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cDNA cloning of biologically active chicken interleukin-18.

By searching a chicken EST database, we identified a cDNA clone that appeared to contain the entire open reading frame (ORF) of chicken interleukin-18 (ChIL-18). The encoded protein consists of 198 amino acids and exhibits approximately 30% sequence identity to IL-18 of humans and various others mammals. Sequence comparisons reveals a putative caspase-1 cleavage site at aspartic acid 29 of the primary translation product, indicating that mature ChIL-18 might consist of 169 amino acids. Bacterially expressed ChIL-18 in which the N-terminal 29 amino acids of the putative precursor molecule were replaced by a histidine tag induced the synthesis of interferon-gamma ( IFN-gamma) in cultured primary chicken spleen cells, indicating that the recombinant protein is biologically active.[1]

References

  1. cDNA cloning of biologically active chicken interleukin-18. Schneider, K., Puehler, F., Baeuerle, D., Elvers, S., Staeheli, P., Kaspers, B., Weining, K.C. J. Interferon Cytokine Res. (2000) [Pubmed]
 
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