Langerin (CD207) (CD207)

Langerin (CD207) is a type II transmembrane C-type lectin receptor (CLR) primarily expressed on Langerhans cells, which are specialized dendritic cells found in the epidermis and mucosal tissues. The protein is characterized by its C-terminal carbohydrate recognition domain (CRD), which mediates the calcium-dependent binding of various carbohydrate motifs, including mannose, fucose, and N-acetylglucosamine. This interaction is crucial for the recognition and internalization of pathogens such as HIV-1, Candida albicans, and Mycobacterium leprae. Upon ligand binding, Langerin facilitates the formation of Birbeck granules, unique organelles where pathogens are sequestered and degraded, thereby acting as a natural barrier against viral transmission. In therapeutic development, the Langerin CRD is targeted using glycomimetics and synthetic ligands to deliver antigens specifically to Langerhans cells for cancer vaccines and immunotherapies. Additionally, Langerin serves as a definitive diagnostic biomarker for Langerhans cell histiocytosis (LCH).

Other names

CD207CLEC4KC-type lectin domain family 4 member KLangerhans cell-specific lectin

Binding to carbohydrate moieties (mannose, fucose, GlcNAc) on pathogens or ligands via the carbohydrate recognition domain (CRD), followed by internalization into Birbeck granules for degradation or antigen processing.