Asymmetric selection of T cell antigen receptor alpha- and beta-chains in HLA-B27 alloreactivity
| Autor: | pilar lauzurica, Bragado R, López D, Galocha B, Ja, López Castro |
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| Rok vydání: | 1992 |
| Předmět: |
Base Sequence
Oligodeoxyribonucleotides Receptors Antigen T-Cell alpha-beta Immunology Molecular Sequence Data Immunology and Allergy Humans Amino Acid Sequence Gene Rearrangement beta-Chain T-Cell Antigen Receptor Gene Rearrangement alpha-Chain T-Cell Antigen Receptor Polymerase Chain Reaction HLA-B27 Antigen T-Lymphocytes Cytotoxic |
| Zdroj: | Europe PubMed Central |
| ISSN: | 0022-1767 |
| Popis: | Endogenous peptides constitutively bind to class I MHC Ag and are thought to be integral parts of allospecific T cell epitopes. However, allospecific TCR can recognize structural features of the alloantigen as foreign. To define some crucial parameters determining HLA-B27 allorecognition, the structure of TCR alpha- and beta-chains from HLA-B27-specific CTL was analyzed. A strategy, based on V alpha and V beta family-specific oligonucleotides, was used for specific amplification and direct sequencing of TCR-alpha and -beta cDNA. We observed nonrandom usage of V beta segments and recurrent structural motifs within beta-chain junctional regions. In contrast, no structural restrictions were apparent among alpha-chains, even from CTL clones of related fine specificity. These results indicate an asymmetric contribution of TCR alpha- and beta-chains to HLA-B27 allospecificity among the CTL clones analyzed. They suggest recognition of multiple peptides and involvement of beta-chain junctional regions in recognizing shared motifs among some of these peptides. |
| Databáze: | OpenAIRE |
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