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Although epitopes are usually non-self proteins, sequences derived from the host that can be recognized (as in the case of autoimmune diseases) are also epitopes. [ 1 ] The epitopes of protein antigens are divided into two categories, conformational epitopes and linear epitopes , based on their structure and interaction with the paratope. [ 2 ]
In immunology, an idiotope is the unique set of antigenic determinants (epitopes) of the variable portion of an antibody. [1] In some cases it can be the actual antigen-binding site, and in some cases it may comprise variable region sequences outside of the antigen-binding site on the antibody itself.
Note that conformational epitopes can include some linear segments. B-cell epitope mapping studies suggest that most interactions between antigens and antibodies, particularly autoantibodies and protective antibodies (e.g., in vaccines), rely on binding to discontinuous epitopes. [citation needed]
An illustration that shows how antigens induce the immune system response by interacting with an antibody that matches the molecular structure of an antigen. In immunology, an antigen (Ag) is a molecule, moiety, foreign particulate matter, or an allergen, such as pollen, that can bind to a specific antibody or T-cell receptor. [1]
An antibody can be called monospecific if it has specificity for a single antigen or epitope, [74] or bispecific if it has affinity for two different antigens or two different epitopes on the same antigen. [75] A group of antibodies can be called polyvalent (or unspecific) if they have affinity for various antigens [76] or microorganisms. [76]
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).
Such discontinuous amino acids that come together in three-dimensional conformation and interact with the receptor's paratope are called conformational epitopes. In contrast, if the antigen is digested, small segments called peptides are formed, which bind with major histocompatibility complex molecules, and then later with T cell receptors ...
However, many naturally occurring apparent antigens are actually a mixture of macromolecules (for example, from pathogens, toxins, proteins, or pollen) comprising several epitopes. Contact with a complex antigen such as a virus will stimulate multiple immune responses to the virus' different macromolecules as well as the individual epitopes of ...
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