Structural Requirements for Glycolipid Antigen Recognition by CD 1b- Restricted T Cells

• Published in: Science (American Association for the Advancement of Science) Vol. 278; no. 5336; pp. 283 - 286
• Main Authors: Moody, D. Branch, Reinhold, Bruce B., Guy, Mark R., Beckman, Evan M., Frederique, Daphney E., Furlong, Stephen T., Ye, Song, Reinhold, Vernon N., Sieling, Peter A., Modlin, Robert L., Besra, Gurdyal S., Porcelli, Steven A.
• Format: Journal Article
• Language: English
• Published: American Society for the Advancement of Science 10-10-1997
• Subjects: Antigens; Cell lines; Glycolipids; Lipids; Macrophages; Microbiology; Monocytes; Mycobacterium tuberculosis; Mycolic acids; T lymphocytes
• ISSN: 0036-8075; 1095-9203

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.