Carbohydrate specificities of the murine DC-SIGN homologue mSIGNR1

Estella A Koppel, Irene S Ludwig, Ben J Appelmelk, Yvette van Kooyk, Teunis B H Geijtenbeek

Research output: Contribution to journalArticleAcademicpeer-review

13 Citations (Scopus)

Abstract

C-type lectins are important receptors expressed by antigen presenting cells that are involved in cellular communications as well as in pathogen uptake. An important C-type lectin family is represented by DC-SIGN and its homologues in human and mouse. Here we have investigated the carbohydrate specificity of cellular mSIGNR1 and compared it with DC-SIGN and L-SIGN. mSIGNR1 has a similar specificity as human DC-SIGN for high mannose-containing ligands present on both cellular and pathogen ligands. However, the DC-SIGN molecules differ in their recognition of Lewis antigens; mSIGNR1 interacts not only with Le(x/y) and Le(a/b) antigens similar to DC-SIGN, but also with sialylated Lex, a ligand for selectins. The differential recognition of Lewis antigens suggests differences between mSIGNR1 and DC-SIGN in the recognition of cellular ligands and pathogens that express Lewis epitopes.

Original languageEnglish
Pages (from-to)195-201
Number of pages7
JournalImmunobiology
Volume210
Issue number2-4
DOIs
Publication statusPublished - 2005

Keywords

  • Animals
  • Binding Sites
  • Carbohydrate Metabolism
  • Carbohydrates/chemistry
  • Cell Adhesion Molecules/metabolism
  • Humans
  • Lectins, C-Type/metabolism
  • Lewis X Antigen/metabolism
  • Mice
  • Receptors, Cell Surface/metabolism
  • Substrate Specificity

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