02535     2200241   4500001002100000005001500021035002000036245035200056700001600408700001300424700001600437700015100453250002500604260000900629300003400638084001500672082001500687008003900702100001700741650003600758520148400794990001502278INLIS00000000001691720241015102539  a0010-07210014491 aChicken recombinant antibodies specific for very virulent infectious bursal disease virus. /cParede, Lies(Balai Penelitian Veteriner, Bogor Indonesia)S. I. Sapats; L. Trinidad; G. Gould; H. G. Heine; J. Ignjatovic(CSIRO Livestock Industries, Australian Animal Health Laboratory, Geelong, Australia)T. P. van den Berg(Avian Virology Immunology Vet  aL. Trinidad  aG. Gould  aH. G. Heine  aJ. Ignjatovic(CSIRO Livestock Industries, Australian Animal Health Laboratory, Geelong, Australia)T. P. van den Berg(Avian Virology Immunology Vet  aArchives of Virology  c2006  aVol. 151 p. 1551-1566. (2006)  aARTVET1449  aARTVET1449241015                |          | |  0 aParede, Lies 4ainfectious bursal disease virus  aA 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 9.2×107 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.  aARTVET1449