hendra Virus Fusion Protein. J. Virol. 79: 12714-12720 [Abstract] [Full Text]  
  • Diederich, S., Moll, M., Klenk, H.-D., Maisner, A. (2005). The Nipah Virus Fusion Protein Is Cleaved within the Endosomal Compartment. J. Biol. Chem. 280: 29899-29903 [Abstract] [Full Text]  
  • Springfeld, C., von Messling, V., Tidona, C. A., Darai, G., Cattaneo, R. (2005). Envelope Targeting: Hemagglutinin Attachment Specificity Rather than Fusion Protein Cleavage-Activation Restricts Tupaia Paramyxovirus Tropism. J. Virol. 79: 10155-10163 [Abstract] [Full Text]  
  • Vogt, C., Eickmann, M., Diederich, S., Moll, M., Maisner, A. (2005). Endocytosis of the Nipah Virus Glycoproteins. J. Virol. 79: 3865-3872 [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»