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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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