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

D. Branch Moody; Bruce B. Reinhold; Mark R. Guy; Evan M. Beckman; Daphney E. Frederique; Stephen T. Furlong; Song Ye; Vernon N. Reinhold; Peter A. Sieling; Robert L. Modlin; Gurdyal S. Besra; Steven A. Porcelli

doi:10.1126/science.278.5336.283

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

D. Branch Moody, Bruce B. Reinhold, Mark R. Guy, Evan M. Beckman, Daphney E. Frederique, Stephen T. Furlong, Song Ye, Vernon N. Reinhold, Peter A. Sieling, Robert L. Modlin, Gurdyal S. Besra, Steven A. Porcelli

Research output: Contribution to journal › Article › peer-review

390 Scopus citations

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.

Original language	English (US)
Pages (from-to)	283-286
Number of pages	4
Journal	Science
Volume	278
Issue number	5336
DOIs	https://doi.org/10.1126/science.278.5336.283
State	Published - Oct 10 1997
Externally published	Yes

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title = "Structural requirements for glycolipid antigen recognition by CD1b- restricted T cells",

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.",

author = "Moody, {D. Branch} and Reinhold, {Bruce B.} and Guy, {Mark R.} and Beckman, {Evan M.} and Frederique, {Daphney E.} and Furlong, {Stephen T.} and Song Ye and Reinhold, {Vernon N.} and Sieling, {Peter A.} and Modlin, {Robert L.} and Besra, {Gurdyal S.} and Porcelli, {Steven A.}",

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doi = "10.1126/science.278.5336.283",

language = "English (US)",

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T1 - Structural requirements for glycolipid antigen recognition by CD1b- restricted T cells

AU - Moody, D. Branch

AU - Reinhold, Bruce B.

AU - Guy, Mark R.

AU - Beckman, Evan M.

AU - Frederique, Daphney E.

AU - Furlong, Stephen T.

AU - Ye, Song

AU - Reinhold, Vernon N.

AU - Sieling, Peter A.

AU - Modlin, Robert L.

AU - Besra, Gurdyal S.

AU - Porcelli, Steven A.

PY - 1997/10/10

Y1 - 1997/10/10

N2 - 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.

AB - 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.

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

Abstract

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