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 journalArticlepeer-review

169 Scopus citations


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 languageEnglish (US)
Pages (from-to)331-340
Number of pages10
Issue number3
StatePublished - Mar 1998
Externally publishedYes

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Infectious Diseases


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