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Antibodies bind antigens with high specificity through paratopes formed by variable-region CDRs that recognize specific epitopes.
An antibody (immunoglobulin) is a large immune-system protein that identifies and neutralizes specific antigens (molecules on bacteria, viruses, or infected cells). Each antibody molecule has one or more highly specific antigen-binding sites located at the tips of its “Y”-shaped structure. These binding sites recognize particular antigen features called epitopes, in a precise “lock-and-key” style interaction. Antigen specificity comes from the variable regions of the antibody, especially the complementarity-determining regions (CDRs), which form the paratope (the actual antigen-binding surface). The immune system generates vast diversity of these binding regions through processes such as V(D)J recombination, somatic hypermutation, and affinity maturation, producing antibodies with different paratopes and therefore different antigen specificities. Antibodies can also be classified by how many targets they recognize (e.g., monospecific, bispecific, or polyvalent/unspecific), and by whether they are secreted or membrane-bound (as part of the B cell receptor).
Antibodies bind antigens with high specificity through paratopes formed by variable-region CDRs that recognize specific epitopes.
Antigen specificity is generated and refined by V(D)J recombination, somatic hypermutation, and affinity maturation, creating a diverse antibody repertoire.
Antibody specificity can be described by target number (monospecific, bispecific, polyvalent/unspecific) and by antibody format (secreted antibodies vs membrane-bound B cell receptors).
A large immunoglobulin protein produced by the immune system that binds specific antigens to help identify, tag, or neutralize them.
A molecule (often on pathogens or infected cells) that can be recognized by antibodies.
The ability of an antibody to recognize a particular antigen or epitope with high selectivity.
A specific part of an antigen that is recognized and bound by an antibody’s paratope.
The antigen-binding site on an antibody, formed by the CDRs, that directly contacts an epitope.
Hypervariable loops in the antibody variable region that determine the shape and chemistry of antigen binding.
A genetic rearrangement process that creates unique antibody variable regions by combining V, D, and J gene segments.
A process in activated B cells that introduces point mutations into antibody variable-region genes to increase diversity.
The selection-driven process that increases the average binding strength of antibodies for their antigen over time.
An antibody that has specificity for a single antigen or epitope.
An antibody that can bind two different antigens or two different epitopes on the same antigen.
A group of antibodies that can bind various antigens or microorganisms rather than a single target.
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