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Journal of Virology, April 2004, p. 3296-3303, Vol. 78, No. 7
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.7.3296-3303.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

The Last C-Terminal Residue of VP3, Glutamic Acid 257, Controls Capsid Assembly of Infectious Bursal Disease Virus

Christophe Chevalier,1 Jean Lepault,2 Bruno Da Costa,1 and Bernard Delmas1*

Unité de Recherche de Virologie et Immunologie Moléculaires, INRA, F-78350 Jouy-en-Josas,1 Laboratoire de Virologie Moléculaire et Structurale, UMR 2472 CNRS-INRA, F-91198 Gif-sur-Yvette, France2

Received 25 September 2003/ Accepted 3 December 2003

Infectious bursal disease virus (IBDV) is a nonenveloped virus with an icosahedral capsid composed of two proteins, VP2 and VP3, that derive from the processing of the polyprotein NH2-pVP2-VP4-VP3-COOH. The virion contains VP1, the viral polymerase, which is both free and covalently linked to the two double-stranded RNA (dsRNA) genomic segments. In this study, the virus assembly process was studied further with the baculovirus expression system. While expression of the wild-type polyprotein was not found to be self-sufficient to give rise to virus-like particles (VLPs), deletion or replacement of the five C-terminal residues of VP3 was observed to promote capsid assembly. Indeed, the single deletion of the C-terminal glutamic acid was sufficient to induce VLP formation. Moreover, fusion of various peptides or small proteins (a green fluorescent protein or a truncated form of ovalbumin) at the C terminus of VP3 also promoted capsid assembly, suggesting that assembly required screening of the negative charges at the C terminus of VP3. The fused polypeptides mimicked the effect of VP1, which interacts with VP3 to promote VLP assembly. The C-terminal segment of VP3 was found to contain two functional domains. While the very last five residues of VP3 mainly controlled both assembly and capsid architecture, the five preceding residues constituted the VP1 (and possibly the pVP2/VP2) binding domain. Finally, we showed that capsid formation is associated with VP2 maturation, demonstrating that the protease VP4 is involved in the virus assembly process.

* Corresponding author. Mailing address: Unité de Recherche de Virologie et Immunologie Moléculaires, INRA, F-78350 Jouy-en-Josas, France. Phone: 33 1 34 65 26 27. Fax: 33 1 34 65 26 21. E-mail: delmas{at}jouy.inra.fr.

Journal of Virology, April 2004, p. 3296-3303, Vol. 78, No. 7
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.7.3296-3303.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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