Shared idiotypy between phosphorylcholine-specific antibody and acetylcholinesterase detectable by a monoclonal antibody.

Studies were undertaken to detect structural similarities between immunoglobulins and other proteins that bind to choline-containing ligands. Such proteins may share serologically detectable determinants that may not be predicted from the amino acid sequence alone. A monoclonal antibody was used that recognizes an idiotope near the phosphorylcholine binding site of the IgA myeloma TEPC15. This monoclonal anti-TEPC15 idiotopic antibody (anti-Id) also bound the enzyme acetylcholinesterase (AChE) as well as the nicotinic acetylcholine receptor from Torpedo californica. The anti-Id antibody also significantly decreased the AChE catalytic activity but did not affect the activity of an unrelated enzyme, horseradish peroxidase. These findings suggest that nonimmunoglobulin molecules share antigenic determinants with immunoglobulin that are associated with binding to structurally related ligands, and immune regulation may inadvertently affect the function of nonimmune systems.