Molecular and structural bases for the antigenicity of VP2 of infectious bursal disease virus

Tobias Letzel, Fasseli Joseph Coulibaly, Felix A Rey, Bernard Delmas, Erik Jagt, Adrian A M W van Loon, Egbert Mundt

Research output: Contribution to journalArticleResearchpeer-review

Abstract

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 P(BC) and P(HI) 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 P(BC) loop. Overall, our data provide important new insights for devising efficient vaccines that protect against circulating IBDV strains.
Original languageEnglish
Pages (from-to)12827 - 12835
Number of pages9
JournalJournal of Virology
Volume81
Issue number23
Publication statusPublished - 2007
Externally publishedYes

Cite this

Letzel, T., Coulibaly, F. J., Rey, F. A., Delmas, B., Jagt, E., van Loon, A. A. M. W., & Mundt, E. (2007). Molecular and structural bases for the antigenicity of VP2 of infectious bursal disease virus. Journal of Virology, 81(23), 12827 - 12835.
Letzel, Tobias ; Coulibaly, Fasseli Joseph ; Rey, Felix A ; Delmas, Bernard ; Jagt, Erik ; van Loon, Adrian A M W ; Mundt, Egbert. / Molecular and structural bases for the antigenicity of VP2 of infectious bursal disease virus. In: Journal of Virology. 2007 ; Vol. 81, No. 23. pp. 12827 - 12835.
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abstract = "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 P(BC) and P(HI) 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 P(BC) loop. Overall, our data provide important new insights for devising efficient vaccines that protect against circulating IBDV strains.",
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Letzel, T, Coulibaly, FJ, Rey, FA, Delmas, B, Jagt, E, van Loon, AAMW & Mundt, E 2007, 'Molecular and structural bases for the antigenicity of VP2 of infectious bursal disease virus' Journal of Virology, vol. 81, no. 23, pp. 12827 - 12835.

Molecular and structural bases for the antigenicity of VP2 of infectious bursal disease virus. / Letzel, Tobias; Coulibaly, Fasseli Joseph; Rey, Felix A; Delmas, Bernard; Jagt, Erik; van Loon, Adrian A M W; Mundt, Egbert.

In: Journal of Virology, Vol. 81, No. 23, 2007, p. 12827 - 12835.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Molecular and structural bases for the antigenicity of VP2 of infectious bursal disease virus

AU - Letzel, Tobias

AU - Coulibaly, Fasseli Joseph

AU - Rey, Felix A

AU - Delmas, Bernard

AU - Jagt, Erik

AU - van Loon, Adrian A M W

AU - Mundt, Egbert

PY - 2007

Y1 - 2007

N2 - 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 P(BC) and P(HI) 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 P(BC) loop. Overall, our data provide important new insights for devising efficient vaccines that protect against circulating IBDV strains.

AB - 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 P(BC) and P(HI) 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 P(BC) loop. Overall, our data provide important new insights for devising efficient vaccines that protect against circulating IBDV strains.

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M3 - Article

VL - 81

SP - 12827

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JO - Journal of Virology

JF - Journal of Virology

SN - 0022-538X

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ER -

Letzel T, Coulibaly FJ, Rey FA, Delmas B, Jagt E, van Loon AAMW et al. Molecular and structural bases for the antigenicity of VP2 of infectious bursal disease virus. Journal of Virology. 2007;81(23):12827 - 12835.