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  • The diversity of antigen-specific TCR repertoires reflects the relative complexity of epitopes recognized

    Author(s)
    Maryanski, JL
    Casanova, JL
    Falk, K
    Gournier, H
    Jaulin, C
    Kourilsky, P
    Lemonnier, FA
    Luthy, R
    Rammensee, HG
    Rotzschke, O
    Servis, C
    Lopez, JA
    Griffith University Author(s)
    Lopez Ramirez, Alejandro
    Year published
    1997
    Metadata
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    Abstract
    Antigen-selected T cell receptor (TCR) repertoires vary in complexity from very limited to extremely diverse. We have previously characterized two different CD8 T cell responses, which are restricted by the same mouse major histocompatibility complex (MHC) class I molecule, H-2 Kd. The TCR repertoire in the response against a determinant from Plasmodium berghei circumsporozoite protein (PbCS; region 252-260) is very diverse, whereas TCRs expressed by clones specific for a determinant in region 170-179 of HLA-CW3 (human) MHC class I molecule show relatively limited structural diversity. We had already demonstrated that cytolytic ...
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    Antigen-selected T cell receptor (TCR) repertoires vary in complexity from very limited to extremely diverse. We have previously characterized two different CD8 T cell responses, which are restricted by the same mouse major histocompatibility complex (MHC) class I molecule, H-2 Kd. The TCR repertoire in the response against a determinant from Plasmodium berghei circumsporozoite protein (PbCS; region 252-260) is very diverse, whereas TCRs expressed by clones specific for a determinant in region 170-179 of HLA-CW3 (human) MHC class I molecule show relatively limited structural diversity. We had already demonstrated that cytolytic T lymphocyte (CTL) clones specific for the PbCS peptide display diverse patterns of antigen recognition when tested with a series of single Ala-substituted PbCS peptides or mutant H-2 Kd molecules. We now show that CW3-specific CTL clones display much less diverse patterns of recognition. Our earlier functional studies with synthetic peptide variants suggested that the optimal peptides recognized were 9 (or 8) residues long for PbCS and 10 residues long for CW3. We now present more direct evidence that the natural CW3 ligand is indeed a 10-mer. Our functional data together with molecular modeling suggest that the limited TCR repertoire selected during the CW3 response is not due to a paucity of available epitopes displayed at the surface of the CW3 peptide/Kd complex. We discuss other factors, such as the expression of similar self MHC peptide sequences, that might be involved in trimming this TCR repertoire.
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    Journal Title
    Human Immunology
    Volume
    54
    Issue
    2
    DOI
    https://doi.org/10.1016/S0198-8859(97)00082-7
    Subject
    Immunology
    Immunogenetics (incl. genetic immunology)
    Publication URI
    http://hdl.handle.net/10072/135282
    Collection
    • Journal articles

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