HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Tacken, M. G. J. Articles by Peeters, B. P. H. Search for Related Content PubMed PubMed Citation Articles by Tacken, M. G. J. Articles by Peeters, B. P. H. Agricola Articles by Tacken, M. G. J. Articles by Peeters, B. P. H.

Interactions in vivo between the proteins of infectious bursal disease virus: capsid protein VP3 interacts with the RNA-dependent RNA polymerase, VP1

Institute for Animal Science and Health (ID-Lelystad), Department of Avian Virology, PO Box 65, NL-8200 AB Lelystad, The Netherlands¹
University of Utrecht, Department of Infection and Immunity, Utrecht, The Netherlands²

Author for correspondence: Mirriam Tacken. Fax +31 320 238 668. e-mail m.g.j.tacken{at}id.wag-ur.nl

Little is known about the intermolecular interactions between the viral proteins of infectious bursal disease virus (IBDV). By using the yeast two-hybrid system, which allows the detection of protein–protein interactions in vivo, all possible interactions were tested by fusing the viral proteins to the LexA DNA-binding domain and the B42 transactivation domain. A heterologous interaction between VP1 and VP3, and homologous interactions of pVP2, VP3, VP5 and possibly VP1, were found by co-expression of the fusion proteins in Saccharomyces cerevisiae. The presence of the VP1–VP3 complex in IBDV-infected cells was confirmed by co-immunoprecipitation studies. Kinetic analyses showed that the complex of VP1 and VP3 is formed in the cytoplasm and eventually is released into the cell-culture medium, indicating that VP1–VP3 complexes are present in mature virions. In IBDV-infected cells, VP1 was present in two forms of 90 and 95 kDa. Whereas VP3 initially interacted with both the 90 and 95 kDa proteins, later it interacted exclusively with the 95 kDa protein both in infected cells and in the culture supernatant. These results suggest that the VP1–VP3 complex is involved in replication and packaging of the IBDV genome.

This article has been cited by other articles:

				T. Letzel, E. Mundt, and A. E. Gorbalenya Evidence for functional significance of the permuted C motif in Co2+-stimulated RNA-dependent RNA polymerase of infectious bursal disease virus J. Gen. Virol., October 1, 2007; 88(10): 2824 - 2833. [Abstract] [Full Text] [PDF]

				H.-C. S. Liu and J. A. Hicks Using Proteomics to Understand Avian Systems Biology and Infectious Disease Poult. Sci., July 1, 2007; 86(7): 1523 - 1529. [Abstract] [Full Text] [PDF]

				W. J. Kaiser, Y. Chaudhry, S. V. Sosnovtsev, and I. G. Goodfellow Analysis of protein-protein interactions in the feline calicivirus replication complex J. Gen. Virol., February 1, 2006; 87(2): 363 - 368. [Abstract] [Full Text] [PDF]

				C. L. Nouen, G. Rivallan, D. Toquin, P. Darlu, Y. Morin, V. Beven, C. de Boisseson, C. Cazaban, S. Comte, Y. Gardin, et al. Very virulent infectious bursal disease virus: reduced pathogenicity in a rare natural segment-B-reassorted isolate J. Gen. Virol., January 1, 2006; 87(1): 209 - 216. [Abstract] [Full Text] [PDF]

				C. Chevalier, M. Galloux, J. Pous, C. Henry, J. Denis, B. Da Costa, J. Navaza, J. Lepault, and B. Delmas Structural Peptides of a Nonenveloped Virus Are Involved in Assembly and Membrane Translocation J. Virol., October 1, 2005; 79(19): 12253 - 12263. [Abstract] [Full Text] [PDF]

				J. Pous, C. Chevalier, M. Ouldali, J. Navaza, B. Delmas, and J. Lepault Structure of birnavirus-like particles determined by combined electron cryomicroscopy and X-ray crystallography J. Gen. Virol., August 1, 2005; 86(8): 2339 - 2346. [Abstract] [Full Text] [PDF]

				R. A. Villanueva, J. L. Galaz, J. A. Valdes, M. M. Jashes, and A. M. Sandino Genome Assembly and Particle Maturation of the Birnavirus Infectious Pancreatic Necrosis Virus J. Virol., December 15, 2004; 78(24): 13829 - 13838. [Abstract] [Full Text] [PDF]

				U. I. von Einem, A. E. Gorbalenya, H. Schirrmeier, S.-E. Behrens, T. Letzel, and E. Mundt VP1 of infectious bursal disease virus is an RNA-dependent RNA polymerase J. Gen. Virol., August 1, 2004; 85(8): 2221 - 2229. [Abstract] [Full Text] [PDF]

				M. Galloux, C. Chevalier, C. Henry, J.-C. Huet, B. D. Costa, and B. Delmas Peptides resulting from the pVP2 C-terminal processing are present in infectious pancreatic necrosis virus particles J. Gen. Virol., August 1, 2004; 85(8): 2231 - 2236. [Abstract] [Full Text] [PDF]

				M.-H. Chen and J. P. Icenogle Rubella Virus Capsid Protein Modulates Viral Genome Replication and Virus Infectivity J. Virol., April 15, 2004; 78(8): 4314 - 4322. [Abstract] [Full Text] [PDF]

				C. Chevalier, J. Lepault, B. Da Costa, and B. Delmas The Last C-Terminal Residue of VP3, Glutamic Acid 257, Controls Capsid Assembly of Infectious Bursal Disease Virus J. Virol., April 1, 2004; 78(7): 3296 - 3303. [Abstract] [Full Text] [PDF]

				Y. Dieye, A. J. W. Hoekman, F. Clier, V. Juillard, H. J. Boot, and J.-C. Piard Ability of Lactococcus lactis To Export Viral Capsid Antigens: a Crucial Step for Development of Live Vaccines Appl. Envir. Microbiol., December 1, 2003; 69(12): 7281 - 7288. [Abstract] [Full Text] [PDF]

				A. Maraver, A. Ona, F. Abaitua, D. Gonzalez, R. Clemente, J. A. Ruiz-Diaz, J. R. Caston, F. Pazos, and J. F. Rodriguez The Oligomerization Domain of VP3, the Scaffolding Protein of Infectious Bursal Disease Virus, Plays a Critical Role in Capsid Assembly J. Virol., June 1, 2003; 77(11): 6438 - 6449. [Abstract] [Full Text] [PDF]

				A. Maraver, R. Clemente, J. F. Rodriguez, and E. Lombardo Identification and Molecular Characterization of the RNA Polymerase-Binding Motif of Infectious Bursal Disease Virus Inner Capsid Protein VP3 J. Virol., February 15, 2003; 77(4): 2459 - 2468. [Abstract] [Full Text] [PDF]

				M. G. J. Tacken, B. P. H. Peeters, A. A. M. Thomas, P. J. M. Rottier, and H. J. Boot Infectious Bursal Disease Virus Capsid Protein VP3 Interacts both with VP1, the RNA-Dependent RNA Polymerase, and with Viral Double-Stranded RNA J. Virol., October 11, 2002; 76(22): 11301 - 11311. [Abstract] [Full Text] [PDF]

				H. J. Boot, A. A. H. M. ter Huurne, A. J. W. Hoekman, J. M. Pol, A. L. J. Gielkens, and B. P. H. Peeters Exchange of the C-Terminal Part of VP3 from Very Virulent Infectious Bursal Disease Virus Results in an Attenuated Virus with a Unique Antigenic Structure J. Virol., September 11, 2002; 76(20): 10346 - 10355. [Abstract] [Full Text] [PDF]

				B. Da Costa, C. Chevalier, C. Henry, J.-C. Huet, S. Petit, J. Lepault, H. Boot, and B. Delmas The Capsid of Infectious Bursal Disease Virus Contains Several Small Peptides Arising from the Maturation Process of pVP2 J. Virol., March 1, 2002; 76(5): 2393 - 2402. [Abstract] [Full Text] [PDF]

				J. R. Caston, J. L. Martinez-Torrecuadrada, A. Maraver, E. Lombardo, J. F. Rodriguez, J. I. Casal, and J. L. Carrascosa C Terminus of Infectious Bursal Disease Virus Major Capsid Protein VP2 Is Involved in Definition of the T Number for Capsid Assembly J. Virol., November 15, 2001; 75(22): 10815 - 10828. [Abstract] [Full Text] [PDF]

				H. J. Boot, A. A. H. M. ter Huurne, A. J. W. Hoekman, B. P. H. Peeters, and A. L. J. Gielkens Rescue of Very Virulent and Mosaic Infectious Bursal Disease Virus from Cloned cDNA: VP2 Is Not the Sole Determinant of the Very Virulent Phenotype J. Virol., August 1, 2000; 74(15): 6701 - 6711. [Abstract] [Full Text]