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M700499200v1
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Papers In Press, published online ahead of print March 13, 2007
J. Biol. Chem, 10.1074/jbc.M700499200
Submitted on January 18, 2007
Revised on February 20, 2007
Accepted on March 13, 2007

Identification of an IL-17F/IL-17A heterodimer in activated human CD4+ T cells

Jill F. Wright, Yongjing Guo, Amira Quazi, Deborah P. Luxenberg, Frann Bennett, John F. Ross, Yongchang Qiu, Matthew J. Whitters, Kathleen N. Tomkinson, Kyri Dunussi-Joannopoulos, Beatriz M. Carreno, Mary Collins, and Neil M. Wolfman

Department of Inflammation, Wyeth, Cambridge, MA 02140

Corresponding Author: jwright{at}wyeth.com

IL-17F and IL-17A are members of the IL-17 pro-inflammatory cytokine family. IL-17A has been implicated in the pathogenesis of autoimmune diseases. IL-17F is a disulfide-linked dimer that contains a cysteine-knot motif. We hypothesized that IL-17F and IL-17A could form a heterodimer due to their sequence homology and overlapping pattern of expression. We evaluated the structure of recombinant IL-17F and IL-17A proteins, as well as that of natural IL-17F and IL-17A derived from activated human CD4+ T cells, by ELISA, immunoprecipitation followed by Western blotting, and mass spectrometry. We find that both IL-17F and IL-17A can form both homodimeric and heterodimeric proteins when expressed in a recombinant system, and that all forms of the recombinant proteins have in vitro functional activity. Furthermore, we find that in addition to the homodimers of IL-17F and IL-17A, activated human CD4+ T cells also produce the IL-17F/IL-17A heterodimer. These data suggest that IL-17F/IL-17A heterodimer may contribute to T cell mediated immune responses.


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