期刊
NATURE IMMUNOLOGY
卷 2, 期 3, 页码 229-234出版社
NATURE AMERICA INC
DOI: 10.1038/85286
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- NCI NIH HHS [5T52CA09173-23] Funding Source: Medline
- NIAID NIH HHS [R01 AI07289-32] Funding Source: Medline
- NIAMS NIH HHS [R01 AR42533-5] Funding Source: Medline
Cytotoxic T cell (CTL) activation by antigen requires the specific detection of peptide-major histocompatibility class I (pMHC) molecules on the target-cell surface by the T cell receptor (TCR). We examined the effect of mutations in the antigen-binding site of a K-b-restricted TCR on T cell activation, antigen binding and dissociation from antigen. These parameters were also examined for variants derived from a K-d-restricted peptide that was recognized by a CTL clone, Using these two independent systems, we show that T cell activation can be impaired by mutations that either decrease or increase the binding half-life of the TCR-pMHC interaction. Our data indicate that efficient T cell activation occurs within an optimal dwell-time range of TCR-pMHC interaction. This restricted dwell-time range is consistent with the exclusion of either extremely low or high affinity T cells from the expanded population during immune responses.
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