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
Right arrow Citation Map
Services
Right arrow E-mail this article to a friend
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 Cobbold, C.
Right arrow Articles by Wileman, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cobbold, C.
Right arrow Articles by Wileman, T.

Next Article 

Journal of Virology, August 2001, p. 7221-7229, Vol. 75, No. 16
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.16.7221-7229.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

A Virally Encoded Chaperone Specialized for Folding of the Major Capsid Protein of African Swine Fever Virus

C. Cobbold, M. Windsor, and T. Wileman*

Department of Immunology, Institute for Animal Health, Pirbright Laboratory, Woking, Surrey GU24 ONF, United Kingdom

Received 22 December 2000/Accepted 15 May 2001

It is generally believed that cellular chaperones facilitate the folding of virus capsid proteins, or that capsid proteins fold spontaneously. Here we show that p73, the major capsid protein of African swine fever virus (ASFV) failed to fold and aggregated when expressed alone in cells. This demonstrated that cellular chaperones were unable to aid the folding of p73 and suggested that ASFV may encode a chaperone. An 80-kDa protein encoded by ASFV, termed the capsid-associated protein (CAP) 80, bound to the newly synthesized capsid protein in infected cells. The 80-kDa protein was released following conformational maturation of p73 and dissociated before capsid assembly. Coexpression of the 80-kDa protein with p73 prevented aggregation and allowed the capsid protein to fold with kinetics identical to those seen in infected cells. CAP80 is, therefore, a virally encoded chaperone that facilitates capsid protein folding by masking domains exposed by the newly synthesized capsid protein, which are susceptible to aggregation, but cannot be accommodated by host chaperones. It is likely that these domains are ultimately buried when newly synthesized capsid proteins are added to the growing capsid shell.


* Corresponding author. Mailing address: Institute for Animal Health, Pirbright Laboratory, Ash Road, Woking, Surrey GU24 ONF, United Kingdom. Phone: 44-1483-232441. Fax: 44-1483-232448. E-mail: thomas.wileman{at}bbsrc.ac.uk.


Journal of Virology, August 2001, p. 7221-7229, Vol. 75, No. 16
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.16.7221-7229.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Rodriguez, I., Nogal, M. L., Redrejo-Rodriguez, M., Bustos, M. J., Salas, M. L. (2009). The African Swine Fever Virus Virion Membrane Protein pE248R Is Required for Virus Infectivity and an Early Postentry Event. J. Virol. 83: 12290-12300 [Abstract] [Full Text]  
  • Zhao, Z., Ke, F., Huang, Y.-H., Zhao, J.-G., Gui, J.-F., Zhang, Q.-Y. (2008). Identification and characterization of a novel envelope protein in Rana grylio virus. J. Gen. Virol. 89: 1866-1872 [Abstract] [Full Text]  
  • Chapman, D. A. G., Tcherepanov, V., Upton, C., Dixon, L. K. (2008). Comparison of the genome sequences of non-pathogenic and pathogenic African swine fever virus isolates. J. Gen. Virol. 89: 397-408 [Abstract] [Full Text]  
  • Cobbold, C., Windsor, M., Parsley, J., Baldwin, B., Wileman, T. (2007). Reduced redox potential of the cytosol is important for African swine fever virus capsid assembly and maturation. J. Gen. Virol. 88: 77-85 [Abstract] [Full Text]  
  • Epifano, C., Krijnse-Locker, J., Salas, M. L., Rodriguez, J. M., Salas, J. (2006). The African Swine Fever Virus Nonstructural Protein pB602L Is Required for Formation of the Icosahedral Capsid of the Virus Particle. J. Virol. 80: 12260-12270 [Abstract] [Full Text]  
  • Epifano, C., Krijnse-Locker, J., Salas, M. L., Salas, J., Rodriguez, J. M. (2006). Generation of Filamentous Instead of Icosahedral Particles by Repression of African Swine Fever Virus Structural Protein pB438L. J. Virol. 80: 11456-11466 [Abstract] [Full Text]  
  • Peremyslov, V. V., Andreev, I. A., Prokhnevsky, A. I., Duncan, G. H., Taliansky, M. E., Dolja, V. V. (2004). Complex molecular architecture of beet yellows virus particles. Proc. Natl. Acad. Sci. USA 101: 5030-5035 [Abstract] [Full Text]  
  • Heath, C. M., Windsor, M., Wileman, T. (2003). Membrane Association Facilitates the Correct Processing of pp220 during Production of the Major Matrix Proteins of African Swine Fever Virus. J. Virol. 77: 1682-1690 [Abstract] [Full Text]