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Reaction of overlapping synthetic peptides spanning the extracellular part (residues 1-210) of the alpha chain of the Torpedo californica acetylcholine receptor (an alpha 2 beta gamma delta pentamer) with anti-receptor antibodies produced the profiles of the continuous antigenic regions of the correlate segment. Essentially similar profiles were recognized by rabbit and outbred mouse antibodies against isolated receptor or mouse antibodies against membrane-bound receptor. The antigenic sites reside within eight continuous regions: residues 1-14, 25-36, 41-53, 63-75, 102-114, 128-138, 172-182, and 188-198. Five of these regions (the second and the fifth through the eighth) appeared to be immunodominant. Significantly, two of these antigenic regions (i.e., those residing within residues 128-138 and 188-198) coincided with known toxin-binding regions. The antigenic profile suggests that recognition is directed to the intact molecule and only very slightly to the processed (fragmented) protein.

Profile of the continuous antigenic regions on the extracellular part of the alpha chain of an acetylcholine receptor.