The immunoglobulin constant region contributes to affinity and specificity.
A central dogma in immunology is that antibody specificity is solely the result of variable (V)-region interactions with an antigen. However, this view is not tenable in light of numerous reports that constant heavy (C(H)) domains can affect binding affinity and specificity and V-region structure. Kinetic and thermodynamic proof for the occurrence of this phenomenon is now available. C(H)-region effects on affinity and specificity suggest new mechanisms for generating antibody diversity and polyreactivity (multispecificity) that impact current views on idiotype regulation, autoimmunity, and B cell selection and change our understanding of vaccine responses.
Torres
Marcela
M
Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Casadevall
Arturo
A
D000818:Animals; D000915:Antibody Affinity; D000916:Antibody Diversity; D000917:Antibody Formation; D000918:Antibody Specificity; D006801:Humans; D007127:Immunoglobulin Constant Regions / Q000276:immunology* / Q000378:metabolism; D007130:Immunoglobulin Idiotypes / Q000276:immunology* / Q000378:metabolism; D007132:Immunoglobulin Isotypes / Q000276:immunology* / Q000378:metabolism
D007127:Immunoglobulin Constant Regions; D007130:Immunoglobulin Idiotypes; D007132:Immunoglobulin Isotypes