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 Tacken, M. G. J.
Right arrow Articles by Boot, H. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tacken, M. G. J.
Right arrow Articles by Boot, H. J.

 Previous Article  |  Next Article 

Journal of Virology, November 2002, p. 11301-11311, Vol. 76, No. 22
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.22.11301-11311.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Infectious Bursal Disease Virus Capsid Protein VP3 Interacts both with VP1, the RNA-Dependent RNA Polymerase, and with Viral Double-Stranded RNA

Mirriam G. J. Tacken,1* Ben P. H. Peeters,1 Adri A. M. Thomas,2 Peter J. M. Rottier,3 and Hein J. Boot1

Division of Infectious Diseases and Food Chain Quality, Institute for Animal Science and Health (ID-Lelystad B.V.), NL-8200 AB Lelystad,1 Department of Developmental Biology,2 Virology Division, Veterinary Faculty, Utrecht University, Utrecht, The Netherlands3

Received 20 February 2002/ Accepted 15 August 2002

Infectious bursal disease virus (IBDV) is a double-stranded RNA (dsRNA) virus of the Birnaviridae family. Its two genome segments are encapsidated together with multiple copies of the viral RNA-dependent RNA polymerase, VP1, in a single-shell capsid that is composed of VP2 and VP3. In this study we identified the domains responsible for the interaction between VP3 and VP1. Using the yeast two-hybrid system we found that VP1 binds to VP3 through an internal domain, while VP3 interacts with VP1 solely by its carboxy-terminal 10 amino acids. These results were confirmed by using a reverse-genetics system that allowed us to analyze the interaction of carboxy-terminally truncated VP3 molecules with VP1 in infected cells. Coimmunoprecipitations with VP1- and VP3-specific antibodies revealed that the interaction is extremely sensitive to truncation of VP3. The mere deletion of the C-terminal residue reduced coprecipitation almost completely and also fully abolished production of infectious virions. Surprisingly, these experiments additionally revealed that VP3 also binds to RNA. RNase treatments and reverse transcription-PCR analyses of the immunoprecipitates demonstrated that VP3 interacts with dsRNA of both viral genome segments. This interaction is not mediated by the carboxy-terminal domain of VP3 since C-terminal truncations of 1, 5, or 10 residues did not prevent formation of the VP3-dsRNA complexes. VP3 seems to be the key organizer of birnavirus structure, as it maintains critical interactions with all components of the viral particle: itself, VP2, VP1, and the two genomic dsRNAs.

* Corresponding author. Mailing address: Institute for Animal Science and Health (ID-Lelystad B.V.), Division of Infectious Diseases and Food Chain Quality, P.O. Box 65, NL-8200 AB Lelystad, The Netherlands. Phone: 31 320 238 896. Fax: 31 320 238 668. E-mail: M.G.J.Tacken{at}id.wag-ur.nl.

Journal of Virology, November 2002, p. 11301-11311, Vol. 76, No. 22
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.22.11301-11311.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Galloux, M., Libersou/, S., Morellet, N., Bouaziz, S., Da Costa, B., Ouldali, M., Lepault, J., Delmas, B. (2007). Infectious Bursal Disease Virus, a Non-enveloped Virus, Possesses a Capsid-associated Peptide That Deforms and Perforates Biological Membranes. J. Biol. Chem. 282: 20774-20784 [Abstract] [Full Text]  
  • Liu, H.-C. S., Hicks, J. A. (2007). Using Proteomics to Understand Avian Systems Biology and Infectious Disease. Poult. Sci. 86: 1523-1529 [Abstract] [Full Text]  
  • Pedersen, T., Skjesol, A., Jorgensen, J. B. (2007). VP3, a Structural Protein of Infectious Pancreatic Necrosis Virus, Interacts with RNA-Dependent RNA Polymerase VP1 and with Double-Stranded RNA. J. Virol. 81: 6652-6663 [Abstract] [Full Text]  
  • Nouen, C. L., Rivallan, G., Toquin, D., Darlu, P., Morin, Y., Beven, V., de Boisseson, C., Cazaban, C., Comte, S., Gardin, Y., Eterradossi, N. (2006). Very virulent infectious bursal disease virus: reduced pathogenicity in a rare natural segment-B-reassorted isolate. J. Gen. Virol. 87: 209-216 [Abstract] [Full Text]  
  • Gonzalez, D., Rodriguez, J. F., Abaitua, F. (2005). Intracellular Interference of Infectious Bursal Disease Virus. J. Virol. 79: 14437-14441 [Abstract] [Full Text]  
  • Chevalier, C., Galloux, M., Pous, J., Henry, C., Denis, J., Da Costa, B., Navaza, J., Lepault, J., Delmas, B. (2005). Structural Peptides of a Nonenveloped Virus Are Involved in Assembly and Membrane Translocation. J. Virol. 79: 12253-12263 [Abstract] [Full Text]  
  • Pous, J., Chevalier, C., Ouldali, M., Navaza, J., Delmas, B., Lepault, J. (2005). Structure of birnavirus-like particles determined by combined electron cryomicroscopy and X-ray crystallography. J. Gen. Virol. 86: 2339-2346 [Abstract] [Full Text]  
  • von Einem, U. I., Gorbalenya, A. E., Schirrmeier, H., Behrens, S.-E., Letzel, T., Mundt, E. (2004). VP1 of infectious bursal disease virus is an RNA-dependent RNA polymerase. J. Gen. Virol. 85: 2221-2229 [Abstract] [Full Text]  
  • Galloux, M., Chevalier, C., Henry, C., Huet, J.-C., Costa, B. D., Delmas, B. (2004). Peptides resulting from the pVP2 C-terminal processing are present in infectious pancreatic necrosis virus particles. J. Gen. Virol. 85: 2231-2236 [Abstract] [Full Text]  
  • Chevalier, C., Lepault, J., Da Costa, B., Delmas, B. (2004). The Last C-Terminal Residue of VP3, Glutamic Acid 257, Controls Capsid Assembly of Infectious Bursal Disease Virus. J. Virol. 78: 3296-3303 [Abstract] [Full Text]  
  • Boot, H. J., Pritz-Verschuren, S. B. E. (2004). Modifications of the 3'-UTR stem-loop of infectious bursal disease virus are allowed without influencing replication or virulence. Nucleic Acids Res 32: 211-222 [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»