Chicken recombinant antibodies specific for very virulent infectious bursal disease virus
| Autor: | G Gould, L H Parede, D. Toquin, Daral J. Jackwood, Jagoda Ignjatovic, T. van den Berg, S Sapats, Nicolas Eterradossi, Hans G. Heine, L. Trinidad |
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| Rok vydání: | 2006 |
| Předmět: |
animal structures
Birnaviridae Molecular Sequence Data Immunoglobulin Variable Region Virulence Antibodies Viral Infectious bursal disease virus Virus Infectious bursal disease Antibody Specificity Peptide Library Virology medicine Animals Single-chain variable fragment Amino Acid Sequence Poultry Diseases biology Sequence Analysis DNA General Medicine Birnaviridae Infections medicine.disease biology.organism_classification Recombinant Proteins Hypervariable region biology.protein Immunoglobulin Light Chains Antibody Immunoglobulin Heavy Chains Chickens Spleen Conformational epitope |
| Zdroj: | Archives of Virology. 151:1551-1566 |
| ISSN: | 1432-8798 0304-8608 |
| Popis: | A phage-displayed single chain variable fragment (scFv) antibody library was constructed from the immune spleen cells of chickens immunized with very virulent infectious bursal disease virus (vvIBDV) strain CS89. A library consisting of around 9.2 x 10(7) clones was subjected to 3 rounds of panning against captured CS89 virus. Analysis of individual clones by nucleotide sequencing revealed at least 22 unique scFv antibodies binding to vvIBDV in ELISA. Testing of the scFv antibody panel in ELISA against classical, variant or vaccine strains and a wide variety of vvIBDV isolates from the UK, China, France, Belgium, Africa, Brazil, Indonesia and the Netherlands identified one antibody, termed chicken recombinant antibody 88 (CRAb 88) that was specific for vvIBDV. CRAb 88 was capable of recognizing all vvIBDV strains tested regardless of their country of origin and showed no reactivity with classical, variant or vaccine strains, lending support to the use of this scFv as a powerful diagnostic tool for the differentiation of vvIBDV strains. Immunoprecipitation studies revealed that CRAb 88 was directed towards a highly conformational epitope located within the major neutralizing protein VP2. Sequence analysis of the hypervariable region of VP2 of the IBDV strains tested indicate that Ile(256) and Ile(294) may play roles in binding of CRAb 88. This is the first reagent of its type capable of positively distinguishing vvIBDV from other IBDV strains. |
| Databáze: | OpenAIRE |
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