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.
Schneider
K
K
Abteilung Virologie, Institut für Medizinische Mikrobiologie und Hygiene, University of Freiburg, 79008 Freiburg, Germany.
Puehler
F
F
Baeuerle
D
D
Elvers
S
S
Staeheli
P
P
Kaspers
B
B
Weining
K C
KC
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D002645:Chickens; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000302:isolation & purification*; D006736:Horses; D006801:Humans; D020382:Interleukin-18 / Q000235:genetics* / Q000502:physiology; D051379:Mice; D008969:Molecular Sequence Data; D051381:Rats; D011994:Recombinant Proteins / Q000494:pharmacology; D017386:Sequence Homology, Amino Acid; D013552:Swine
D018076:DNA, Complementary; D020382:Interleukin-18; D011994:Recombinant Proteins