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Título: | NKT TCR Recognition of CD1d-α-C-Galactosylceramide |
Autor: | Patel, Onisha; Cameron, Garth; Pellicci, Daniel G.; Liu, Zheng; Byun, Hoe-Sup; Beddoe, Travis; McCluskey, James; Franck, Richard W.; Castaño, A. Raúl; Harrak Serifi, Youssef CSIC; Llebaria, Amadeu CSIC ORCID; Bittman, Robert; Porcelli, Steven A.; Godfrey, Dale I.; Rossjohn, Jamie | Fecha de publicación: | 2011 | Editor: | American Association of Immunologists | Citación: | Journal of Immunology | Resumen: | NKT 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 editor: | http://dx.doi.org/10.4049/jimmunol.1100794 | URI: | http://hdl.handle.net/10261/48088 | DOI: | 10.4049/jimmunol.1100794 | ISSN: | 0022-1767 | E-ISSN: | 1550-6606 |
Aparece en las colecciones: | (IQAC) Artículos |
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