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Cloning and expression of interleukin‐18 binding protein
Author(s) -
Aizawa Yasushi,
Akita Kenji,
Taniai Madoka,
Torigoe Kakuji,
Mori Tetsuya,
Nishida Yoshihiro,
Ushio Shimpei,
Nukada Yoshiyuki,
Tanimoto Tadao,
Ikegami Hakuo,
Ikeda Masao,
Kurimoto Masashi
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00148-9
Subject(s) - microbiology and biotechnology , complementary dna , recombinant dna , biology , binding protein , interleukin 1 receptor , interleukin , peptide sequence , protein a/g , biochemistry , cytokine , gene , fusion protein , immunology
Interleukin‐18 binding protein is a novel glycoprotein that we successfully cloned and expressed. First, murine interleukin‐18 binding protein was purified from the sera of mice with endotoxin shock using ligand affinity chromatography. The murine interleukin‐18 binding protein cDNA was cloned after RT‐PCR using mixed primer pair sequences based on partial murine interleukin‐18 binding protein amino acid sequence analysis. Subsequently, human interleukin‐18 binding protein cDNA was cloned from cDNA libraries of normal human liver using murine interleukin‐18 binding protein cDNA as a probe. Next, we transiently expressed recombinant human and murine interleukin‐18 binding proteins in COS‐1 cells and purified them from culture supernatants. Both recombinant interleukin‐18 binding proteins did not exhibit species specificity and prevented interleukin‐18 binding to its receptor. In addition, they inhibited interleukine‐18 dependent IFN‐γ production from KG‐1 cells effectively. These results suggest that the interleukin‐18 binding protein may possess interleukine‐18 antagonist activity.