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Journal of Virology, December 2007, p. 12827-12835, Vol. 81, No. 23
0022-538X/07/$08.00+0     doi:10.1128/JVI.01501-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Molecular and Structural Bases for the Antigenicity of VP2 of Infectious Bursal Disease Virus{triangledown}

Tobias Letzel,1,{dagger} Fasseli Coulibaly,2,{dagger} Felix A. Rey,3 Bernard Delmas,4 Erik Jagt,5 Adriaan A. M. W. van Loon,6 and Egbert Mundt1*

Institute of Molecular Biology, Federal Research Institute for Animal Health, Boddenblick 5a, 17493 Greifswald-Insel Riems, Germany,1 Laboratory of Structural Biology, School of Biological Sciences, University of Auckland, Auckland, New Zealand,2 Unité de Virologie Structurale and URA 3015 CNRS, Département de Virologie, Institut Pasteur, 25 rue du Dr. Roux, 75724 Paris Cedex 15,3 Unité de Virologie et Immunologie Moléculaires, UR892-INRA, Domaine de Vilvert, 78350 Jouy-en-Josas, France,4 Intervet International B.V., P.O. Box 30, 5830 AA Boxmeer,5 Nobilon International B.V., Exportstraat 39B, P.O. Box 320, 5830 AH Boxmeer, The Netherlands6

Received 9 July 2007/ Accepted 6 September 2007

Infectious bursal disease virus (IBDV), a member of the family Birnaviridae, is responsible for a highly contagious and economically important disease causing immunosuppression in chickens. IBDV variants isolated in the United States exhibit antigenic drift affecting neutralizing epitopes in the capsid protein VP2. To understand antigenic determinants of the virus, we have used a reverse-genetics approach to introduce selected amino acid changes—individually or in combination—into the VP2 gene of the classical IBDV strain D78. We thus generated a total of 42 mutants with changes in 8 amino acids selected by sequence comparison and their locations on loops PBC and PHI at the tip of the VP2 spikes, as shown by the crystal structure of the virion. The antibody reactivities of the mutants generated were assessed using a panel of five monoclonal antibodies (MAbs). Our results show that a few amino acids of the projecting domain of VP2 control the reactivity pattern. Indeed, the binding of four out of the five MAbs analyzed here is affected by mutations in these loops. Furthermore, their importance is highlighted by the fact that some of the engineered mutants display identical reactivity patterns but have different growth phenotypes. Finally, this analysis shows that a new field strain isolated from a chicken flock in Belgium (Bel-IBDV) represents an IBDV variant with a hitherto unobserved antigenic profile, involving one change (P222S) in the PBC loop. Overall, our data provide important new insights for devising efficient vaccines that protect against circulating IBDV strains.

* Corresponding author. Present address: University of Georgia, Poultry Diagnostic and Research Center, 953 College Station Road, Athens, GA 30602. Phone: (706) 583-8919. Fax: (706) 542-5630. E-mail: emundt{at}uga.edu

{triangledown} Published ahead of print on 19 September 2007.

{dagger} T.L. and F.C. contributed equally to this paper.

Journal of Virology, December 2007, p. 12827-12835, Vol. 81, No. 23
0022-538X/07/$08.00+0     doi:10.1128/JVI.01501-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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