C-type lectin domain family 4 member K (Langerin) (CD207)

Langerin (CD207) is a type II transmembrane C-type lectin receptor (CLR) specifically expressed by Langerhans cells, which are specialized dendritic cells found in the skin and other mucosal epithelia (UniProt Q9UJ71). It functions as a pattern recognition receptor that identifies carbohydrate motifs such as mannose, fucose, and N-acetylglucosamine on the surface of various pathogens, including HIV-1, Candida albicans, and Mycobacterium leprae (PubMed: 10649988). Upon ligand binding, Langerin mediates the internalization of these pathogens into Birbeck granules, unique tennis-racket-shaped organelles that facilitate antigen processing and degradation (PubMed: 10649988). In the context of HIV-1 infection, Langerin is generally considered protective as it captures and destroys the virus, preventing its transmission to T cells, though this barrier can be bypassed at high viral titers (PubMed: 17351628). Due to its specific expression and endocytic capability, Langerin is a target of interest for transdermal vaccine delivery and the treatment of Langerhans cell histiocytosis, a rare cancer characterized by the proliferation of Langerin-positive cells (PubMed: 23547071). Current pharmacological research focuses on developing high-affinity glycomimetics and targeted antibodies to modulate Langerin's role in immunity and disease (PubMed: 28846404).

Other names

LangerinCLEC4KCD207 antigenLangerhans cell-specific lectin

Langerin acts as a pattern recognition receptor that binds to carbohydrate moieties on pathogens, triggering endocytosis into Birbeck granules for degradation or antigen processing.