A Peptide from Heat Shock Protein 60 Is the Dominant Peptide Bound To Qa-1 in the Absence of the MHC Class Ia Leader Sequence Peptide Qdm
| Autor: | Suzanne R. Kalb, Bitao Liang, Carla J. Aldrich, Mark J. Soloski, François A. Lemonnier, Adrian Davies, Hong Jiang, Robert J. Cotter |
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| Rok vydání: | 2003 |
| Předmět: |
Cytotoxicity
Immunologic Immunology Epitopes T-Lymphocyte Peptide Protein Sorting Signals Epitope Cell Line Mice Heat shock protein MHC class I Animals Immunology and Allergy Mice Knockout chemistry.chemical_classification Antigen Presentation biology Immunodominant Epitopes Effector Histocompatibility Antigens Class I T-cell receptor Chaperonin 60 MHC restriction GroEL Molecular biology Peptide Fragments Clone Cells Mice Inbred C57BL chemistry biology.protein Peptides Oligopeptides Protein Binding T-Lymphocytes Cytotoxic |
| Zdroj: | The Journal of Immunology. 170:5027-5033 |
| ISSN: | 1550-6606 0022-1767 |
| DOI: | 10.4049/jimmunol.170.10.5027 |
| Popis: | The MHC class Ib molecule Qa-1 binds specifically and predominantly to a single 9-aa peptide (AMAPRTLLL) derived from the leader sequence of many MHC class Ia proteins. This peptide is referred to as Qdm. In this study, we report the isolation and sequencing of a heat shock protein 60-derived peptide (GMKFDRGYI) from Qa-1. This peptide is the dominant peptide bound to Qa-1 in the absence of Qdm. A Qa-1-restricted CTL clone recognizes this heat shock protein 60 peptide, further verifying that it binds to Qa-1 and a peptide from the homologous Salmonella typhimurium protein GroEL (GMQFDRGYL). These observations have implications for how Qa-1 can influence NK cell and T cell effector function via the TCR and CD94/NKG2 family members, and how this effect can change under conditions that cause the peptides bound to Qa-1 to change. |
| Databáze: | OpenAIRE |
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