| First Author | Tikhonova AN | Year | 2012 |
| Journal | Immunity | Volume | 36 |
| Issue | 1 | Pages | 79-91 |
| PubMed ID | 22209676 | Mgi Jnum | J:180750 |
| Mgi Id | MGI:5307174 | Doi | 10.1016/j.immuni.2011.11.013 |
| Citation | Tikhonova AN, et al. (2012) alphabeta T Cell Receptors that Do Not Undergo Major Histocompatibility Complex-Specific Thymic Selection Possess Antibody-like Recognition Specificities. Immunity 36(1):79-91 |
| abstractText | Major histocompatibility complex (MHC) restriction is the cardinal feature of T cell antigen recognition and is thought to be intrinsic to alphabeta T cell receptor (TCR) structure because of germline-encoded residues that impose MHC specificity. Here, we analyzed alphabetaTCRs from T cells that had not undergone MHC-specific thymic selection. Instead of recognizing peptide-MHC complexes, the two alphabetaTCRs 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 alphabetaTCR 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, alphabetaTCRs can resemble antibodies in recognizing conformational epitopes on MHC-independent ligands. |
