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• W2152655356 abstract "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." @default.
• W2152655356 created "2016-06-24" @default.
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• W2152655356 date "2011-11-01" @default.
• W2152655356 modified "2023-09-23" @default.
• W2152655356 title "NKT TCR Recognition of CD1d-α-<i>C</i>-Galactosylceramide" @default.
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• W2152655356 doi "https://doi.org/10.4049/jimmunol.1100794" @default.
• W2152655356 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3710193" @default.
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• W2152655356 hasPublicationYear "2011" @default.
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