What is IgG Antibodies

Immunoglobulin G (IgG) is a monomeric immunoglobulin, built of two heavy chains γ and two light chains. Each IgG has two antigen binding sites. It is the most abundant immunoglobulin and is approximately equally distributed in blood and in tissue liquids, constituting 75% of serum immunoglobulins in humans. IgG molecules are synthesised and secreted by plasma B cells.


IgG antibodies are predominately involved in the secondary antibody response, (the main antibody involved in primary response is IgM) which occurs approximately one month following antigen recognition, thus the presence of specific IgG generally corresponds to maturation of the antibody response. Pro-inflammatory cytokines particularly IL-4 and IL-2, have a crucial role in activation of the IgG antibody response.

This is the only isotype that can pass through the human placenta, thereby providing protection to the fetus in utero. Along with IgA secreted in the breast milk, residual IgG absorbed through the placenta provides the neonate with humoral immunity before its own immune system develops.

It can bind to many kinds of pathogens, for example viruses, bacteria, and fungi, and protects the body against them by agglutination and immobilization, complement activation (classical pathway), opsonization for phagocytosis and neutralization of their toxins. It also plays an important role in Antibody-dependent cell-mediated cytotoxicity(ADCC).

IgG is also associated with Type II and Type III Hypersensitivity.

IgG antibodies are large molecules of about 150 kDa composed of 4 peptide chains. It contains 2 identical heavy chains of about 50 kDa and 2 identical light chains of about 25 kDa, thus tetrameric quaternary structure. The two heavy chains are linked to each other and to a light chain each by disulfide bonds. The resulting tetramer has two identical halves which together form the Y-like shape. Each end of the fork contains an identical antigen binding site.


In humans, the three receptors for IgG are:
  • FcγRI (CD64) – 72kDa in size. Expressed on cells of mononuclear phagocyte lineage.
  • FcγRII (CD32) – 40kDa in size. Has 2 forms, alpha (with an ITAM receptor motif) and beta (with an ITIM receptor motif).
  • FcγRIII (CD16) – 50-80kDa in size. Has 2 forms, alpha (a transmembrane protein) and beta (expressed on neutrophils).

Glycosylation is essential for IgG binding to its receptors, regardless of its class

"Immunoglobulin G." Wikipedia, The Free Encyclopedia. 13 Jun 2009, 07:45 UTC. 13 Jun 2009 <http://en.wikipedia.org/w/index.php?title=Immunoglobulin_G&oldid=296129750>. 

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