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Protein Expr Purif. 2008 Jul;60(1):25-30. doi: 10.1016/j.pep.2008.03.020. Epub 2008 Mar 31.

Expression of the extracellular region of the human interleukin-4 receptor alpha chain and interleukin-13 receptor alpha1 chain by a silkworm-baculovirus system.

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Neutron Biology Research Center, Quantum Beam Science Directorate, Japan Atomic Energy Agency, 2-4 Shirakata-Shirane, Tokai, Ibaraki 319-1195, Japan.


The receptor binding to interleukin (IL)-13 is composed of the IL-13 receptor alpha1 chain (IL-13Ralpha1) and the IL-4 receptor alpha chain (IL-4Ralpha). In order to investigate the interaction of IL-13 with IL-13Ralpha1 and IL-4Ralpha, the DNA fragments coding the extracellular regions of human IL-13Ralpha1 and the IL-4Ralpha (containing a cytokine receptor homologous region) were fused with mouse Fc and expressed by a silkworm-baculovirus system. The expressed receptors were successfully purified by affinity chromatography using protein A, and the Fc region was removed by thrombin digestion. After further purification with anion-exchange chromatography, these receptors were used to investigate the ligand-receptor interaction. Size exclusion chromatography and SPR analysis revealed that mixture of IL-13 and IL-13Ralpha1 showed predominant affinity to IL-4Ralpha, although neither detectable affinity of IL-13 nor IL-13Ralpha1 was observed against IL-4Ralpha. Combining these data with the moderate affinity of IL-13 to IL-13Ralpha1, this indicates that IL-13 first binds to IL-13Ralpha1 and recruits consequently to IL-4R.

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