Search results
Results from the WOW.Com Content Network
Antigen can originate either from within the body ("self-protein" or "self antigens") or from the external environment ("non-self"). [2] The immune system identifies and attacks "non-self" external antigens. Antibodies usually do not react with self-antigens due to negative selection of T cells in the thymus and B cells in the bone marrow. [5]
An antibody is made up of two heavy chains and two light chains. The unique variable region allows an antibody to recognize its matching antigen. [73] A B cell identifies pathogens when antibodies on its surface bind to a specific foreign antigen. [74] This antigen/antibody complex is taken up by the B cell and processed by proteolysis into ...
Each antibody binds to a specific antigen in a highly specific interaction analogous to a lock and key.. An antibody (Ab) or immunoglobulin (Ig) is a large, Y-shaped protein belonging to the immunoglobulin superfamily which is used by the immune system to identify and neutralize antigens such as bacteria and viruses, including those that cause disease.
Antigen processing, or the cytosolic pathway, is an immunological process that prepares antigens for presentation to special cells of the immune system called T lymphocytes. It is considered to be a stage of antigen presentation pathways.
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]
Secondary antibodies bind to primary antibodies, which are directly bound to the target antigen(s). In immunolabeling, the primary antibody's Fab domain binds to an antigen and exposes its Fc domain to secondary antibody. Then, the secondary antibody's Fab domain binds to the primary antibody's Fc domain.
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.
Class switching is mediated by the enzyme AID (activation-induced cytidine deaminase) and occurs after the B cell binds an antigen through its B cell receptor. Class-switching usually requires interaction with a T helper cell. [3] [4] In humans, there are five heavy chain isotypes α,δ,γ,ε,μ, corresponding to five antibody isotypes: