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

doi:10.1016/j.imbio.2005.05.012

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 journal › Article › Academic › peer-review

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
Pages (from-to)	195-201
Number of pages	7
Journal	Immunobiology
Volume	210
Issue number	2-4
DOIs	https://doi.org/10.1016/j.imbio.2005.05.012
Publication status	Published - 2005

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@article{d509473e71c942268318c0f20efa2981,

title = "Carbohydrate specificities of the murine DC-SIGN homologue mSIGNR1",

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.",

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",

author = "Koppel, {Estella A} and Ludwig, {Irene S} and Appelmelk, {Ben J} and {van Kooyk}, Yvette and Geijtenbeek, {Teunis B H}",

year = "2005",

doi = "10.1016/j.imbio.2005.05.012",

language = "English",

volume = "210",

pages = "195--201",

journal = "Immunobiology",

issn = "0171-2985",

publisher = "Urban und Fischer Verlag GmbH und Co. KG",

number = "2-4",

}

TY - JOUR

T1 - Carbohydrate specificities of the murine DC-SIGN homologue mSIGNR1

AU - Koppel, Estella A

AU - Ludwig, Irene S

AU - Appelmelk, Ben J

AU - van Kooyk, Yvette

AU - Geijtenbeek, Teunis B H

PY - 2005

Y1 - 2005

N2 - 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.

AB - 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.

KW - Animals

KW - Binding Sites

KW - Carbohydrate Metabolism

KW - Carbohydrates/chemistry

KW - Cell Adhesion Molecules/metabolism

KW - Humans

KW - Lectins, C-Type/metabolism

KW - Lewis X Antigen/metabolism

KW - Mice

KW - Receptors, Cell Surface/metabolism

KW - Substrate Specificity

U2 - 10.1016/j.imbio.2005.05.012

DO - 10.1016/j.imbio.2005.05.012

M3 - Article

C2 - 16164026

SN - 0171-2985

VL - 210

SP - 195

EP - 201

JO - Immunobiology

JF - Immunobiology

IS - 2-4

ER -