A cluster of mutations in HLA-A2 alpha 2 helix abolishes peptide recognition by T cells.
In order to investigate the regions of HLA-A2 that control peptide-specific cytotoxic T lymphocyte (CTL) recognition, 37 HLA-A2 genes coding for 50 point mutations that span the alpha 2 helix were synthesized by the technique of saturation mutagenesis. Twenty-nine of these genes, which code for 41 p...
| Hoofdauteurs: | , , , , |
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| Formaat: | Journal article |
| Taal: | English |
| Gepubliceerd in: |
1991
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| _version_ | 1826299089885593600 |
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| author | Moots, R Matsui, M Pazmany, L Mcmichael, A Frelinger, J |
| author_facet | Moots, R Matsui, M Pazmany, L Mcmichael, A Frelinger, J |
| author_sort | Moots, R |
| collection | OXFORD |
| description | In order to investigate the regions of HLA-A2 that control peptide-specific cytotoxic T lymphocyte (CTL) recognition, 37 HLA-A2 genes coding for 50 point mutations that span the alpha 2 helix were synthesized by the technique of saturation mutagenesis. Twenty-nine of these genes, which code for 41 point mutations, were transfected into C1R cells and used as targets in cytotoxicity assays, in the presence of influenza-A matrix peptide 58-68 with specific CTL as effectors. All the transfectants were recognized fully by matrix peptide-specific CTL apart from those with amino acid substitutions at positions 152, 154, 155, 156, or 161, which led to a total loss of recognition and those with mutations at residue 27 or a double mutation at 138 and 150, which were recognized in an intermediate manner. The clustering of the crucial residues that emerges may reflect direct interaction of their side-chains with peptide or the CTL receptor. |
| first_indexed | 2024-03-07T04:56:37Z |
| format | Journal article |
| id | oxford-uuid:d6d20309-5802-4099-b68a-51fe32eb9cd4 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T04:56:37Z |
| publishDate | 1991 |
| record_format | dspace |
| spelling | oxford-uuid:d6d20309-5802-4099-b68a-51fe32eb9cd42022-03-27T08:36:27ZA cluster of mutations in HLA-A2 alpha 2 helix abolishes peptide recognition by T cells.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:d6d20309-5802-4099-b68a-51fe32eb9cd4EnglishSymplectic Elements at Oxford1991Moots, RMatsui, MPazmany, LMcmichael, AFrelinger, JIn order to investigate the regions of HLA-A2 that control peptide-specific cytotoxic T lymphocyte (CTL) recognition, 37 HLA-A2 genes coding for 50 point mutations that span the alpha 2 helix were synthesized by the technique of saturation mutagenesis. Twenty-nine of these genes, which code for 41 point mutations, were transfected into C1R cells and used as targets in cytotoxicity assays, in the presence of influenza-A matrix peptide 58-68 with specific CTL as effectors. All the transfectants were recognized fully by matrix peptide-specific CTL apart from those with amino acid substitutions at positions 152, 154, 155, 156, or 161, which led to a total loss of recognition and those with mutations at residue 27 or a double mutation at 138 and 150, which were recognized in an intermediate manner. The clustering of the crucial residues that emerges may reflect direct interaction of their side-chains with peptide or the CTL receptor. |
| spellingShingle | Moots, R Matsui, M Pazmany, L Mcmichael, A Frelinger, J A cluster of mutations in HLA-A2 alpha 2 helix abolishes peptide recognition by T cells. |
| title | A cluster of mutations in HLA-A2 alpha 2 helix abolishes peptide recognition by T cells. |
| title_full | A cluster of mutations in HLA-A2 alpha 2 helix abolishes peptide recognition by T cells. |
| title_fullStr | A cluster of mutations in HLA-A2 alpha 2 helix abolishes peptide recognition by T cells. |
| title_full_unstemmed | A cluster of mutations in HLA-A2 alpha 2 helix abolishes peptide recognition by T cells. |
| title_short | A cluster of mutations in HLA-A2 alpha 2 helix abolishes peptide recognition by T cells. |
| title_sort | cluster of mutations in hla a2 alpha 2 helix abolishes peptide recognition by t cells |
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