The immunoglobulin constant region contributes to affinity and specificity

Trends Immunol. 2008 Feb;29(2):91-7. doi: 10.1016/j.it.2007.11.004. Epub 2008 Jan 10.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Antibody Affinity*
  • Antibody Diversity
  • Antibody Formation
  • Antibody Specificity*
  • Humans
  • Immunoglobulin Constant Regions / immunology*
  • Immunoglobulin Constant Regions / metabolism
  • Immunoglobulin Idiotypes / immunology*
  • Immunoglobulin Idiotypes / metabolism
  • Immunoglobulin Isotypes / immunology*
  • Immunoglobulin Isotypes / metabolism

Substances

  • Immunoglobulin Constant Regions
  • Immunoglobulin Idiotypes
  • Immunoglobulin Isotypes