Cyclosporin A as a model antigen: immunochemical and structural studies

• Published in: Journal of molecular recognition Vol. 15; no. 5; pp. 277 - 285
• Main Author: Altschuh, Danièle
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 01.09.2002
• Subjects: Animals; Antibodies, Monoclonal - chemistry; Antibodies, Monoclonal - metabolism; antigen-antibody affinity; Antigens - chemistry; Antigens - metabolism; Biacore; competition ELISA; crystallographic analysis; Crystallography, X-Ray; cyclosporin; Cyclosporine - chemistry; Cyclosporine - immunology; Cyclosporine - metabolism; Fab-antigen complex; Immunochemistry; Immunoglobulin Fab Fragments - chemistry; Immunoglobulin Fab Fragments - metabolism; Immunosuppressive Agents - chemistry; Immunosuppressive Agents - immunology; Immunosuppressive Agents - metabolism; In Vitro Techniques; Macromolecular Substances; Models, Immunological; Models, Molecular; Molecular Structure; Protein Binding; Protein Conformation; Static Electricity; structure-activity relationship
• ISSN: 0952-3499; 1099-1352
• DOI: 10.1002/jmr.588

The immunosuppressant drug cyclosporin (Cs) A is a cyclic undecapeptide which has been used as a model antigen because structural information and a large number of analogs, modified at each of its 11 positions, were available. This review summarizes immunochemical and crystallographic studies of the interaction between the Fab of monoclonal antibody R45‐45‐11 and Cs. Three points are discussed: (1) the different conformations of CsA and the question of its biologically active form; (2) the Fab–CsA recognition mechanism; and (3) the relationship between structure and binding properties of CsA analogs. Copyright © 2002 John Wiley & Sons, Ltd.