Frontal affinity chromatography analysis of constructs of DC-SIGN, DC-SIGNR and LSECtin extend evidence for affinity to agalactosylated N-glycans.

ABSTRACT: Dendritic cell-specific intracellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN) is a member of the C-type lectin family selectively expressed on immune-related cells. In the present study, we performed a systematic interaction analysis of DC-SIGN and its related receptors, DC-SIGN-related protein (DC-SIGNR) and liver and lymph node sinusoidal endothelial cell C-type lectin (LSECtin) using frontal affinity chromatography (FAC). Carbohydrate-recognition domains of the lectins, expressed as Fc-fusion chimeras, were immobilized to Protein A-Sepharose and subjected to quantitative FAC analysis using 157 pyridylaminated glycans. Both DC-SIGN-Fc and DC-SIGNR-Fc showed similar specificities for glycans containing terminal mannose and fucose, but great difference in affinity under the give

SUBMITTER: Yabe R 

PROVIDER: S-EPMC7163941 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature