Molecular interaction of CD1b with lipoglycan antigens

William A. Ernst; Juli Maher; Sungae Cho; Kayvan R. Niazi; Delphi Chatterjee; D. Branch Moody; Gurdyal S. Besra; Yutaka Watanabe; Peter E. Jensen; Steven A. Porcelli; Mitchell Kronenberg; Robert L. Modlin

doi:10.1016/S1074-7613(00)80538-5

Molecular interaction of CD1b with lipoglycan antigens

William A. Ernst, Juli Maher, Sungae Cho, Kayvan R. Niazi, Delphi Chatterjee, D. Branch Moody, Gurdyal S. Besra, Yutaka Watanabe, Peter E. Jensen, Steven A. Porcelli, Mitchell Kronenberg, Robert L. Modlin

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

170 Scopus citations

Abstract

The ability of human CD1b molecules to present non-peptide antigens is suggested by the T cell recognition of microbial lipids and lipoglycans in the presence of CD1b-expressing antigen-presenting cells. We demonstrate the high-affinity interaction of CD1b molecules with the acyl side chains of known T cell antigens, lipoarabinomannan, phosphatidylinositol mannoside, and glucose monomycolate. Furthermore, CD1b-antigen binding was optimal at acidic pH, consistent with the known requirement for endosomal acidification in CD1b-restricted antigen presentation. The mechanism for CD1b-ligand interaction involves the partial unfolding of the α helices of CD1b at acidic pH, revealing a hydrophobic binding site that could accommodate lipid. These data provide direct evidence that the CD1b molecule has evolved unique biochemical properties that enable the binding of lipid-containing antigens from intracellular pathogens.

Original language	English (US)
Pages (from-to)	331-340
Number of pages	10
Journal	Immunity
Volume	8
Issue number	3
DOIs	https://doi.org/10.1016/S1074-7613(00)80538-5
State	Published - Mar 1998
Externally published	Yes

ASJC Scopus subject areas

Immunology and Allergy
Immunology
Infectious Diseases

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/S1074-7613(00)80538-5

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@article{6f21f62616834adda6f87f11ec61498d,

title = "Molecular interaction of CD1b with lipoglycan antigens",

abstract = "The ability of human CD1b molecules to present non-peptide antigens is suggested by the T cell recognition of microbial lipids and lipoglycans in the presence of CD1b-expressing antigen-presenting cells. We demonstrate the high-affinity interaction of CD1b molecules with the acyl side chains of known T cell antigens, lipoarabinomannan, phosphatidylinositol mannoside, and glucose monomycolate. Furthermore, CD1b-antigen binding was optimal at acidic pH, consistent with the known requirement for endosomal acidification in CD1b-restricted antigen presentation. The mechanism for CD1b-ligand interaction involves the partial unfolding of the α helices of CD1b at acidic pH, revealing a hydrophobic binding site that could accommodate lipid. These data provide direct evidence that the CD1b molecule has evolved unique biochemical properties that enable the binding of lipid-containing antigens from intracellular pathogens.",

author = "Ernst, {William A.} and Juli Maher and Sungae Cho and Niazi, {Kayvan R.} and Delphi Chatterjee and Moody, {D. Branch} and Besra, {Gurdyal S.} and Yutaka Watanabe and Jensen, {Peter E.} and Porcelli, {Steven A.} and Mitchell Kronenberg and Modlin, {Robert L.}",

note = "Funding Information: We thank S. Morrison for use of the IAsys biosensor and E. Reisler for the use of the Jasco spectrapolarimeter and the Perkin-Elmer fluorometer. We are grateful to A. Brunmark and M. Jackson for helpful suggestions in the purification of class I molecules. We would also like to thank B. Bloom, P. J. Brennan, K. Fisher-Lindahl, H. Grey, and D. Margulies for helpful discussions. This work was supported by grants from the National Institutes of Health (AI07126-19, AI22553, AI36069, AR40312, and AI37139) and the UNDP/World Bank/World Health Organization Special Programme for Research and Training in Tropical Diseases (IMMLEP).",

year = "1998",

month = mar,

doi = "10.1016/S1074-7613(00)80538-5",

language = "English (US)",

volume = "8",

pages = "331--340",

journal = "Immunity",

issn = "1074-7613",

publisher = "Cell Press",

number = "3",

}

TY - JOUR

T1 - Molecular interaction of CD1b with lipoglycan antigens

AU - Ernst, William A.

AU - Maher, Juli

AU - Cho, Sungae

AU - Niazi, Kayvan R.

AU - Chatterjee, Delphi

AU - Moody, D. Branch

AU - Besra, Gurdyal S.

AU - Watanabe, Yutaka

AU - Jensen, Peter E.

AU - Porcelli, Steven A.

AU - Kronenberg, Mitchell

AU - Modlin, Robert L.

N1 - Funding Information: We thank S. Morrison for use of the IAsys biosensor and E. Reisler for the use of the Jasco spectrapolarimeter and the Perkin-Elmer fluorometer. We are grateful to A. Brunmark and M. Jackson for helpful suggestions in the purification of class I molecules. We would also like to thank B. Bloom, P. J. Brennan, K. Fisher-Lindahl, H. Grey, and D. Margulies for helpful discussions. This work was supported by grants from the National Institutes of Health (AI07126-19, AI22553, AI36069, AR40312, and AI37139) and the UNDP/World Bank/World Health Organization Special Programme for Research and Training in Tropical Diseases (IMMLEP).

PY - 1998/3

Y1 - 1998/3

N2 - The ability of human CD1b molecules to present non-peptide antigens is suggested by the T cell recognition of microbial lipids and lipoglycans in the presence of CD1b-expressing antigen-presenting cells. We demonstrate the high-affinity interaction of CD1b molecules with the acyl side chains of known T cell antigens, lipoarabinomannan, phosphatidylinositol mannoside, and glucose monomycolate. Furthermore, CD1b-antigen binding was optimal at acidic pH, consistent with the known requirement for endosomal acidification in CD1b-restricted antigen presentation. The mechanism for CD1b-ligand interaction involves the partial unfolding of the α helices of CD1b at acidic pH, revealing a hydrophobic binding site that could accommodate lipid. These data provide direct evidence that the CD1b molecule has evolved unique biochemical properties that enable the binding of lipid-containing antigens from intracellular pathogens.

AB - The ability of human CD1b molecules to present non-peptide antigens is suggested by the T cell recognition of microbial lipids and lipoglycans in the presence of CD1b-expressing antigen-presenting cells. We demonstrate the high-affinity interaction of CD1b molecules with the acyl side chains of known T cell antigens, lipoarabinomannan, phosphatidylinositol mannoside, and glucose monomycolate. Furthermore, CD1b-antigen binding was optimal at acidic pH, consistent with the known requirement for endosomal acidification in CD1b-restricted antigen presentation. The mechanism for CD1b-ligand interaction involves the partial unfolding of the α helices of CD1b at acidic pH, revealing a hydrophobic binding site that could accommodate lipid. These data provide direct evidence that the CD1b molecule has evolved unique biochemical properties that enable the binding of lipid-containing antigens from intracellular pathogens.

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JO - Immunity

JF - Immunity

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ER -

Molecular interaction of CD1b with lipoglycan antigens

Abstract

ASJC Scopus subject areas

UN SDGs

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