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An epitope, also known as antigenic determinant, is the part of an antigen that is recognized by the immune system, specifically by antibodies, B cells, or T cells. The part of an antibody that binds to the epitope is called a paratope .
The uniqueness of a paratope allows it to bind to only one epitope with high affinity and as a result, each B cell can only respond to one epitope. The paratopes on B-cell receptors binding to their specific epitope is a critical step in the adaptive immune response .
Antibody-antigen interactions are highly specific and those that have high affinity will interact with increased bond strength and trigger downstream immune responses. The strength of the bond between the epitope of the antigen and the paratope of the antibody will determine the affinity of the interaction. [1]
The antigenic determinant or epitope is recognized by the paratope of the antibody, situated at the variable region of the polypeptide chain. The variable region in turn has hyper-variable regions which are unique amino acid sequences in each antibody.
He defined idiotype as the set of epitopes on the V region of an antibody molecule, where epitope means an antigenic determinant. He also defined the " paratope " to be that part of an antibody variable region that binds to an antigen.
Recognition of epitopes in a linear fashion. Note: the same (colored) segment of protein can be a part of more than one epitopes. In immunology, a linear epitope (also sequential epitope) is an epitope—a binding site on an antigen—that is recognized by antibodies by its linear sequence of amino acids (i.e. primary structure).
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The antibody's paratope interacts with the antigen's epitope. An antigen usually contains different epitopes along its surface arranged discontinuously, and dominant epitopes on a given antigen are called determinants. [citation needed] Antibody and antigen interact by spatial complementarity (lock and key).
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