Immunoglobulins Structure and Function /Antibody Structure Types and Function

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Immunoglobulins/Antibody Structure Types and Function
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Antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shape protein produced by plasma cells that is used by the immune system to identify and neutralize pathogens such as bacteria and viruses. The antibody recognizes a unique molecule of the harmful agent, called an antigen, via the variable region
Each tip of the "Y" of an antibody contains a paratope (analogous to a lock) that is specific for one particular epitope (similarly analogous to a key) on an antigen, allowing these two structures to bind together with precision. Using this binding mechanism, an antibody can tag a microbe or an infected cell for attack by other parts of the immune system, or can neutralize its target directly (for example, by blocking a part of a microbe that is essential for its invasion and survival).
Antibodies are glycoproteins belonging to the immunoglobulin superfamily; ] the terms antibody and immunoglobulin are often used interchangeably. Though strictly speaking, an antibody is not the same as an immunoglobulin; B cells can produce two types of immunoglobulins - surface immunoglobulins, which are B cell receptors; and secreted immunoglobulins, which are antibodies. So antibodies are one of two classes of immunoglobulins.
Though the general structure of all antibodies is very similar, a small region at the tip of the protein is extremely variable, allowing millions of antibodies with slightly different tip structures, or antigen-binding sites, to exist. This region is known as the hypervariable region. Each of these variants can bind to a different antigen. This enormous diversity of antibody paratopes on the antigen-binding fragments allows the immune system to recognize an equally wide variety of antigens The large and diverse population of antibody paratope is generated by random recombination events of a set of gene segments that encode different antigen-binding sites (or paratopes), followed by random mutations in this area of the antibody gene, which create further diversity.[ This recombinational process that produces clonal antibody paratope diversity is called V(D)J or VJ recombination. Basically, the antibody paratope is polygenic, made up of three genes, V, D, and J. Each paratope locus is also polymorphic, such that during antibody production, one allele of V, one of D, and one of J is chosen. These gene segments are then joined together using random genetic recombination to produce the paratope. The regions where the genes are randomly recombined together is the hyper variable region used to recognise different antigens on a clonal basis.
IgA Found in mucosal areas, such as the gut, respiratory tract and urogenital tract, and prevents colonization by pathogens.[14] Also found in saliva, tears, and breast milk. Some antibodies form complexes that bind to multiple antigen molecules.
IgD Functions mainly as an antigen receptor on B cells that have not been exposed to antigens. ] It has been shown to activate basophils and mast cells to produce antimicrobial factors.
IgE Binds to allergens and triggers histamine release from mast cells and basophils, and is involved in allergy. Also protects against parasitic worms
IgG In its four forms, provides the majority of antibody-based immunity against invading pathogens. The only antibody capable of crossing the placenta to give passive immunity to the fetus.
IgM Expressed on the surface of B cells (monomer) and in a secreted form (pentamer) with very high avidity. Eliminates pathogens in the early stages of B cell-mediated (humoral) immunity before there is sufficient IgG
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