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Expression of the extracellular region of the human interleukin-4 receptor $$alpha$$ chain and interleukin-13 receptor $$alpha$$1 chain by a silkworm-baculovirus system

Honjo, Eijiro; Shoyama, Yoshinari; Tamada, Taro; Shigematsu, Hideki*; Hatanaka, Takaaki*; Kanaji, Sachiko*; Arima, Kazuhiko*; Ito, Yuji*; Izuhara, Kenji*; Kuroki, Ryota

The receptor binding to Interleukin (IL)-13 is composed of the IL-13 receptor $$alpha$$1 chain (IL-13R $$alpha$$1) and the IL-4 receptor $$alpha$$ chain (IL-4R $$alpha$$). In order to investigate the interaction of IL-13 with IL-13R $$alpha$$1 and IL-4R $$alpha$$, the DNA fragments coding the extracellular regions of human IL-13R $$alpha$$1 and the IL-4R $$alpha$$ 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. Size exclusion chromatography and SPR analysis revealed that mixture of IL-13 and IL-13R$$alpha$$1 showed predominant affinity to IL-4R$$alpha$$, although neither detectable affinity of IL-13 nor IL-13R$$alpha$$1 was observed against IL-4R$$alpha$$. Combining these data with the moderate affinity of IL-13 to IL-13R$$alpha$$1, this indicates that IL-13 first binds to IL-13R$$alpha$$1 and recruits consequently to IL-4R.

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Category:Biochemical Research Methods

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