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.
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.
|Name||Percent||Crosses placenta easily||Complement activator||Binds to Fc receptors on phagocytic cells|
|IgG1||66%||yes||second highest||high affinity|
|IgG2||23%||no||third highest||extremely low affinity|
Note: IgG affinity to Fc receptors on phagocytic cells is specific to individual species from which the antibody comes as well as the class. The structure of the hinge regions gives each of the 4 IgG classes their unique biological profile. Even though there is about 95% similarity between their Fc regions, the structure of the hinge regions are relatively different.
Glycosylation is essential for IgG binding to its receptors, regardless of its class.
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