1. Academic Validation
  2. Molecular characterization of the human interleukin (IL)-17 receptor

Molecular characterization of the human interleukin (IL)-17 receptor

  • Cytokine. 1997 Nov;9(11):794-800. doi: 10.1006/cyto.1997.0240.
Z Yao 1 M K Spriggs J M Derry L Strockbine L S Park T VandenBos J D Zappone S L Painter R J Armitage
Affiliations

Affiliation

  • 1 Department of Molecular Biology, Immunex Corporation, Seattle, WA 98101, USA.
Abstract

Human interleukin 17 (hIL-17) is a T-cell derived cytokine that exhibits 63% amino acid sequence identity to mouse IL-17 (mIL-17) and 57% identity to a viral protein encoded by the herpesvirus saimiri (HSV) gene 13 (HVS13). The IL-17 family of proteins binds to a unique mouse receptor (mIL-17R). Using nucleic acid hybridization techniques, a cDNA encoding a human homologue of the mIL-17R (hIL-17R) was isolated from a human T cell library. The predicted amino acid sequence of the hIL-17R is 69% identical to the mIL-17R, shares no homology with previously identified cytokine receptor families, and exhibits a broad tissue distribution. The hIL-17R gene was localized to chromosome 22. Monoclonal Antibodies (mAbs) generated against the hIL-17R were able to block the IL-17-induced production of cytokine from human foreskin fibroblast (HFF) cells. Binding studies suggest that recombinant hIL-17 binds to the hIL-17R with low affinity.

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