Speir J A, Abdel-Motal U M, Jondal M, Wilson I A
Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
Immunity. 1999 Jan;10(1):51-61. doi: 10.1016/s1074-7613(00)80006-0.
T cell receptor (TCR) recognition of nonpeptidic and modified peptide antigens has been recently uncovered but is still poorly understood. Immunization with an H-2Kb-restricted glycopeptide RGY8-6H-Gal2 generates a population of cytotoxic T cells that express both alpha/beta TCR, specific for glycopeptide, and gamma/delta TCR, specific for the disaccharide, even on glycolipids. The crystal structure of Kb/RGY8-6H-Gal2 now demonstrates that the peptide and H-2Kb structures are unaffected by the peptide glycosylation, but the central region of the putative TCR binding site is dominated by the extensive exposure of the tethered carbohydrate. These features of the Kb/RGY8-6H-Gal2 structure are consistent with the individual ligand binding preferences identified for the alpha/beta and gamma/delta TCRs and thus explain the generation of a carbohydrate-specific T cell response.
T细胞受体（TCR）对非肽类和修饰肽抗原的识别最近才被发现，但仍了解甚少。用H-2Kb限制性糖肽RGY8-6H-Gal2进行免疫可产生一群细胞毒性T细胞，这些细胞既表达对糖肽特异的α/β TCR，也表达对二糖特异的γ/δ TCR，甚至对糖脂也有反应。Kb/RGY8-6H-Gal2的晶体结构表明，肽和H-2Kb的结构不受肽糖基化的影响，但假定的TCR结合位点的中心区域主要由连接的碳水化合物的广泛暴露所主导。Kb/RGY8-6H-Gal2结构的这些特征与为α/β和γ/δ TCR确定的个体配体结合偏好一致，从而解释了碳水化合物特异性T细胞反应的产生。
