Immunoglobulin G
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IgG is a monomeric immunoglobulin, built of two heavy chains γ and two light chains. Each molecule has two antigen binding sites. This is the most abundant immunoglobulin and is approximately equally distributed in blood and in tissue liquids, constituting 75% of serum immunoglobulins in humans<ref>Junqueira, Luiz C., Jose Carneiro (2003). Basic Histology. McGraw-Hill. ISBN 0-07-141365.</ref>. This is the only isotype that can pass through the placenta, thereby providing protection to the fetus in its first weeks of life before its own immune system has developed. It can bind to many kinds of pathogens, for example viruses, bacteria, and fungi, and protects the body against them by complement activation (classic pathway), opsonization for phagocytosis and neutralisation of their toxins. There are 4 subclasses: IgG1 (66%), IgG2 (23%), IgG3 (7%) and IgG4 (4%).
- IgG1, IgG3 and IgG4 cross the placenta easily.
- IgG3 is the most effective complement activator, followed by IgG1 and then IgG2. IgG4 does not activate complement.
- IgG1 and IgG3 bind with high affinity to Fc receptors on phagocytic cells. IgG4 has intermediate affinity and IgG2 affinity is extremely low.
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| Immune system proteins - edit |
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| MAC complex | Nanobodies | Perforin | Antibodies |
