|Title||αβ T cell receptors that do not undergo major histocompatibility complex-specific thymic selection possess antibody-like recognition specificities.|
|Publication Type||Journal Article|
|Year of Publication||2012|
|Authors||Tikhonova, AN, Van Laethem, F, Hanada, K-ichi, Lu, J, Pobezinsky, LA, Hong, C, Guinter, TI, Jeurling, SK, Bernhardt, G, Park, J-H, Yang, JC, Sun, PD, Singer, A|
|Date Published||2012 Jan 27|
|Keywords||Amino Acid Sequence, Animals, Antibody Specificity, Epitopes, T-Lymphocyte, Gene Deletion, Ligands, Major Histocompatibility Complex, Mice, Molecular Sequence Data, Protein Binding, Receptors, Antigen, T-Cell, alpha-beta, Receptors, Virus, T-Lymphocytes, Thymus Gland|
Major histocompatibility complex (MHC) restriction is the cardinal feature of T cell antigen recognition and is thought to be intrinsic to αβ T cell receptor (TCR) structure because of germline-encoded residues that impose MHC specificity. Here, we analyzed αβTCRs from T cells that had not undergone MHC-specific thymic selection. Instead of recognizing peptide-MHC complexes, the two αβTCRs studied here resembled antibodies in recognizing glycosylation-dependent conformational epitopes on a native self-protein, CD155, and they did so with high affinity independently of MHC molecules. Ligand recognition was via the αβTCR combining site and involved the identical germline-encoded residues that have been thought to uniquely impose MHC specificity, demonstrating that these residues do not only promote MHC binding. This study demonstrates that, without MHC-specific thymic selection, αβTCRs can resemble antibodies in recognizing conformational epitopes on MHC-independent ligands.