IL-15 was discovered in the supernatant from a simian kidney epithelial cell line CV-1/EBNA, as a soluble factor capable of supporting proliferation of the IL-2-dependent cell line, CTLL-2 (1). Interleukin-15 (IL-15) is a regulatory cytokine, and it is produced by dendritic cells, epithelial cells, human stromal cell line (IMTLH), fibroblasts, and monocytes (2). IL-15 plays an important role in immune response and shares many functions with IL-2, for example, stimulating the proliferation of activated T cells (1, 2), NK cells (3) and B cells, and inducing immunoglobulin synthesis by B cells stimulated by anti-IgM or CD40 ligand (4). In addition, IL-15 promotes the development of dendritic cells (5), activates human neutrophils (6, 7) and induces the production of proinflammatory cytokines from macrophages (8). IL-15 acts as a bridge between innate and adaptive immunity because of its diverse roles in the immune system. IL-15 binds to heterotrimeric receptors composed of IL-15Ralpha, IL-15Rbeta, and IL-15Rgammac. IL-15 shares with IL-2 the receptor chains beta and gammac. IL-15 is normally not secreted in soluble form but is held on the cell surface bound to a unique receptor, IL-15Ralpha, especially on dendritic cells. Cell-bound IL-15 then is presented in trans to T cells and NK cells and is recognized by the gammac receptor on these cells; such recognition maintains cell survival and intermittent proliferation (9).