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    Proc Natl Acad Sci U S A. 2006 Jun 13;103(24):9166-71. Epub 2006 Jun 6.

    Converting IL-15 to a superagonist by binding to soluble IL-15R{alpha}.

    Rubinstein MP, Kovar M, Purton JF, Cho JH, Boyman O, Surh CD, Sprent J.

    Department of Immunology, IMM4, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

    IL-15 is normally presented in vivo as a cell-associated cytokine bound to IL-15Ralpha. We show here that the biological activity of soluble IL-15 is much improved after interaction with recombinant soluble IL-15Ralpha; after injection, soluble IL-15/IL-15Ralpha complexes rapidly induce strong and selective expansion of memory-phenotype CD8(+) cells and natural killer cells. These findings imply that binding of IL-15Ralpha to IL-15 may create a conformational change that potentiates IL-15 recognition by the betagamma(c) receptor on T cells. The enhancing effect of IL-15Ralpha binding may explain why IL-15 normally functions as a cell-associated cytokine. Significantly, the results with IL-2, a soluble cytokine, are quite different; thus, IL-2 function is markedly inhibited by binding to soluble IL-2Ralpha.

    PMID: 16757567 [PubMed - indexed for MEDLINE]

    PMCID: 1482584

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