Cloning and expression of interleukin‐18 binding protein

FEBS Letters

Akita, Kenji¹  Taniai, Madoka¹  Torigoe, Kakuji¹  Kurimoto, Masashi¹  Tanimoto, Tadao¹  Ushio, Shimpei¹  Ikeda, Masao¹  Nishida, Yoshihiro¹  Aizawa, Yasushi¹  Mori, Tetsuya¹  Nukada, Yoshiyuki¹  Ikegami, Hakuo¹ 

[1] Fujisaki Institute, Hayashibara Biochemical Laboratories, Fujisaki 675-1, Okayama 702-8006, Japan

关键词: Interleukin-18 binding protein;    Interleukin-18;    Interleukin-18 receptor;    Complex;    Antagonist;   

DOI  :  10.1016/S0014-5793(99)00148-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown