Search results
Results From The WOW.Com Content Network
The Immune Epitope Database and Analysis Resource (IEDB) is a project hosted by scientists at the La Jolla Institute for Allergy and Immunology (LIAI), with support from the National Institute of Allergy and Infectious Diseases (NIAID), a part of the National Institutes of Health [permanent dead link ] (NIH), and Department of Health and Human Services (HHS).
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 .
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.
The idiotype is based upon the variable region (labeled VL and VH in the diagram.) In immunology, an idiotype is a shared characteristic between a group of immunoglobulin or T-cell receptor (TCR) molecules based upon the antigen binding specificity and therefore structure of their variable region.
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).
Immunodominance is the immunological phenomenon in which immune responses are mounted against only a few of the antigenic peptides out of the many produced. [1] That is, despite multiple allelic variations of MHC molecules and multiple peptides presented on antigen presenting cells, the immune response is skewed to only specific combinations of the two. [1]
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]
MHC class I and II epitopes can be reliably predicted by computational means alone, [14] although not all in-silico T cell epitope prediction algorithms are equivalent in their accuracy. [15] There are two main methods of predicting peptide-MHC binding: data-driven and structure-based. [11]