Cloning and expression of interleukin-18 binding protein

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...

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Bibliographic Details
Published in:FEBS letters 1999-02, Vol.445 (2), p.338-342
Main Authors: Aizawa, Yasushi, Akita, Kenji, Taniai, Madoka, Torigoe, Kakuji, Mori, Tetsuya, Nishida, Yoshihiro, Ushio, Shimpei, Nukada, Yoshiyuki, Tanimoto, Tadao, Ikegami, Hakuo, Ikeda, Masao, Kurimoto, Masashi
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Antagonist
Base Sequence
Cell Line
CHO Cells
Cloning, Molecular
Complex
COS Cells
Cricetinae
DNA, Complementary
Gene Expression
Glycoproteins - genetics
Glycoproteins - metabolism
Humans
Intercellular Signaling Peptides and Proteins
Interleukin-18
Interleukin-18 - metabolism
Interleukin-18 binding protein
Interleukin-18 receptor
Mice
Molecular Sequence Data
Proteins - genetics
Proteins - metabolism
Sequence Homology, Amino Acid
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(99)00148-9