Abstract:
:Interleukin-13 (IL-13) is a T-cell-derived pleiotropic cytokine of particular medical importance because of its critical role in the development of allergic asthma. The effects of IL-13 on its target cells are mediated through a dimeric transmembrane receptor (IL-13R), which shares the IL-4Ralpha subunit with the IL-4R system, but contains as a specific component the IL-13Ralpha1 chain. We have generated a set of single-chain Fv fragments with specific binding capacity to the extracellular domain of the human IL-13Ralpha1 receptor. Bacteriophage clones displaying receptor-binding antibody domains were selected from both naive and synthetic libraries by repetitive panning on recombinant and cell surface-expressed recombinant IL-13Ralpha1. Their specific reactivity with native human IL-13Ralpha1 expressed on the surface of transfected cells was demonstrated by flow cytometry. One binder that specifically interfered with cell activation by IL-13 was extensively characterized. This scFv inhibited IL-13-driven gene transcription and cell proliferation in test cell lines, as well as IL-13-induced activation of primary human monocytes in a dose-dependent manner, with an IC(50) below 300 nM. This novel reagent thus constitutes a valuable tool for the further elucidation of IL-13 function in disease and offers potential therapeutic perspectives.
journal_name
Biol Chemjournal_title
Biological chemistryauthors
Knackmuss S,Krause S,Engel K,Reusch U,Virchow JC,Mueller T,Kraich M,Little M,Luttmann W,Friedrich Kdoi
10.1515/BC.2007.036subject
Has Abstractpub_date
2007-03-01 00:00:00pages
325-30issue
3eissn
1431-6730issn
1437-4315journal_volume
388pub_type
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