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Journal of Interferon & Cytokine Research
cDNA Cloning of Biologically Active Chicken Interleukin-18
To cite this article:
Kirsten Schneider, Florian Puehler, Daniela Baeuerle, Sandra Elvers, Peter Staeheli, Bernd Kaspers, Kirsten C. Weining.
Journal of Interferon & Cytokine Research.
October 2000,
20(10): 879-883.
doi:10.1089/10799900050163244.
Kirsten Schneider Abteilung Virologie, Institut für Medizinische Mikrobiologie und Hygiene, University of Freiburg, 79008 Freiburg, Germany Florian Puehler Abteilung Virologie, Institut für Medizinische Mikrobiologie und Hygiene, University of Freiburg, 79008 Freiburg, Germany Daniela Baeuerle Abteilung Virologie, Institut für Medizinische Mikrobiologie und Hygiene, University of Freiburg, 79008 Freiburg, Germany Sandra Elvers Abteilung Virologie, Institut für Medizinische Mikrobiologie und Hygiene, University of Freiburg, 79008 Freiburg, Germany Peter Staeheli Abteilung Virologie, Institut für Medizinische Mikrobiologie und Hygiene, University of Freiburg, 79008 Freiburg, Germany Bernd Kaspers Institut für Tierphysiologie, University of Munich, 80539 Munich, Germany Kirsten C. Weining Abteilung Virologie, Institut für Medizinische Mikrobiologie und Hygiene, University of Freiburg, 79008 Freiburg, Germany 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-γ (IFN-γ) in cultured primary chicken spleen cells, indicating that the recombinant protein is biologically active.  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