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Journal of Virology, March 2002, p. 2393-2402, Vol. 76, No. 5
0022-538X/02/$04.00+0     DOI: 10.1128/jvi.76.5.2393-2402.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

The Capsid of Infectious Bursal Disease Virus Contains Several Small Peptides Arising from the Maturation Process of pVP2

*** Bruno Da Costa,1 Christophe Chevalier,1 Celine Henry,2 Jean-Claude Huet,2 Stéphanie Petit,1 Jean Lepault,3 Hein Boot,4 and Bernard Delmas1*

Unité de Virologie et Immunologie Moléculaires,1 Unité de Biochimie et Structure des Protéines, Institut National de la Recherche Agronomique, F-78350 Jouy-en-Josas,2 Laboratoire de Génétique des Virus, Centre National de la Recherche Scientifique, F-91198 Gif-sur-Yvette, France,3 Department of Avian Virology, Institute for Animal Science and Health, Lelystad, The Netherlands4

Received 23 July 2001/ Accepted 28 November 2001

The capsid proteins VP2 and VP3 of infectious bursal disease virus, a birnavirus, are derived from the processing of a large polyprotein: NH2-pVP2-VP4-VP3-COOH. Although the primary cleavage sites at the pVP2-VP4 and VP4-VP3 junctions have been identified, the proteolytic cascade involved in the processing of this polyprotein is not yet fully understood, particularly the maturation of pVP2. By using different approaches, we showed that the processing of pVP2 (residues 1 to 512) generated VP2 and four small peptides (residues 442 to 487, 488 to 494, 495 to 501, and 502 to 512). We also showed that in addition to VP2, at least three of these peptides (residues 442 to 487, 488 to 494, and 502 to 512) were associated with the viral particles. The importance of the small peptides in the virus cycle was assessed by reverse genetics. Our results showed that the mutants lacking the two smaller peptides were viable, although the virus growth was affected. In contrast, deletions of the domain 442 to 487 or 502 to 512 did not allow virus recovery. Several amino acids of the peptide 502 to 512 appeared essential for virus viability. Substitutions of the P1 and/or P1" position were engineered at each of the cleavage sites (P1-P1": 441-442, 487-488, 494-495, 501-502, and 512-513). Most substitutions at the pVP2-VP4 junction (512-513) and at the final VP2 maturation cleavage site (441-442) were lethal. Mutations of intermediate cleavage sites (487-488, 494-495, and 501-502) led to viable viruses showing different but efficient pVP2 processing. Our data suggested that while peptides 488 to 494 and 495 to 501 play an accessory role, peptides 442 to 487 and 502 to 512 have an unknown but important function within the virus cycle.

* Corresponding author. Mailing address: Unité de Virologie et Immunologie Moléculaires, Institut National de la Recherche Agronomique, F-78350 Jouy-en-Josas, France. Phone: 33 1 3465 2627. Fax: 33 1 3465 2621. E-mail: delmas{at}biotec.jouy.inra.fr.

Journal of Virology, March 2002, p. 2393-2402, Vol. 76, No. 5
0022-538X/02/$04.00+0     DOI: 10.1128/jvi.76.5.2393-2402.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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