An interleukin-18 binding protein (IL-18BP) was purified from urine by chromatography on IL-18 beads, sequenced, cloned, and expressed in COS7 cells. IL-18BP abolished IL-18 induction of interferon-gamma (IFNgamma), IL-8, and activation of NF-kappaB in vitro. Administration of IL-18BP to mice abrogated circulating IFNgamma following LPS. Thus, IL-18BP functions as an inhibitor of the early Th1 cytokine response. IL-18BP is constitutively expressed in the spleen, belongs to the immunoglobulin superfamily, and has limited homology to the IL-1 type II receptor. Its gene was localized on human chromosome 11q13, and no exon coding for a transmembrane domain was found in an 8.3 kb genomic sequence. Several Poxviruses encode putative proteins highly homologous to IL-18BP, suggesting that viral products may attenuate IL-18 and interfere with the cytotoxic T cell response.
Pubmed ID: 10023777 RIS Download
Mesh terms: Amino Acid Sequence | Animals | Base Sequence | COS Cells | Carrier Proteins | Cloning, Molecular | Cytokines | DNA, Complementary | Exons | Humans | Injections, Intraperitoneal | Interferon Inducers | Interferon-gamma | Interleukin-18 | Introns | Lipopolysaccharides | Mice | Molecular Sequence Data | Poxviridae | Recombinant Proteins | Sequence Homology, Amino Acid | Spleen | Th1 Cells | Viral Proteins
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