Requirement of the proteasome for the trimming of signal peptide-derived epitopes presented by the nonclassical major histocompatibility complex class I molecule HLA-E.
The nonclassical major histocompatibility complex class I molecule HLA-E acts as a ligand for CD94/NKG2 receptors on the surface of natural killer cells and a subset of T cells. HLA-E presents closely related nonameric peptide epitopes derived from the highly conserved signal sequences of classical...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2003
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| _version_ | 1797063412588478464 |
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| author | Bland, F Lemberg, M Mcmichael, A Martoglio, B Braud, V |
| author_facet | Bland, F Lemberg, M Mcmichael, A Martoglio, B Braud, V |
| author_sort | Bland, F |
| collection | OXFORD |
| description | The nonclassical major histocompatibility complex class I molecule HLA-E acts as a ligand for CD94/NKG2 receptors on the surface of natural killer cells and a subset of T cells. HLA-E presents closely related nonameric peptide epitopes derived from the highly conserved signal sequences of classical major histocompatibility complex class I molecules as well as HLA-G. Their generation requires cleavage of the signal sequence by signal peptidase followed by the intramembrane-cleaving aspartic protease, signal peptide peptidase. In this study, we have assessed the subsequent proteolytic requirements leading to generation of the nonameric HLA-E peptide epitopes. We show that proteasome activity is required for further processing of the peptide generated by signal peptide peptidase. This constitutes the first example of capture of a naturally derived short peptide by the proteasome, producing a class I peptide ligand. |
| first_indexed | 2024-03-06T20:59:29Z |
| format | Journal article |
| id | oxford-uuid:3a6287ed-ce8e-4488-87ca-09af54bc66df |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T20:59:29Z |
| publishDate | 2003 |
| record_format | dspace |
| spelling | oxford-uuid:3a6287ed-ce8e-4488-87ca-09af54bc66df2022-03-26T14:01:20ZRequirement of the proteasome for the trimming of signal peptide-derived epitopes presented by the nonclassical major histocompatibility complex class I molecule HLA-E.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:3a6287ed-ce8e-4488-87ca-09af54bc66dfEnglishSymplectic Elements at Oxford2003Bland, FLemberg, MMcmichael, AMartoglio, BBraud, VThe nonclassical major histocompatibility complex class I molecule HLA-E acts as a ligand for CD94/NKG2 receptors on the surface of natural killer cells and a subset of T cells. HLA-E presents closely related nonameric peptide epitopes derived from the highly conserved signal sequences of classical major histocompatibility complex class I molecules as well as HLA-G. Their generation requires cleavage of the signal sequence by signal peptidase followed by the intramembrane-cleaving aspartic protease, signal peptide peptidase. In this study, we have assessed the subsequent proteolytic requirements leading to generation of the nonameric HLA-E peptide epitopes. We show that proteasome activity is required for further processing of the peptide generated by signal peptide peptidase. This constitutes the first example of capture of a naturally derived short peptide by the proteasome, producing a class I peptide ligand. |
| spellingShingle | Bland, F Lemberg, M Mcmichael, A Martoglio, B Braud, V Requirement of the proteasome for the trimming of signal peptide-derived epitopes presented by the nonclassical major histocompatibility complex class I molecule HLA-E. |
| title | Requirement of the proteasome for the trimming of signal peptide-derived epitopes presented by the nonclassical major histocompatibility complex class I molecule HLA-E. |
| title_full | Requirement of the proteasome for the trimming of signal peptide-derived epitopes presented by the nonclassical major histocompatibility complex class I molecule HLA-E. |
| title_fullStr | Requirement of the proteasome for the trimming of signal peptide-derived epitopes presented by the nonclassical major histocompatibility complex class I molecule HLA-E. |
| title_full_unstemmed | Requirement of the proteasome for the trimming of signal peptide-derived epitopes presented by the nonclassical major histocompatibility complex class I molecule HLA-E. |
| title_short | Requirement of the proteasome for the trimming of signal peptide-derived epitopes presented by the nonclassical major histocompatibility complex class I molecule HLA-E. |
| title_sort | requirement of the proteasome for the trimming of signal peptide derived epitopes presented by the nonclassical major histocompatibility complex class i molecule hla e |
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