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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 .
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 .
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).
Note how the segments widely separated in the primary structure have come in contact in the three-dimensional tertiary structure forming part of the same epitope [1] In immunology, a conformational epitope is a sequence of sub-units (usually amino acids) composing an antigen that come in direct contact with a receptor of the immune system.
Likewise, T Cell epitopes can cause unwanted immunogenicity, including the development of ADAs. A key determinant in T cell epitope immunogenicity is the binding strength of T cell epitopes to major histocompatibility complexes (MHC or HLA) molecules. Epitopes with higher binding affinities are more likely to be displayed on the surface of a cell.
An epitope that can be attacked by many different B cells is said to be highly immunogenic. In these cases, the binding affinities for respective epitope-paratope pairs vary, with some B cell clones producing antibodies that bind strongly to the epitope, and others producing antibodies that bind weakly. [1]
The first use of epitope tagging was described by Munro and Pelham in 1984. [4] The FLAG-tag was the second example of a fully functional, improved epitope tag, published in the scientific literature. [1] [5] [6] and was the only epitope tag to be patented. [7] [8] It has since become one of the most commonly used protein tags in laboratories ...
A well-known example of a hapten is urushiol, which is the toxin found in poison ivy. When absorbed through the skin from a poison ivy plant, urushiol undergoes oxidation in the skin cells to generate the actual hapten, a reactive quinone -type molecule, which then reacts with skin proteins to form hapten adducts.