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Loading with mixed bovine brain sulfatides (predominantly 24:0 and 24:1 acyl chains) dramatically enhanced CD1d binding to the DP10.7 TCR (Kd: 5.5 µM) and moderately affected binding to the AB18.1 TCR (Kd: 8.9 µM). Both clones bound to CD1d loaded with 24:1 sulfatide (acyl chain 24:1) at affinities comparable to that with mixed sulfatides (DP10.7 Kd: 5.6 µM; AB18.1 Kd: 13.9 µM). Comparing binding with 24:1 βGalCer-loaded CD1d, which lacks the 3'-galactose sulfate group characteristic of sulfatide lipids, showed that the sulfate moiety was essential for DP10.7 recognition (Kd> 100 µM). In line with sulfatide having a secondary role in recognition by the AB18.1 TCR, the absence of the 3' sulfate group only moderately affected AB18.1 binding (Kd: 16.8 µM). Thus, the DP10.7 TCR makes energetically important contacts with the sulfatide antigen, whereas the AB18.1 TCR can recognize CD1d molecules largely indiscriminately of lipid antigens.
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