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An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions
08:40

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Published on: March 14, 2016

Identification of regions within the third FnIII-like domain of the IL-5Ralpha involved in IL-5 interaction

P E Czabotar1, J Holland, C J Sanderson

  • 1Molecular Immunology Group, Curtin University of Technology, Perth, Australia. pczabot@nimr.mrc.ac.uk

Cytokine
|July 6, 2000
PubMed

Previously, two binding sites for interleukin 5 (IL-5) were identified on the IL-5 receptor alpha chain (IL-5Ralpha). They are located within the CD loop of the first fibronectin type III (FnIII)-like domain and the EF loop of the second FnIII-like domain. The first binding site was identified by exploiting the different abilities of human IL-5Ralpha (hIL-5Ralpha) and mouse IL-5Ralpha (mIL-5Ralpha) to bind hIL-5. Here we show that ovine IL-5 (oIL-5) has the ability to activate the hIL-5Ralpha but not the mIL-5Ralpha. By using chimeras of the mIL-5Ralpha and hIL-5Ralpha we demonstrate that residues within the first and third FnIII-like domains of mIL-5Ralpha are responsible for this lack of activity. Furthermore, mutation of residues on hIL-5Ralpha to mIL-5Ralpha within the predicted DE and FG loop regions of the third FnIII domain reduces oIL-5 activity. These results show that regions of the third FnIII domain of IL-5Ralpha are involved in binding, in addition to the regions in domains one and two of the IL-5Ralpha that were identified in an earlier study.

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