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immunoglobulin

An immunoglobulin, also known as an antibody, is a large Y-shaped protein used by the immune system to identify and neutralize foreign objects such as bacteria and viruses.

The antibody recognizes a unique part of the foreign target, termed an antigen. Each tip of the "Y" of an antibody contains a paratope (a structure 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). The production of antibodies is the main function of the humoral immune system.

Immonoglobulin can come in different varieties known as isotypes or classes. In placental mammals there are five antibody isotypes known as IgA, IgD, IgE, IgG and IgM. They are each named with an "Ig" prefix that stands for immunoglobulin, another name for antibody, and differ in their biological properties, functional locations and ability to deal with different antigens, as depicted in the table.





Schematic representation of the structure of immunoglobulin.


Vnější zdroje:




CEBIO

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  • Envisan Gem
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  • Jihočeská univerzita
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