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In alloimmunity, the body creates antibodies (called alloantibodies) against the alloantigens, attacking transfused blood, allotransplanted tissue, and even the fetus in some cases. Alloimmune ( isoimmune ) response results in graft rejection , which is manifested as deterioration or complete loss of graft function.
The structure of immunoglobulin polypeptide chain is dictated and controlled by number of genes encoded in the germ line. [2] However, these genes, as it was discovered by serologic and chemical methods, could be highly polymorphic. This polymorphism is subsequently projected to the overall amino acid structure of antibody chains.
Isoantibodies, formerly called alloantibodies, are antibodies produced by an individual against isoantigens produced by members of the same species. In the case of the species Homo sapiens, for example, there are a significant number of antigens that are different in every individual. When antigens from another individual are introduced into ...
Characteristics of clinically significant alloantibodies include: immunoglobulin G antibody subclass, reactivity at body temperature, and ability to cause red blood cell agglutination in the presence of anti-human globulin (AHG) in an indirect antiglobulin test. [4] Sometimes, clinical significance of an antibody can be difficult to determine. [6]
The technology can uniquely identify a person by analyzing the antibodies in body fluids. A unique, individual set of antibodies, called individual specific autoantibodies (ISA), is found in blood, serum, saliva, urine, semen, perspiration, tears, and body tissues, and the antibodies are not affected by illness, medication, or food/drug intake.
The "upper" part of an antibody. The complementarity-determining regions of the heavy chain are shown in red (Complementarity-determining regions (CDRs) are polypeptide segments of the variable chains in immunoglobulins (antibodies) and T cell receptors, generated by B-cells and T-cells respectively. CDRs are where these molecules bind to their ...
Class switching occurs after activation of a mature B cell via its membrane-bound antibody molecule (or B cell receptor) to generate the different classes of antibody, all with the same variable domains as the original antibody generated in the immature B cell during the process of V(D)J recombination, but possessing distinct constant domains in their heavy chains.
IgA antibodies are secreted in the respiratory or the intestinal tract and act as the main mediators of mucosal immunity. [13] They are monomeric in the serum, but appear as a dimer termed secretory IgA (sIgA) at mucosal surfaces. The secretory IgA is associated with a J-chain and another polypeptide chain called the secretory component. [14]