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Molecular mechanism of lipopeptide presentation by CD1a

Dirk M Zajonc1, M D Max Crispin, Thomas A Bowden

  • 1Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.

Immunity
|February 23, 2005
PubMed

Insights

CD1a presents lipopeptides to T cells, enabling recognition of both lipid and peptide components. Structural analysis reveals how the peptide moiety is presented for T cell receptor interaction.

Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • CD1a presents lipid antigens to T cells, including glycolipids and lipopeptides with varying alkyl chain numbers.
  • Langerhans cells (LCs) and dendritic cells (DCs) express CD1a, playing a role in immune surveillance.

Purpose of the Study:

  • To investigate the structural basis of CD1a-mediated recognition of didehydroxymycobactin lipopeptides.
  • To elucidate how CD1a presents lipopeptides with a single alkyl chain and peptide components to T cells.

Main Methods:

  • X-ray crystallography of CD1a cocrystallized with a synthetic mycobactin lipopeptide at 2.8 Å resolution.
  • Structural analysis of the CD1a-lipopeptide complex.

Main Results:

  • CD1a presents lipopeptides via insertion of the single alkyl chain into the A' pocket.
  • The peptide branches of the lipopeptide protrude along the F' pocket for T cell receptor (TCR) recognition.
  • A cyclized lysine branch mimics the presentation of alkyl chains in CD1a-sulfatide structures.

Conclusions:

  • CD1a can present single-chain lipids and discriminate the peptide component of lipopeptides.
  • The structural study reveals the mechanism of lipopeptide presentation and TCR interaction via CD1a.

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