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In immunology, epitope mapping is the process of experimentally identifying the binding site, or epitope, of an antibody on its target antigen (usually, on a protein). [ 1 ] [ 2 ] [ 3 ] Identification and characterization of antibody binding sites aid in the discovery and development of new therapeutics , vaccines , and diagnostics .
The purported mechanism of action is the cleavage of peptides that mask the epitope, thereby restoring antigenicity. Disadvantages of enzyme digestion include a low success rate for restoring immunoreactivity and the potential destruction of tissue morphology and the antigen of interest.
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 .
A cryptotope is an antigenic site or epitope hidden in a protein or virion by surface subunits. Cryptotopes are antigenically active only after the dissociation of protein aggregates and virions. [1] Some infectious pathogens are known to escape immunological targeting by B-cells by masking antigen-binding sites as cryptotopes. [2]
Epitope binning is a competitive immunoassay used to characterize and then sort a library of monoclonal antibodies against a target protein. [1] Antibodies against a similar target are tested against all other antibodies in the library in a pairwise fashion to see if antibodies block one another's binding to the epitope of an antigen . [ 2 ]
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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]
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