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J. Biol. Chem., Vol. 265, Issue 11, 5922-5925, 04, 1990

A point mutation uncouples human interleukin-1 beta biological activity and receptor binding

L Gehrke, SA Jobling, LS Paik, B McDonald, LJ Rosenwasser and PE Auron
Division of Health Sciences and Technology, Massachusetts Institute of Technology, Cambridge 02139.

Interleukin-1 proteins elicit a number of biological activities, but the molecular events following formation of a cell surface receptor- ligand complex have not been well defined. Conversion of Arg127 to Gly127 in the mature human interleukin-1 beta protein reduces bioactivity by 100-fold while the receptor binding affinity decreases by only 25%. The results suggest that the mutant IL-1 beta protein is defective in activating signal transduction events and indicate that binding of interleukin-1 beta protein to receptor is necessary but insufficient for biological activity. The finding that the features of the IL-1 beta protein responsible for receptor binding and biological activity are at least in part distinct may be clinically relevant to the design of interleukin-1 antagonists.
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