Glycosylation of the T-cell antigen-specific receptor and its potential role in lectin-mediated cytotoxicity.

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Abstract
Cytotoxic T lymphocytes (CTLs) normally destroy only those cells ("target cells") whose surface antigens they recognize. However, in the presence of lectins such as Con A, CTLs destroy virtually any cell, regardless of its antigens. The oligosaccharide of the T-cell antigen-specific receptor, a dimeric surface glycoprotein composed of disulfide-linked .alpha. and .beta. subunits, are of interest because of their potential involvement in this lectin-dependent cytotoxic activity. We report here that three or four asparagine-linked oligosaccharides could be enzymatically removed from each of the receptor subunits expressed by a cloned line of murine CTLs (clone 2C), consistent with the presence of glycosylation sites deduced from cDNA sequences of the .alpha. and .beta. genes expressed in this clone. All the N-linked glycans on the .beta. subunit were of the complex type (i.e., resistant to endoglycosidase H), but the .beta. subunit carried two or three endoglycosidase H-sensitive (high-mannose) oligosaccharides. High-mannose glycans can bind tightly to Con A and, indeed, this lectin was found to bind specifically to solubilized 2C T-cell receptor. The Con A-dependent cytotoxic activity of clone 2C, but not of other CTL clones, was inhibited by a monoclonal antibody (1B2) that is specific for the T-cell receptor of clone 2C. Antibody 1B2 also inhibited clone 2C cytotoxicity mediated by phytohemagglutinin, lentil-lectin, and wheat-germ agglutinin. These results suggest that, although lectin-dependent lysis of target cells by CTLs is antigen nonspecific, the cytolytic activity can be triggered by binding of the lectin to the T-cell antigen-specific receptor.