αβ T Cell Receptors that Do Not Undergo Major Histocompatibility Complex-Specific Thymic Selection Possess Antibody-like Recognition Specificities
| Autor: | Anastasia N. Tikhonova, Terry I. Guinter, François Van Laethem, Susanna Jeurling, Jinghua Lu, Günter Bernhardt, Changwan Hong, Peter D. Sun, James Chih-Hsin Yang, Ken-ichi Hanada, Leonid A. Pobezinsky, Jung-Hyun Park, Alfred Singer |
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| Rok vydání: | 2012 |
| Předmět: |
Receptors
Antigen T-Cell alpha-beta T-Lymphocytes Molecular Sequence Data Immunology Epitopes T-Lymphocyte chemical and pharmacologic phenomena Thymus Gland Biology Ligands Major histocompatibility complex Article Epitope Major Histocompatibility Complex Mice Antibody Specificity Animals Immunology and Allergy Amino Acid Sequence CD155 Receptor T-cell receptor MHC restriction Molecular biology Cell biology Infectious Diseases biology.protein Receptors Virus Antibody Gene Deletion CD8 Protein Binding |
| Zdroj: | Immunity. 36:79-91 |
| ISSN: | 1074-7613 |
| Popis: | Summary 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. |
| Databáze: | OpenAIRE |
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