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Molecular interaction of CD1b with lipoglycan antigens.

Abstract：

:The ability of human CD1b molecules to present nonpeptide 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 alpha 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.

journal_name

Immunity

journal_title

Immunity

authors

Ernst WA,Maher J,Cho S,Niazi KR,Chatterjee D,Moody DB,Besra GS,Watanabe Y,Jensen PE,Porcelli SA,Kronenberg M,Modlin RL

doi

10.1016/s1074-7613(00)80538-5

subject

Has Abstract

pub_date

1998-03-01 00:00:00

pages

331-40

issue

3

eissn

1074-7613

issn

1097-4180

pii

S1074-7613(00)80538-5

journal_volume

8

pub_type

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