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*
Ludwig Institute for Cancer Research, Lausanne Branch, and
Institute of Biochemistry, University of Lausanne, Epalinges, Switzerland
Using H-2Kd-restricted CTL clones, which are
specific for a photoreactive derivative of the Plasmodium
berghei circumsporozoite peptide PbCS252–260
(SYIPSAEKI) and permit assessment of TCR-ligand interactions by TCR
photoaffinity labeling, we have previously identified several peptide
derivative variants for which TCR-ligand binding and the efficiency of
Ag recognition deviated by fivefold or more. Here we report that the
functional CTL response (cytotoxicity and IFN-
production)
correlated with the rate of TCR-ligand complex dissociation, but not
the avidity of TCR-ligand binding. While peptide antagonists exhibited
very rapid TCR-ligand complex dissociation, slightly slower
dissociation was observed for strong agonists. Conversely and
surprisingly, weak agonists typically displayed slower dissociation
than the wild-type agonists. Acceleration of TCR-ligand complex
dissociation by blocking CD8 participation in TCR-ligand binding
increased the efficiency of Ag recognition in cases where dissociation
was slow. In addition, permanent TCR engagement by TCR-ligand
photocross-linking completely abolished sustained intracellular calcium
mobilization, which is required for T cell activation. These results
indicate that the functional CTL response depends on the frequency of
serial TCR engagement, which, in turn, is determined by the rate of
TCR-ligand complex dissociation.
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