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 language | English |
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Pages (from-to) | 195-201 |
Number of pages | 7 |
Journal | Immunobiology |
Volume | 210 |
Issue number | 2-4 |
DOIs | |
Publication status | Published - 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