Journal
BIOPHYSICAL JOURNAL
Volume 104, Issue 8, Pages 1670-1675Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2013.03.023
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Funding
- Austrian Federal Ministry for Science and Research
- Austrian Science Fund (FWF) [Y250-B10]
- Federation of European Biochemical Societies
- Austrian Science Fund (FWF) [Y 250] Funding Source: researchfish
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T cell activation is mediated via the recognition of peptides by the T cell receptor (TCR). This receptor ligand interaction is highly specific, and the TCR has to discriminate between a huge number of peptides presented by the products of the major histocompatibility complexes (MHCs). Recent studies indicate that cells probe the TCR-pMHC interaction by imposing force on the interaction. Here we investigated in a theoretical analysis the consequences of such force-induced unbinding for T cell recognition. Our findings are as follows. First, the bond rupture under force is much faster, improving the time resolution of the discrimination process. Second, cells can access additional parameters characterizing the shape of the binding energy surface. Third, load-induced unbinding yields a reduced coefficient of variation of the bond lifetimes, which improves the discriminative power even between peptide/MHCs (pMHCs) with similar off-rates.
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