Abstract
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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Antigen Presentation
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Cell Line
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Chaperonin 60 / immunology
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Chaperonin 60 / metabolism*
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Clone Cells
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Cytotoxicity, Immunologic
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Epitopes, T-Lymphocyte / metabolism
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Histocompatibility Antigens Class I / metabolism*
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Immunodominant Epitopes / metabolism*
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Mice
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Mice, Inbred C57BL
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Mice, Knockout
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Oligopeptides / immunology
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Oligopeptides / metabolism*
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Peptide Fragments / immunology
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Peptide Fragments / metabolism*
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Peptides* / immunology
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Peptides* / metabolism
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Protein Binding / immunology
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Protein Sorting Signals*
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T-Lymphocytes, Cytotoxic / immunology
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T-Lymphocytes, Cytotoxic / metabolism
Substances
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Chaperonin 60
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Epitopes, T-Lymphocyte
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Histocompatibility Antigens Class I
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Immunodominant Epitopes
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Oligopeptides
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Peptide Fragments
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Peptides
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Protein Sorting Signals
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Q surface antigens
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Qdm protein, mouse