A role for the region encompassing the c'' strand of a TCR Vα domain in T cell activation events

Qadri, Ayub, Radu, Caius G., Thatte, Jayant, Cianga, Petru, Ober, Bertram T., Ober, Raimund J. and Ward, E. Sally (2000) A role for the region encompassing the c'' strand of a TCR Vα domain in T cell activation events. Journal of Immunology, 165 (2), 820-829.

Abstract

The distinct strand topology of TCR Vα domains results in a flatter surface in the region encompassing the c' strand than the corresponding region in Ig V domains. In the current study a possible role for this region in T cell activation has been investigated by inserting a potential glycosylation site at Vα residue 82. This residue is in proximity to the c'' strand and distal to the putative interaction site for cognate peptide:MHC ligand. An additional N-linked carbohydrate at this position would create a protrusion on the Vα domain surface, and this may interfere with TCR aggregation and/or recruitment of signaling molecules. The modified TCR has been expressed in transfected T cells, and the phenotype following stimulation has been compared with that of cells expressing the wild-type TCR. The mutation has significant effects on activation-induced cell death and TCR internalization, but, unexpectedly, does not affect IL-2 secretion. Furthermore, analyses with tetrameric, peptide:MHC class II complexes suggest that the mutation decreases the ability of the TCR to aggregate into a configuration compatible with avid binding by these multivalent ligands.

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Contributors

Author: Raimund J. Ober

Author: E. Sally Ward

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