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The water-accessible surface area of an IgG antibody. Immunoglobulin G (IgG) is a type of antibody. Representing approximately 75% of serum antibodies in humans, IgG is the most common type of antibody found in blood circulation. [1] IgG molecules are created and released by plasma B cells. Each IgG antibody has two paratopes.
IgG1 is present in the bloodstream at a percentage of about 60-70%, IgG2-20-30%, IgG3 about 5-8 %, and IgG4 1-3 %. IgG subclass deficiencies affect only IgG subclasses (usually IgG2 or IgG3), with normal total IgG and IgM immunoglobulins and other components of the immune system being at normal levels.
Despite the high sequence similarity (90% identical on the amino acid level), each subclass has a different half-life, a unique profile of antigen binding and distinct capacity for complement activation. IgG1 antibodies are the most abundant IgG class and dominate the responses to protein antigens.
Once set, light chain class remains fixed for the life of the B lymphocyte. In a healthy individual, the total kappa-to-lambda ratio is roughly 2:1 in serum (measuring intact whole antibodies) or 1:1.5 if measuring free light chains, with a highly divergent ratio indicative of neoplasm. The free light chain ratio ranges from 0.26 to 1.65. [1]
Antibody-mediated opsonisation (marking) of pathogens depends on high affinity paratope-epitope interactions. Immunoglobulins are highly effective opsonins, with the IgG subclasses IgG1 and IgG3 being recognised as the most efficacious opsonins in humans. [1] Antibodies structurally contain two important domains
The word allotype comes from two Greek roots, allo meaning 'other or differing from the norm' and typos meaning 'mark'. [1] In immunology , allotype is an immunoglobulin variation (in addition to isotypic variation) that can be found among antibody classes and is manifested by heterogeneity of immunoglobulins present in a single vertebrate species.
The main ligand is Protein G (prepared from Group C or G Streptococcus or by recombinant technology), which has high affinity for all four IgG subclasses. Another ReACT ligand is Protein A (from Group A Staphylococcus), which binds to IgG 1, 2, and 4. A study published in 2002 showed a loss of sensitivity for detecting significant antibodies.
Antibody (or immunoglobulin) structure is made up of two heavy-chains and two light-chains.These chains are held together by disulfide bonds.The arrangement or processes that put together different parts of this antibody molecule play important role in antibody diversity and production of different subclasses or classes of antibodies.
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