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These two TCRs 9C1 and 9B2 were selected based on their contrasting Ag reactivity profiles, whereby the 9C1 TCR demonstrated a strong dependence on α-GalCer for activation, whereas the 9B2 TCR, whilst still reactive to CD1d–α-GalCer tetramers, demonstrated an auto-reactive profile that was associated with less Ag-specific activation. The 9C1 and 9B2 TCRs did not bind, or bound very poorly, to CD1d-endogenous tetramers respectively, consistent with the tetramer-binding data. The 9C1 TCR and 9B2 TCR both bound to CD1d–α-GalCer with an affinity (KD) of 3.9 μM and 4.0 μM respectively, values that, while comparable to many TCR–pMHC interactions, were weaker than the affinity of the canonical type I NKT TCR (NKT15) towards CD1d–α-GalCer (KD=0.19 μM). The affinity of the 9C1 and 9B2 TCRs towards CD1d-3′-deoxy-α-GalCer (KD=1.4 μM and 3.6 μM, respectively) was comparable or moderately higher than that of CD1d–α-GalCer. This is in stark contrast to the NKT15 TCR, which bound with much lower affinity to CD1d-3′-deoxy-α-GalCer (KD=4.7 μM, ∼20-fold reduction). Conversely, the 9C1 TCR exhibited a markedly reduced affinity (KD> 100 μM) towards the 4′-deoxy-α-GalCer analogue, while there was no negative impact of this analogue on NKT15 or 9B2 TCR binding. Consistent with tetramer staining and functional studies, α-GlcCer was bound with much lower affinity by 9C1 TCR and 9B2 TCR (KD> 100 μM and 19 μM, respectively), yet was well-tolerated by NKT15 TCR (KD=0.12 μM). The recognition of 4′-deoxy-α-GalCer but not α-GlcCer by 9B2 TCR implies that the equatorial 4′-OH group of α-GlcCer may cause a conformational change in CD1d and/or the lipid headgroup, which is not tolerated by 9B2. Thus, while the atypical NKT TCRs and type I NKT TCRs are reactive towards α-GalCer, they clearly differ in their fine specificity towards CD1d-restricted Ags.
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