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DCIR interacts with ligands from both endogenous and pathogenic origin.

Karien Bloem1, Ilona M Vuist2, Meike van den Berk2

  • 1Department of Molecular Cell Biology and Immunology, VU University Medical Center, Amsterdam, The Netherlands; Danone Research, Centre for Specialized Nutrition, Wageningen, The Netherlands.

Immunology Letters
|November 19, 2013
PubMed
Summary
This summary is machine-generated.

Dendritic cell immunoreceptor (DCIR) binds specific glycans, differing from the broader specificity of DC-SIGN. DCIR shows high affinity for sulfo-Lewis(a) and interacts with pathogenic and endogenous ligands.

Keywords:
C-type lectinsDendritic cellGlycanGlycosylationPathogen and cancer

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Area of Science:

  • Immunology
  • Glycobiology
  • Cell Biology

Background:

  • C-type lectins on dendritic cells (DCs) are crucial for antigen uptake and immune response modulation.
  • Dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN) is a well-characterized DC lectin.
  • The carbohydrate specificity of dendritic cell immunoreceptor (DCIR) was previously debated.

Purpose of the Study:

  • To compare the carbohydrate specificity of DCIR and DC-SIGN.
  • To elucidate the interaction of DCIR with known DC-SIGN ligands.
  • To identify DCIR-specific ligands and understand factors influencing its binding.

Main Methods:

  • Comparative analysis of DCIR and DC-SIGN binding to various carbohydrate ligands.
  • Investigation of ligand interactions with purified DCIR and DC-SIGN.
  • Assessment of DCIR binding to viral glycoproteins (HIV-1 gp140 and gp120) and cancer cell line glycoproteins.
  • Detection of DCIR-specific ligands on keratinocytes.

Main Results:

  • DC-SIGN exhibits broader glycan specificity than DCIR.
  • DCIR specifically binds mannotriose, sulfo-Lewis(a), Lewis(b), and Lewis(a).
  • While most DC-SIGN ligands also bind DCIR, Candida albicans and certain cancer-associated glycoproteins are DC-SIGN-specific.
  • DCIR strongly binds HIV-1 gp140 but weakly binds gp120; DCIR-specific ligands are found on keratinocytes.
  • DCIR glycosylation significantly influences ligand interaction, with sulfo-Lewis(a) identified as a high-affinity ligand.

Conclusions:

  • DCIR and DC-SIGN share many ligands, but possess distinct specificities.
  • DCIR binds ligands from both pathogenic (e.g., HIV-1) and endogenous sources (e.g., keratinocytes).
  • Sulfo-Lewis(a) is a high-affinity ligand for DCIR, highlighting its role in immune recognition.