An HLA-B35-restricted epitope modified at an anchor residue results in an antagonist peptide.
Peptides associated with HLA-B35 commonly have a proline or occasionally a serine residue in the P2 anchor position of the peptide, with a tyrosine at the C terminus. Based on this motif, we identified an octamer epitope from influenza A matrix protein which is presented by HLA-B35. The requirements...
| Main Authors: | , , , , , , |
|---|---|
| Format: | Journal article |
| Language: | English |
| Published: |
1996
|
| _version_ | 1826264089749356544 |
|---|---|
| author | Dong, T Boyd, D Rosenberg, W Alp, N Takiguchi, M McMichael, A Rowland-Jones, S |
| author_facet | Dong, T Boyd, D Rosenberg, W Alp, N Takiguchi, M McMichael, A Rowland-Jones, S |
| author_sort | Dong, T |
| collection | OXFORD |
| description | Peptides associated with HLA-B35 commonly have a proline or occasionally a serine residue in the P2 anchor position of the peptide, with a tyrosine at the C terminus. Based on this motif, we identified an octamer epitope from influenza A matrix protein which is presented by HLA-B35. The requirements for MHC binding and T cell receptor contact have been analyzed using analogs of this peptide with substitutions at positions 1, 2, 4, 7 and 8. The natural epitope contains a serine residue at P2 of the peptide. Substitution of this residue with proline (the favored amino acid in this position in B35-associated peptides) considerably enhances binding to HLA-B35 in the T2-B35 cell line, but the peptide is not recognized by the majority of CTL clones and can antagonize recognition of the index peptide. This suggests that a conservative substitution at the P2 anchor position results in a conformational change in the peptide-MHC surface exposed to the T cell receptor. |
| first_indexed | 2024-03-06T20:02:10Z |
| format | Journal article |
| id | oxford-uuid:27aefa85-710d-4f5d-9047-7f99fe3902ff |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T20:02:10Z |
| publishDate | 1996 |
| record_format | dspace |
| spelling | oxford-uuid:27aefa85-710d-4f5d-9047-7f99fe3902ff2022-03-26T12:08:21ZAn HLA-B35-restricted epitope modified at an anchor residue results in an antagonist peptide.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:27aefa85-710d-4f5d-9047-7f99fe3902ffEnglishSymplectic Elements at Oxford1996Dong, TBoyd, DRosenberg, WAlp, NTakiguchi, MMcMichael, ARowland-Jones, SPeptides associated with HLA-B35 commonly have a proline or occasionally a serine residue in the P2 anchor position of the peptide, with a tyrosine at the C terminus. Based on this motif, we identified an octamer epitope from influenza A matrix protein which is presented by HLA-B35. The requirements for MHC binding and T cell receptor contact have been analyzed using analogs of this peptide with substitutions at positions 1, 2, 4, 7 and 8. The natural epitope contains a serine residue at P2 of the peptide. Substitution of this residue with proline (the favored amino acid in this position in B35-associated peptides) considerably enhances binding to HLA-B35 in the T2-B35 cell line, but the peptide is not recognized by the majority of CTL clones and can antagonize recognition of the index peptide. This suggests that a conservative substitution at the P2 anchor position results in a conformational change in the peptide-MHC surface exposed to the T cell receptor. |
| spellingShingle | Dong, T Boyd, D Rosenberg, W Alp, N Takiguchi, M McMichael, A Rowland-Jones, S An HLA-B35-restricted epitope modified at an anchor residue results in an antagonist peptide. |
| title | An HLA-B35-restricted epitope modified at an anchor residue results in an antagonist peptide. |
| title_full | An HLA-B35-restricted epitope modified at an anchor residue results in an antagonist peptide. |
| title_fullStr | An HLA-B35-restricted epitope modified at an anchor residue results in an antagonist peptide. |
| title_full_unstemmed | An HLA-B35-restricted epitope modified at an anchor residue results in an antagonist peptide. |
| title_short | An HLA-B35-restricted epitope modified at an anchor residue results in an antagonist peptide. |
| title_sort | hla b35 restricted epitope modified at an anchor residue results in an antagonist peptide |
| work_keys_str_mv | AT dongt anhlab35restrictedepitopemodifiedatananchorresidueresultsinanantagonistpeptide AT boydd anhlab35restrictedepitopemodifiedatananchorresidueresultsinanantagonistpeptide AT rosenbergw anhlab35restrictedepitopemodifiedatananchorresidueresultsinanantagonistpeptide AT alpn anhlab35restrictedepitopemodifiedatananchorresidueresultsinanantagonistpeptide AT takiguchim anhlab35restrictedepitopemodifiedatananchorresidueresultsinanantagonistpeptide AT mcmichaela anhlab35restrictedepitopemodifiedatananchorresidueresultsinanantagonistpeptide AT rowlandjoness anhlab35restrictedepitopemodifiedatananchorresidueresultsinanantagonistpeptide AT dongt hlab35restrictedepitopemodifiedatananchorresidueresultsinanantagonistpeptide AT boydd hlab35restrictedepitopemodifiedatananchorresidueresultsinanantagonistpeptide AT rosenbergw hlab35restrictedepitopemodifiedatananchorresidueresultsinanantagonistpeptide AT alpn hlab35restrictedepitopemodifiedatananchorresidueresultsinanantagonistpeptide AT takiguchim hlab35restrictedepitopemodifiedatananchorresidueresultsinanantagonistpeptide AT mcmichaela hlab35restrictedepitopemodifiedatananchorresidueresultsinanantagonistpeptide AT rowlandjoness hlab35restrictedepitopemodifiedatananchorresidueresultsinanantagonistpeptide |