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

被引：382

作者：

Moody, DB

Reinhold, BB

Guy, MR

Beckman, EM

Frederique, DE

Furlong, ST

Ye, S

Reinhold, VN

Sieling, PA

Modlin, RL

Besra, GS

Porcelli, SA

机构：

[1] BRIGHAM & WOMENS HOSP,DIV RHEUMATOL IMMUNOL & ALLERGY,LYMPHOCYTE BIOL SECT,BOSTON,MA 02115

[2] HARVARD UNIV,SCH MED,BOSTON,MA 02115

[3] BOSTON UNIV,SCH MED,MASS SPECTROMETRY UNIT,BOSTON,MA 02118

[4] COLORADO STATE UNIV,DEPT MICROBIOL,FT COLLINS,CO 80523

[5] UNIV CALIF LOS ANGELES,SCH MED,DIV DERMATOL,LOS ANGELES,CA 90033

[6] UNIV CALIF LOS ANGELES,SCH MED,DEPT IMMUNOL & MICROBIOL,LOS ANGELES,CA 90033

来源：

SCIENCE | 1997年 / 278卷 / 5336期

关键词：

D O I：

10.1126/science.278.5336.283

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：283 / 286

页数：4

共 20 条

[1] Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution [J].