Utilization of the beta and gamma chains of the IL-2 receptor by the novel cytokine IL-15.

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Abstract
We have recently cloned a novel cytokine, IL‐15, with shared bioactivities but no sequence homology with IL‐2. We found high affinity IL‐15 binding to many cell types, including cells of non‐lymphoid origin. Analysis of IL‐15 interaction with subunits of the IL‐2 receptor (IL‐2R) revealed that the alpha subunit was not involved in IL‐15 binding. We demonstrated directly in cells transfected with IL‐2R subunits that both the beta and gamma chains are required for IL‐15 binding and signaling. Hence, IL‐15, like IL‐2, IL‐4 and IL‐7, utilizes the common IL‐2R gamma subunit found to be defective in X‐linked severe combined immunodeficiency in humans. IL‐15 is the only cytokine other than IL‐2 that has also been shown to share the beta signaling subunit of IL‐2R. The differential ability of some cells to bind and respond to IL‐2 and IL‐15 implies the existence of an additional IL‐15‐specific component.