Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9913311 | Immunobiology | 2005 | 7 Pages |
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 Lex/y and Lea/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.
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Authors
Estella A. Koppel, Irene S. Ludwig, Ben J. Appelmelk, Yvette van Kooyk, Teunis B.H. Geijtenbeek,