HLA-E: A Novel Player for Histocompatibility
The classical class I human leukocyte antigens (HLA-A, -B, and -C) present allele-specific self- or pathogenic peptides originated by intracellular processing to CD8+ immune effector cells. Even a single mismatch in the heavy chain (hc) of an HLA class I molecule can impact on the peptide binding pr...
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| Format: | Article |
| Language: | English |
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Wiley
2014-01-01
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| Series: | Journal of Immunology Research |
| Online Access: | http://dx.doi.org/10.1155/2014/352160 |
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| author | Thomas Kraemer Rainer Blasczyk Christina Bade-Doeding |
| author_facet | Thomas Kraemer Rainer Blasczyk Christina Bade-Doeding |
| author_sort | Thomas Kraemer |
| collection | DOAJ |
| description | The classical class I human leukocyte antigens (HLA-A, -B, and -C) present allele-specific self- or pathogenic peptides originated by intracellular processing to CD8+ immune effector cells. Even a single mismatch in the heavy chain (hc) of an HLA class I molecule can impact on the peptide binding profile. Since HLA class I molecules are highly polymorphic and most of their polymorphisms affect the peptide binding region (PBR), it becomes obvious that systematic HLA matching is crucial in determining the outcome of transplantation. The opposite holds true for the nonclassical HLA class I molecule HLA-E. HLA-E polymorphism is restricted to two functional versions and is thought to present a limited set of highly conserved peptides derived from class I leader sequences. However, HLA-E appears to be a ligand for the innate and adaptive immune system, where the immunological response to peptide-HLA-E complexes is dictated through the sequence of the bound peptide. Structural investigations clearly demonstrate how subtle amino acid differences impact the strength and response of the cognate CD94/NKG2 or T cell receptor. |
| format | Article |
| id | doaj-art-b558c2dc5f2c46c980899f8ec6c013be |
| institution | Kabale University |
| issn | 2314-8861 2314-7156 |
| language | English |
| publishDate | 2014-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Journal of Immunology Research |
| spelling | doaj-art-b558c2dc5f2c46c980899f8ec6c013be2025-08-20T03:39:26ZengWileyJournal of Immunology Research2314-88612314-71562014-01-01201410.1155/2014/352160352160HLA-E: A Novel Player for HistocompatibilityThomas Kraemer0Rainer Blasczyk1Christina Bade-Doeding2Institute for Transfusion Medicine, Hannover Medical School, Medical Park, Feodor-Lynen-Straße 5, 30625 Hannover, GermanyInstitute for Transfusion Medicine, Hannover Medical School, Medical Park, Feodor-Lynen-Straße 5, 30625 Hannover, GermanyInstitute for Transfusion Medicine, Hannover Medical School, Medical Park, Feodor-Lynen-Straße 5, 30625 Hannover, GermanyThe classical class I human leukocyte antigens (HLA-A, -B, and -C) present allele-specific self- or pathogenic peptides originated by intracellular processing to CD8+ immune effector cells. Even a single mismatch in the heavy chain (hc) of an HLA class I molecule can impact on the peptide binding profile. Since HLA class I molecules are highly polymorphic and most of their polymorphisms affect the peptide binding region (PBR), it becomes obvious that systematic HLA matching is crucial in determining the outcome of transplantation. The opposite holds true for the nonclassical HLA class I molecule HLA-E. HLA-E polymorphism is restricted to two functional versions and is thought to present a limited set of highly conserved peptides derived from class I leader sequences. However, HLA-E appears to be a ligand for the innate and adaptive immune system, where the immunological response to peptide-HLA-E complexes is dictated through the sequence of the bound peptide. Structural investigations clearly demonstrate how subtle amino acid differences impact the strength and response of the cognate CD94/NKG2 or T cell receptor.http://dx.doi.org/10.1155/2014/352160 |
| spellingShingle | Thomas Kraemer Rainer Blasczyk Christina Bade-Doeding HLA-E: A Novel Player for Histocompatibility Journal of Immunology Research |
| title | HLA-E: A Novel Player for Histocompatibility |
| title_full | HLA-E: A Novel Player for Histocompatibility |
| title_fullStr | HLA-E: A Novel Player for Histocompatibility |
| title_full_unstemmed | HLA-E: A Novel Player for Histocompatibility |
| title_short | HLA-E: A Novel Player for Histocompatibility |
| title_sort | hla e a novel player for histocompatibility |
| url | http://dx.doi.org/10.1155/2014/352160 |
| work_keys_str_mv | AT thomaskraemer hlaeanovelplayerforhistocompatibility AT rainerblasczyk hlaeanovelplayerforhistocompatibility AT christinabadedoeding hlaeanovelplayerforhistocompatibility |