Human T cell receptor-mediated recognition of HLA-E.
The HLA-E class Ib molecule presents hydrophobic peptides derived from the leader sequences of other class I molecules, constituting the ligands for CD94/NKG2 lectin-like receptors. Along the course of our studies on human CD94+ T cells, we characterized an alpha beta CD8+CD94/NKG2C+ CTL clone (K14)...
| Main Authors: | , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2002
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| _version_ | 1797064828975579136 |
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| author | García, P Llano, M de Heredia, AB Willberg, C Caparrós, E Aparicio, P Braud, V López-Botet, M |
| author_facet | García, P Llano, M de Heredia, AB Willberg, C Caparrós, E Aparicio, P Braud, V López-Botet, M |
| author_sort | García, P |
| collection | OXFORD |
| description | The HLA-E class Ib molecule presents hydrophobic peptides derived from the leader sequences of other class I molecules, constituting the ligands for CD94/NKG2 lectin-like receptors. Along the course of our studies on human CD94+ T cells, we characterized an alpha beta CD8+CD94/NKG2C+ CTL clone (K14). In cytolytic assays against the murine TAP-deficient RMA-S cells transfected with human beta2 microglobulin and HLA-E (RMA-S/HLA-E), loaded with different synthetic peptides, K14 displayed a pattern of specific recognition distinct to that observed in CD94/NKG2C+ NK clones tested in parallel. RMA-S/HLA-E cells loaded with some but not all HLA class I leader sequence peptides were efficiently recognized by K14 but not by CD94/NKG2C clones, andvice versa. Remarkably, K14 also reacted with HLA-E loaded with a peptide derived from the BZLF-1 Epstein-Barr virus protein. Anti-CD94 mAb did not prevent K14 cytotoxicity against RMA-S/HLA-E cells, whereas incubation with anti-clonotypic mAb specific for the K14 TCR markedly inhibited lysis. Soluble HLA-E tetramers refolded with different peptides (i.e. VMAPRTVLL, VMAPRTLIL, VMAPRTLFL) specifically stained K14 cells. HLA-E tetramer binding was minimally reduced by pretreatment with anti-CD94 mAb alone, but was completely prevented in combination with anti-clonotypic mAb. Altogether, the data unequivocally imply the generation of human T cells potentially recognizing through the alpha beta TCR HLA-E molecules that bind to class I- and virus-derived peptides. |
| first_indexed | 2024-03-06T21:19:58Z |
| format | Journal article |
| id | oxford-uuid:411fc583-7e8a-48e5-aa1a-80599e1d08f7 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T21:19:58Z |
| publishDate | 2002 |
| record_format | dspace |
| spelling | oxford-uuid:411fc583-7e8a-48e5-aa1a-80599e1d08f72022-03-26T14:41:41ZHuman T cell receptor-mediated recognition of HLA-E.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:411fc583-7e8a-48e5-aa1a-80599e1d08f7EnglishSymplectic Elements at Oxford2002García, PLlano, Mde Heredia, ABWillberg, CCaparrós, EAparicio, PBraud, VLópez-Botet, MThe HLA-E class Ib molecule presents hydrophobic peptides derived from the leader sequences of other class I molecules, constituting the ligands for CD94/NKG2 lectin-like receptors. Along the course of our studies on human CD94+ T cells, we characterized an alpha beta CD8+CD94/NKG2C+ CTL clone (K14). In cytolytic assays against the murine TAP-deficient RMA-S cells transfected with human beta2 microglobulin and HLA-E (RMA-S/HLA-E), loaded with different synthetic peptides, K14 displayed a pattern of specific recognition distinct to that observed in CD94/NKG2C+ NK clones tested in parallel. RMA-S/HLA-E cells loaded with some but not all HLA class I leader sequence peptides were efficiently recognized by K14 but not by CD94/NKG2C clones, andvice versa. Remarkably, K14 also reacted with HLA-E loaded with a peptide derived from the BZLF-1 Epstein-Barr virus protein. Anti-CD94 mAb did not prevent K14 cytotoxicity against RMA-S/HLA-E cells, whereas incubation with anti-clonotypic mAb specific for the K14 TCR markedly inhibited lysis. Soluble HLA-E tetramers refolded with different peptides (i.e. VMAPRTVLL, VMAPRTLIL, VMAPRTLFL) specifically stained K14 cells. HLA-E tetramer binding was minimally reduced by pretreatment with anti-CD94 mAb alone, but was completely prevented in combination with anti-clonotypic mAb. Altogether, the data unequivocally imply the generation of human T cells potentially recognizing through the alpha beta TCR HLA-E molecules that bind to class I- and virus-derived peptides. |
| spellingShingle | García, P Llano, M de Heredia, AB Willberg, C Caparrós, E Aparicio, P Braud, V López-Botet, M Human T cell receptor-mediated recognition of HLA-E. |
| title | Human T cell receptor-mediated recognition of HLA-E. |
| title_full | Human T cell receptor-mediated recognition of HLA-E. |
| title_fullStr | Human T cell receptor-mediated recognition of HLA-E. |
| title_full_unstemmed | Human T cell receptor-mediated recognition of HLA-E. |
| title_short | Human T cell receptor-mediated recognition of HLA-E. |
| title_sort | human t cell receptor mediated recognition of hla e |
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