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Antigen-antibody interaction, or antigen-antibody reaction, is a specific chemical interaction between antibodies produced by B cells of the white blood cells and antigens during immune reaction. The antigens and antibodies combine by a process called agglutination.
Each antibody binds to a specific antigen in a highly specific interaction analogous to a lock and key.. An antibody (Ab) or immunoglobulin (Ig) is a large, Y-shaped protein belonging to the immunoglobulin superfamily which is used by the immune system to identify and neutralize antigens such as bacteria and viruses, including those that cause disease.
An illustration that shows how antigens induce the immune system response by interacting with an antibody that matches the molecular structure of an antigen. In immunology, an antigen (Ag) is a molecule, moiety, foreign particulate matter, or an allergen, such as pollen, that can bind to a specific antibody or T-cell receptor. [1]
The IgG, IgE and IgA antibody isotypes are generated following class-switching during germinal centre reaction and provide different effector functions in response to specific antigens. IgG is the most abundant antibody class in the serum and it is divided into 4 subclasses based on differences in the structure of the constant region genes and ...
There are three basic variants of immunoglobulin antigens in humans that share a very similar chemical structure but are distinctly different. Red circles show where there are differences in chemical structure in the antigen-binding site (sometimes called the antibody-combining site) of human immunoglobulin.
In immunology, cross-reactivity has a more narrow meaning of the reaction between an antibody and an antigen that differs from the immunogen. It is sometimes also referred to as cross-immunity or cross-protective immunity, [2] although cross-reactivity does not necessarily confer cross-protection. In some cases, the cross-reactivity can be ...
A single antibody molecule has two antigen receptors and therefore contains twelve CDRs total. There are three CDR loops per variable domain in antibodies. Sixty CDRs can be found on a pentameric IgM molecule, which is composed of five antibodies and has increased avidity as a result of the collective affinity of all antigen-binding sites combined.
The antibodies created against these environmental antigens in the first years of life can cross react with ABO-incompatible red blood cells when it comes in contact with during blood transfusion later in life. Anti-A and anti-B antibodies are usually IgM type. O-type individuals can produce IgG-type ABO antibodies.
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