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J. Exp. Med.,
Volume 186, Number 9, November 3, 1997 1419-1429
By
From the * Institute of Clinical Microbiology and Immunology, University of Erlangen-Nürnberg,
91054 Erlangen, Germany; and The murine interleukin 4 receptor (IL-4R) exists as a transmembrane protein transducing
pleiotropic IL-4 functions, or as soluble (s)IL-4-binding molecule with potent immunoregulatory effects. In this study we identified and characterized a murine IL-4R allotype. Sequence
analysis of the IL-4R cDNA of BALB/c mice revealed 18 base substitutions leading to three
extracellular and five cytoplasmic amino acid changes when compared with the published IL-4R
sequence of C57BL/6 mice. Analyses with allotype-specific mAbs revealed that AKR/J and
SJL/J mice possess the newly identified BALB/c IL-4R allotype whereas the IL-4Rs of C3H,
CBA, DBA-2, and FVB/N mice are identical to that of the C57BL/6 mouse. The extracellular Thr49 to Ile substitution abrogates one N-glycosylation site in the naturally occurring BALB/c
IL-4R as well as in the experimentally point mutated C57BL/6-T49I sIL-4R, and both molecules display a nearly threefold reduction in IL-4-neutralizing activity compared to the
C57BL/6 sIL-4R. In line with this, a significantly enhanced dissociation rate of IL-4 was detected for the BALB/c IL-4R allotype by surface plasmon resonance and in radioligand binding
studies with IL-4R-transfected cell lines. These findings suggest that the altered ligand binding
behavior of the newly described IL-4R allotype may influence the IL-4 responsiveness, thus
contributing to the diverse phenotypes of inbred mouse strains in IL-4-dependent diseases.
Behringwerke AG, 35001 Marburg, Germany
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