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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 contrast, most antibodies recognize a conformational epitope that has a specific three-dimensional shape (tertiary structure).
Conformational and linear epitopes interact with the paratope based on the 3-D conformation adopted by the epitope, which is determined by the surface features of the involved epitope residues and the shape or tertiary structure of other segments of the antigen. A conformational epitope is formed by the 3-D conformation adopted by the ...
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.
This technique can be used to map both linear and conformational epitopes but is labor-intensive and time-consuming, typically limiting analysis to a small number of amino-acid residues. [2] High-throughput shotgun mutagenesis epitope mapping. [2] [10] [30] Shotgun mutagenesis is a high-throughput approach for mapping the epitopes of mAbs. [30]
Such epitopes are known as conformational epitopes and tend to be longer (15–22 amino acid residues) than the linear epitopes. [1] Likewise, the antibodies produced by the plasma cells belonging to the same clone would bind to the same conformational epitopes on the pathogen proteins. [12] [13] [14] [15]
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Either the linear amino acid sequence or the conformational fit of the immunodominant epitope may be shared between the pathogen and host. This is also known as "cross-reactivity" between self antigen of the host and immunodominant epitopes of the pathogen. An autoimmune response is then generated against the epitope.
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