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NKT TCR Recognition of CD1d-α-C-Galactosylceramide

AutorPatel, Onisha; Cameron, Garth; Pellicci, Daniel G.; Liu, Zheng; Byun, Hoe-Sup; Beddoe, Travis; McCluskey, James; Franck, Richard W.; Castaño, A. Raúl; Harrak Serifi, Youssef; Llebaria, Amadeu; Bittman, Robert; Porcelli, Steven A.; Godfrey, Dale I.; Rossjohn, Jamie
Fecha de publicación2011
EditorAmerican Association of Immunologists
CitaciónJournal of Immunology
ResumenNKT cells respond to a variety of CD1d-restricted glycolipid Ags that are structurally related to the prototypic Ag α-galactosylceramide (α-GalCer). A modified analog of α-GalCer with a carbon-based glycosidic linkage (α-C-GalCer) has generated great interest because of its apparent ability to promote prolonged, Th1-biased immune responses. In this study, we report the activation of spleen NKT cells to α-C-GalCer, and related C-glycoside ligands, is weaker than that of α-GalCer. Furthermore, the Vβ8.2 and Vβ7 NKT TCR affinity for CD1d–α-C-GalCer, and some related analogs, is ∼10-fold lower than that for the NKT TCR–CD1d–α-GalCer interaction. Nevertheless, the crystal structure of the Vβ8.2 NKT TCR–CD1d–α-C-GalCer complex is similar to that of the corresponding NKT TCR–CD1d–α-GalCer complex, although subtle differences at the interface provide a basis for understanding the lower affinity of the NKT TCR–CD1d–α-C-GalCer interaction. Our findings support the concept that for CD1d-restricted NKT cells, altered glycolipid ligands can promote markedly different responses while adopting similar TCR-docking topologies.
Versión del editorhttp://dx.doi.org/10.4049/jimmunol.1100794
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