The γδT Cell Receptor
Along with important conceptual similarities, there are also fundamental differences in structure and in the mode of operation of the antigen receptors on B and T cells. The B lymphocyte receptor is the immunoglobulin molecule. The large number of antibody molecules that can be produced by the organism result in part from somatic recombination of germ-line variable (V), diversity (D), joining (J), and constant (C) gene segments to form a contiguous (rearranged) gene, encoding an immunoglobulin polypeptide chain. Antibody diversity is extensive and is contributed by hundreds of V gene segments, dozens of D gene segments, and several J gene segments. The paired light and heavy chains of each antibody molecule form a unique site that is involved in the recognition of antigen; in turn, this unique site may be recognized by other antibodies as an idiotypic determinant. T cells differ from B cells in antigen recognition, because they often recognize different determinants, generally do not react with soluble or free antigen, and recognize antigen on the cell surface and only in conjunction with products encoded by self-major histocompatibility complex (MHC) genes. The 55 kDa species could be immunoprecipitated using antiserum made against synthetic peptides corresponding to the deduced amino acid sequence of a human TCR γ cDNA clone, suggesting that it was the elusive protein product of the TCR γ gene. The 40-kDa species failed to react with anti-TCR γ sera, and thus appeared to represent an additional component of the TCR γ–CD3 complex, which was termed “TCR δ.” © 1988, Academic Press, Inc.
Brenner, MB; Strominger, JL; Krangel, MS
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