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Departments of
*
Microbiology and Immunology and
Cell Biology, Albert Einstein College of Medicine, Bronx, NY 10461.
Cytotoxic CD8+ T lymphocytes are activated upon the
engagement of their Ag-specific receptors by MHC class I molecules
loaded with peptides 8–11 amino acids long. T cell responses triggered
by certain antigenic peptides are restricted to a limited number of TCR
Vß elements. The precise role of the peptide in causing this
restricted TCR Vß expansion in vivo remains unclear. To address this
issue, we immunized C57BL/6 mice with the immunodominant peptide of the
vesicular stomatitis virus (VSV) and several peptide variants carrying
single substitutions at TCR-contact residues. We observed the expansion
of a limited set of TCR Vß elements responding to each peptide
variant. To focus our analysis solely on the TCR ß-chain, we created
a transgenic mouse expressing exclusively the TCR 
-chain from a VSV
peptide-specific CD8+ T cell clone. These mice showed an
even more restricted TCR Vß usage consequent to peptide immunization.
However, in both C57BL/6 and TCR transgenic mice, single amino acid
replacements in TCR-contact residues of the VSV peptide could alter the
TCR Vß usage of the responding CD8+ T lymphocytes. These
results provide in vivo evidence for an interaction between the
antigenic peptide and the germline-encoded complementarity-determining
region-ß loops that can influence the selection of the responding TCR
repertoire. Furthermore, only replacements at residues near the C
terminus of the peptide were able to alter the TCR Vß usage, which is
consistent with the notion that the TCR ß-chain interacts in vivo
preferentially with this region of the MHC/peptide
complex.
This article has been cited by other articles:
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 K. D. Bourcier, D.-G. Lim, Y.-H. Ding, K. J. Smith, K. Wucherpfennig, and D. A. Hafler Conserved CDR3 Regions in T-Cell Receptor (TCR) CD8+ T Cells That Recognize the Tax11-19/HLA-A*0201 Complex in a Subject Infected with Human T-Cell Leukemia Virus Type 1: Relationship of T-Cell Fine Specificity and Major Histocompatibility Complex/Peptide/TCR Crystal Structure J. Virol., October 15, 2001; 75(20): 9836 - 9843. [Abstract] [Full Text] [PDF]
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S. Honda, W. Zhang, A. M. Kalergis, T. P. DiLorenzo, F. Wang, and S. G. Nathenson Hapten Addition to an MHC Class I-Binding Peptide Causes Substantial Adjustments of the TCR Structure of the Responding CD8+ T Cells J. Immunol., October 15, 2001; 167(8): 4276 - 4285. [Abstract] [Full Text] [PDF]
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W. Zhang, S. Honda, F. Wang, T. P. DiLorenzo, A. M. Kalergis, D. A. Ostrov, and S. G. Nathenson Immunobiological Analysis of TCR Single-Chain Transgenic Mice Reveals New Possibilities for Interaction between CDR3{alpha} and an Antigenic Peptide Bound to MHC Class I J. Immunol., October 15, 2001; 167(8): 4396 - 4404. [Abstract] [Full Text] [PDF]
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C. T. Thomson, A. M. Kalergis, J. C. Sacchettini, and S. G. Nathenson A Structural Difference Limited to One Residue of the Antigenic Peptide Can Profoundly Alter the Biological Outcome of the TCR-Peptide/MHC Class I Interaction J. Immunol., March 15, 2001; 166(6): 3994 - 3997. [Abstract] [Full Text] [PDF]
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A. M. Kalergis and S. G. Nathenson Altered Peptide Ligand-Mediated TCR Antagonism Can Be Modulated by a Change in a Single Amino Acid Residue Within the CDR3{beta} of an MHC Class I-Restricted TCR J. Immunol., July 1, 2000; 165(1): 280 - 285. [Abstract] [Full Text] [PDF]
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