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 Bergeron, E.
Right arrow Articles by Nichol, S. T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bergeron, E.
Right arrow Articles by Nichol, S. T.

 Previous Article  |  Next Article 

Journal of Virology, December 2007, p. 13271-13276, Vol. 81, No. 23
0022-538X/07/$08.00+0     doi:10.1128/JVI.01647-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Crimean-Congo Hemorrhagic Fever Virus Glycoprotein Processing by the Endoprotease SKI-1/S1P Is Critical for Virus Infectivity{triangledown}

Éric Bergeron, Martin J. Vincent, and Stuart T. Nichol*

Special Pathogens Branch, Division of Viral and Rickettsial Diseases, National Center for Zoonotic, Vector-borne and Enteric Diseases, Centers for Disease Control and Prevention, Atlanta, Georgia 30333

Received 27 July 2007/ Accepted 11 September 2007

Crimean-Congo hemorrhagic fever virus (CCHFV) causes severe human disease. The CCHFV medium RNA encodes a polyprotein which is proteolytically processed to yield the glycoprotein precursors PreGn and PreGc, followed by structural glycoproteins Gn and Gc. Subtilisin kexin isozyme-1/site-1 protease (SKI-1/S1P) plays a central role in Gn processing. Here we show that CCHFV-infected cells deficient in SKI-1/S1P produce no infectious virus, although PreGn and PreGc accumulated normally in the Golgi apparatus, the site of virus assembly. Only nucleoprotein-containing particles which lacked virus glycoproteins (Gn/Gc or PreGn/PreGc) were secreted. Complementation of SKI-1/S1P-deficient cells with a SKI-1/S1P expression vector restored release of infectious virus (>106 PFU/ml), confirming that SKI-1/S1P processing is required for incorporation of viral glycoproteins. SKI-1/S1P may represent a promising antiviral target.

* Corresponding author. Mailing address: Special Pathogens Branch, Division of Viral and Rickettsial Diseases, National Center for Zoonotic, Vector-borne and Enteric Diseases, Centers for Disease Control and Prevention, 1600 Clifton Road, MS G-14, Atlanta, GA 30329. Phone: (404) 639-1115. Fax: (404) 639-1118. E-mail: snichol{at}cdc.gov

{triangledown} Published ahead of print on 26 September 2007.

Journal of Virology, December 2007, p. 13271-13276, Vol. 81, No. 23
0022-538X/07/$08.00+0     doi:10.1128/JVI.01647-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Wegelt, A., Reimann, I., Zemke, J., Beer, M. (2009). New insights into processing of bovine viral diarrhea virus glycoproteins Erns and E1. J. Gen. Virol. 90: 2462-2467 [Abstract] [Full Text]  
  • Albarino, C. G., Bergeron, E., Erickson, B. R., Khristova, M. L., Rollin, P. E., Nichol, S. T. (2009). Efficient Reverse Genetics Generation of Infectious Junin Viruses Differing in Glycoprotein Processing. J. Virol. 83: 5606-5614 [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»