Subunit selectivity and epitope characterization of mAbs directed against the GABAA/benzodiazepine receptor.

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Abstract
MAbs bd 17, bd 28 raised against bovine cerebral .gamma.-aminobutyric acid (GABAA)-benzodiazepine receptors were analyzed for their ability to detect each of 12 GABAA receptor subunits expressed in cultured mammalian cells. Results showed that mAb bd 17 recognized epitopes on both .beta.2 and .beta.3 subunits while mAb bd 24 is selective for the .alpha.1 subunit of human and bovine, but not of rat origin. The latter antibody reacts with the rat .alpha.1 subunit carrying an engineered Leu at position four, documenting the first epitope mapping of GABAA receptor subunit-specific mAb. In contrast to mAbs bd 17 and bd 24, mAb bd 28 reacts with all GABAA receptor subunits tested but not with a glycine receptor subunit, suggesting the presence of shared epitopes on subunits of GABA-gated chloride channels.