Abstract
Interleukin-18(IL-18) is a member of the IL-1 family,which plays important roles in host immune response and regulation.Chicken IL-18(chIL-18) was cloned in 2000,and the subsequent studies showed that it had similar biological functions with mammalian IL-18.The biological activities of IL-18 are mediated by its receptors(IL-18R,including IL-18Rα and IL-18Rβ) expressed on the surface of target cells.The binding of IL-18 with IL-18Rα and IL-18Rβ forms a stable ligand-receptor complex,which subsequently activates intracellular signal transduction molecules.The authors expressed and purified mature chIL-18 with prokaryotic expression system and also obtained the extracellular domains of IL-18Rα and IL-18Rβ with insect cell expression system.They then reconstituted and purified the binary complex chIL-18 with chIL-18Rα and the ternary complex of chIL-18 with chIL-18Rα and chIL-18Rβ in vitro.They also successfully grew the crystals of chIL-18/18Rα binary complex and collected a diffraction dataset of 3 resolution.These results lay a strong basis for future structural studies of chIL-18 with its receptors,which would help better understanding of chIL-18 signal transduction.
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