Searching for MHC-Restricted Antibodies: Antibodies Induced by Injections with Syngeneic Cells Coated with Sendai Virus, Trinitrophenyl, and Xenogeneic β2-Microglobulin Are Not Restricted by the Mouse MHC
The capacity of the immune system to discriminate among an enormous number of different antigens is mediated by two distinct but interactive subpopulations of lymphocytes, B and T cells. These subpopulations differ profoundly in the way they recognize foreign antigens. B cells use immunoglobulins (lg) as cell surface receptors for recognition of free antigen whereas the lg-Iike receptors on T cells (TcR) recognize foreign antigens presented by their own major histocompatibility complex (MHC) gene products, a phenomenon known as MHC restriction (Zinkernagel and Doherty 1979). Another major difference exists between the structure and recognition of lg and the TcR. Immunoglobulins are composed of two heavy and light chain disulfide-Iinked hetrodimers while one set of disulfide-linked α- and β-glycoproteins forms the functional TcR (Kappler et al. 1983). The genomic organization of the genes for B (Tonegawa 1983; Honjo 1983) and T (Gascoigne et al. 1984; Hayday et al. 1985) cell receptors are similar and it is likely that the gene families originate from the same ancestral gene (Hood et al. 1985). Recently, it has been suggested that the T cell αβ receptor molecule has an antigen specific binding site that is fundamentally not different from the conventional binding site on antibodies (Novotny et al. 1986). The structural basis for the difference in the mode of antigen recognition between B and T cells might therefore be in the structure of the antigen that is recognized. Thus while the epitopes that occupy the binding sites of immunoglobulins are derived entirely from the antigen, the epitopes recognized by T cell receptors may be derived in part from the nominal antigen and in part from the restricting MHC molecule and can be seen as a neodeterminant.
KeywordsLeukemia Influenza Polypeptide Prep Allo
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