CD1b 限制性 T 细胞识别糖脂抗原的结构要求。

Structural requirements for glycolipid antigen recognition by CD1b-restricted T cells.

作者信息

Moody D B, Reinhold B B, Guy M R, Beckman E M, Frederique D E, Furlong S T, Ye S, Reinhold V N, Sieling P A, Modlin R L, Besra G S, Porcelli S A

机构信息

Lymphocyte Biology Section, Division of Rheumatology, Immunology, and Allergy, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA.

出版信息

Science. 1997 Oct 10;278(5336):283-6. doi: 10.1126/science.278.5336.283.

DOI:10.1126/science.278.5336.283

PMID:9323206

Abstract

The human CD1b protein presents lipid antigens to T cells, but the molecular mechanism is unknown. Identification of mycobacterial glucose monomycolate (GMM) as a CD1b-presented glycolipid allowed determination of the structural requirements for its recognition by T cells. Presentation of GMM to CD1b-restricted T cells was not affected by substantial variations in its lipid tails, but was extremely sensitive to chemical alterations in its carbohydrate or other polar substituents. These findings support the view that the recently demonstrated hydrophobic CD1 groove binds the acyl chains of lipid antigens relatively nonspecifically, thereby positioning the hydrophilic components for highly specific interactions with T cell antigen receptors.

摘要

人类CD1b蛋白将脂质抗原呈递给T细胞，但其分子机制尚不清楚。鉴定出分枝杆菌单葡萄糖酰基鞘氨醇（GMM）为CD1b呈递的糖脂，从而确定了T细胞识别该糖脂的结构要求。GMM呈递给受CD1b限制的T细胞不受其脂尾大量变化的影响，但对其碳水化合物或其他极性取代基的化学改变极为敏感。这些发现支持了以下观点：最近证明的疏水性CD1凹槽相对非特异性地结合脂质抗原的酰基链，从而将亲水性成分定位，以便与T细胞抗原受体进行高度特异性相互作用。