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| An Epitope is the part of a macromolecule that is recognized by the immune system, specifically by antibodies, or T cells. Although epitope are usually thought to be derived from non self proteins, sequences derived from the host that can be recognized are also classified as epitope. |
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Paratope |
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Most epitope recognized by antibodies or B cells can be thought of as three-dimensional surface features of an antigen molecule; these features fit precisely and thus bind to antibodies. The part of an antibody that recognizes the epitope is called a paratope. Exceptions are linear epitope, which are determined by the amino acid sequence (the primary structure) rather than by the 3D shape (tertiary structure) of a protein. |
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Antigen-Presenting Cell |
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T cell epitope are presented on the surface of an antigen-presenting cell, where they are bound to molecules. T cell epitope presented by MHC class I molecules are typically peptides between 8 and 11 amino acid in lengths, while MHC class II molecules present longer peptides, and non-classical MHC molecules also present non-peptidic epitope such as glycolipids. Epitope can be mapped using protein micro arrays, and with the ELISPOT or ELISA techniques. Genetic sequences coding for epitope that are recognised by common antibodies can be fused to genes, thus aiding further molecular characterization of the gene product. Common epitope used for this purpose are c-myc, HA, FLAG, V5.
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