Go Back CD209L - Fc Chimera/DCSIGNR - Fc Chimera

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A DNA sequence encoding the signal peptide of IL-10 receptor alpha chain was fused to the extracellular domain of human CD209L (aa 1-328), which was in turn fused to the Fc region of human IgG1 (aa 93-330). The chimeric protein was expressed in modified human 293 cells.

CD209L / DC-SIGNR, a member of the ‘SIGN’ family of C-type lectin receptors, is a type II membrane protein that is expressed on liver sinusoidal endothelial cells (LSEC), specialized capillary vessels that are involved in antigen presentation and hepatic immune surveillance. CD209L is also expressed by endothelial cells associated with lymph nodes and in the human lung on type II alveolar cells and endothelial cells. Structurally CD209L shares 77% amino acid sequence homology with DC-SIGN, a dendritic cell expressed homolog, and comprises the following domains; the cytoplasmic domain, a transmembrane domain, and an extracellular domain comprising a neck region with seven repeats of a 23 amino acid sequence and a carbohydrate recognition domain (CRD). There are 4 potential glycosylation sites within the extracellular domain of CD209L. CD209L binds with high affinity to mannose rich carbohydrate moieties of pathogens such as viral envelope proteins. CD209L initiates antigen internalisation and is therefore an important first step in antigen processing, presentation and the initiation of an immune response. Recently it has been shown that viruses such as HIV and HCV bind CD209L and are internalized into non-lysosomal compartments and subsequently transferred to infect target cells. For a recent review on CD209L please refer to Koppel et al. (2005) Cell Microbiol 7(2):157-65.