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The first epitope-based vaccine was developed in 1985 by Jacob et al. [28] Epitope-based vaccines stimulate humoral and cellular immune responses using isolated B-cell or T-cell epitopes. [28] [22] [17] These vaccines can use multiple epitopes to increase their efficacy. [28] To find epitopes to use for the vaccine, in silico mapping is often ...
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).
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 major histocompatibility complex (MHC) is a large locus on vertebrate DNA containing a set of closely linked polymorphic genes that code for cell surface proteins essential for the adaptive immune system. These cell surface proteins are called MHC molecules. Its name comes from its discovery during the study of transplanted tissue ...
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]
On a molecular scale, the proteins are relatively large, so they cannot be recognized as a whole; instead, their segments, called epitopes, can be recognized. [1] An epitope comes in contact with a very small region (of 15–22 amino acids) of the antibody molecule; this region is known as the paratope. [1]
M protein is a virulence factor that can be produced by certain species of Streptococcus. [1] Viruses, parasites and bacteria are covered in protein and sugar molecules that help them gain entry into a host by counteracting the host's defenses. One such molecule is the M protein produced by certain streptococcal bacteria.
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.