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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 part of the antigen that immunoglobulin or antibodies bind to is called a B-cell epitope. [11] B cell epitopes can be divided into two groups: conformational or linear. [11] B cell epitopes are mainly conformational. [12] [13] There are additional epitope types when the quaternary structure is considered. [13]
To test the efficacy in which TMEV uses molecular mimicry to its advantage, a sequence of the human myelin-specific epitope was inserted into a non-pathogenic TMEV variant. As a result, there was a CD4 + T cell response and autoimmune demyelination was initiated by infection with a TMEV peptide ligand. [ 20 ]
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).
T cell epitope content is one of the factors that contributes to antigenicity. 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 ...
Acquired immunity depends upon the interaction between antigens and a group of proteins called antibodies produced by B cells of the blood. There are many antibodies and each is specific for a particular type of antigen. Thus immune response in acquired immunity is due to the precise binding of antigens to antibody.
As IgM antibodies are expressed early in a B cell response, they are rarely highly mutated and have broad antigen reactivity thus providing an early response to a wide range of antigens without the need for T cell help. [5] IgD isotypes are expressed on naive B cells as they leave bone marrow and populate secondary lymphoid organs.
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.