Abstract
The remarkable evolutionary advantage of T and B lymphocytes as a defense mechanism is their ability to specifically recognize millions of different microbes, including some that may not yet even exist. The genes that encode T and B cell receptors and as antibodies that are the soluble form of the B cell receptors, are arranged unlike any other genes in the body. The process of generating the receptors includes somatic recombination of different segments of DNA, the addition or subtraction of nucleotides during the process (junctional diversity), and pairing of different chains of the receptors (combinatorial diversity). The B cell receptor and the corresponding antibody can further diversify by changing their constant domains in a process called isotype switching so that there are five possible isotypes (IgM, IgD, IgG, IgA, and IgE). While the B cell receptor binds a variety of antigens as ligands, the T cell receptor binds to peptides presented on the cell surface by proteins of the major histocompatibility complex (MHC), named HLA proteins in humans. One advantage of the MHC system is that CD8 killer T cells can recognize and destroy host cells infected by an intracellular pathogen because peptides from pathogen proteins are brought to the cell surface by HLA proteins as a type of “flag.” In order for a population of diverse individuals to have the potential to survive an epidemic, the HLA proteins are highly polymorphic so that at least some individuals will be able to present peptides from pathogen proteins and mount an effective immune response. Because the process of generating T and B cell receptors is random, it is important to eliminate cells with receptors recognizing self-antigens. This process is called central tolerance.
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Kavathas, P.B., Krause, P.J., Ruddle, N.H. (2019). Adaptive Immunity: Antigen Recognition by T and B Lymphocytes. In: Krause, P., Kavathas, P., Ruddle, N. (eds) Immunoepidemiology. Springer, Cham. https://doi.org/10.1007/978-3-030-25553-4_4
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