Characterization of carbohydrate recognition by langerin, a C-type lectin of Langerhans cells

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A Protocol for the Production of KLRG1 Tetramer
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A Protocol for the Production of KLRG1 Tetramer

Published on: January 13, 2010

Nicola S Stambach1, Maureen E Taylor

  • 1Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.

Glycobiology
|March 11, 2003
PubMed

Insights

Langerin, a receptor on Langerhans cells, forms a stable trimer. This trimeric structure is crucial for binding and internalizing mannose-containing glycoprotein antigens.

Area of Science:

  • Immunology
  • Glycobiology
  • Structural Biology

Background:

  • Langerin is a type II transmembrane receptor on Langerhans cells.
  • Its extracellular domain includes a neck region and a C-type carbohydrate-recognition domain (CRD).
  • A role in glycoprotein antigen processing has been suggested, but the protein remains understudied.

Purpose of the Study:

  • To investigate the structure and function of the extracellular domain of human langerin.
  • To determine the oligomeric state and ligand-binding properties of langerin.
  • To elucidate the mechanism of glycoprotein antigen uptake mediated by langerin.

Main Methods:

  • Analytical ultracentrifugation
  • Circular dichroism spectroscopy
  • Expression of full-length langerin in rat fibroblast transfectants

Main Results:

  • The extracellular region of langerin forms a stable trimer via alpha-helical coiled-coils in the neck region.
  • The langerin CRD specifically recognizes mannose, GlcNAc, and fucose.
  • Only the trimeric form binds glycoprotein ligands, including high mannose oligosaccharides and yeast invertase structures, but not complex glycans.
  • Full-length langerin mediates efficient uptake and degradation of mannosylated neoglycoproteins.
  • pH-dependent ligand release involves CRD or CRD-neck interactions within the trimer.

Conclusions:

  • Langerin functions as a trimer, essential for recognizing and internalizing mannose-containing glycoprotein antigens.
  • The findings support a role for langerin in the uptake of both self and non-self glycoprotein antigens.
  • Structural insights into langerin's trimeric assembly and ligand binding provide a basis for understanding its immunological function.

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