Monoclonal Antibodies Used to Probe Acetylcholine Receptor Structure: Localization of the Main Immunogenic Region and Detection of Similarities between Subunits

Seventeen cell lines producing monoclonal antibodies against Torpedo californica (torpedo) acetylcholine receptor (AcChoR) and its subunits were established. By using these antibodies as probes, we identified: (i) a similar antigenic determinant on α and β torpedo subunits, (ii) a similar antigenic...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1980-02, Vol.77 (2), p.755-759
Main Authors: Tzartos, Socrates J., Lindstrom, Jon M.
Format: Article
Language:English
Subjects:
Animals
Antibodies
Antibody Specificity
Binding sites
Biochemistry
Cholinergic receptors
Clone Cells - immunology
Epitopes
Fishes
Immune response
Immunization, Passive
Immunoprecipitation
Macromolecular Substances
Monoclonal antibodies
Myasthenia gravis
Myasthenia Gravis - immunology
Protein Conformation
Rats
Rats, Inbred Lew
Receptors, Cholinergic - immunology
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Summary:Seventeen cell lines producing monoclonal antibodies against Torpedo californica (torpedo) acetylcholine receptor (AcChoR) and its subunits were established. By using these antibodies as probes, we identified: (i) a similar antigenic determinant on α and β torpedo subunits, (ii) a similar antigenic determinant on γ and δ subunits, (iii) antigenic determinants unique for α or β torpedo AcChoR subunits, (iv) a small region on the α subunit that dominates the immunogenicity of native torpedo AcChoR in rats (a monoclonal antibody directed at this region could bind to rat AcChoR in vivo and cause passive experimental autoimmune myasthenia gravis), and (v) antigenic determinants on torpedo subunits recognized in AcChoR from other species. The unexpected similarities between α and β and between γ and δ subunits raise the possibility that the complex four-subunit structure of AcChoR was derived from a simpler precursor and suggests that these antigenic similarities might reflect some structural and functional homologies.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.77.2.755