Disease relevance of CLEC4G

• Here, we show that LSECtin enhances infection driven by filovirus glycoproteins (GP) and the S protein of SARS coronavirus, but does not interact with human immunodeficiency virus type-1 and hepatitis C virus envelope proteins [1].

High impact information on CLEC4G

• Moreover, LSECtin is expressed predominantly by sinusoidal endothelial cells of human liver and lymph node and co-expressed with DC-SIGNR [2].
• LSECtin mRNA was only expressed in liver and lymph node among 15 human tissues tested, intriguingly neither expressed on hematopoietic cell lines nor on monocyte-derived dendritic cells (DCs) [2].
• Characterization of a novel C-type lectin-like gene, LSECtin: demonstration of carbohydrate binding and expression in sinusoidal endothelial cells of liver and lymph node [2].
• LSECtin binds to mannose, GlcNAc, and fucose in a Ca(2+)-dependent manner but not to galactose [2].
• The lectin LSECtin is encoded in the same chromosomal locus as DC-SIGN/R and is coexpressed with DC-SIGNR on sinusoidal endothelial cells in liver and lymphnodes [1].

Biological context of CLEC4G

• Finally, we demonstrate that LSECtin is N-linked glycosylated and that glycosylation is required for cell surface expression [1].

Associations of CLEC4G with chemical compounds

• Ligand binding to LSECtin was inhibited by EGTA but not by mannan, suggesting that LSECtin unlike DC-SIGN/R does not recognize high-mannose glycans on viral GPs [1].

Physical interactions of CLEC4G

• LSECtin interacts with filovirus glycoproteins and the spike protein of SARS coronavirus [1].

Other interactions of CLEC4G

• In summary, we identified LSECtin as an attachment factor that in conjunction with DC-SIGNR might concentrate viral pathogens in liver and lymph nodes [1].

References