Paradoxical behavior of asymmetric IgG antibodies

Immunol Rev. 1998 Jun;163:77-87. doi: 10.1111/j.1600-065x.1998.tb01189.x.

Abstract

Changes in the quantity and quality of antibodies occur in the course of an immune response. This review describes the physicochemical and biological properties of asymmetric antibodies as well as their functions, beneficial or harmful to the host, according to the nature of the antigen and the particular situation in which they act. Asymmetric antibodies have two paratopes, one of high affinity, with K0 similar to that of symmetric antibodies, and the other one with an affinity for the antigen 100 times lower. Functional univalence is due to steric hindrance present in one of the paratopes by the carbohydrate moiety attached to the Fd fragment of the Fab region, so these antibodies are unable to form large antibody-antigen complexes and cannot trigger reactions, such as complement fixation, phagocytic activity and antigen clearance. When asymmetric IgG antibodies are specific for self-antigens, they prove beneficial for the host by exerting regulatory functions. In allergic manifestations, in autoimmune diseases and especially during pregnancy, despite the fact that the antigens responsible for the process are foreign to the host, they also perform beneficial activity. During pregnancy, the placenta secretes molecules or factors that regulate the synthesis of these antibodies, thus favoring fetal protection.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Antigens / immunology
  • Female
  • Glycosylation
  • Humans
  • Immunoglobulin G / chemistry
  • Immunoglobulin G / immunology*
  • Precipitin Tests
  • Pregnancy

Substances

  • Antigens
  • Immunoglobulin G