CD207, also known as Langerin, is a type II transmembrane protein encoded by the CD207 gene in humans . It is primarily expressed on Langerhans cells (LCs), which are a specialized subset of dendritic cells found in the epidermis and mucosal tissues . Langerin plays a crucial role in the immune system by recognizing and binding to specific carbohydrates on the surface of pathogens, facilitating their internalization and subsequent antigen presentation to T-cells .
CD207 was discovered by scientists Sem Saeland and Jenny Valladeau as a main component of Birbeck granules, which are unique organelles found in LCs . The protein consists of a relatively short intracellular domain and an extracellular domain that includes a neck region and a carbohydrate recognition domain (CRD) . The intracellular part contains a proline-rich domain (PRD), while the neck region, composed of alpha-helices, mediates the formation of langerin homotrimers via coiled-coil interactions . This trimerization increases the avidity and specificity of antigen binding .
Langerin is involved in the immune response by recognizing and binding to carbohydrates such as mannose, fucose, and N-acetylglucosamine . This binding allows LCs to react against various pathogens, including HIV-1, Mycobacterium leprae, and Candida albicans . Upon binding to a pathogen, langerin internalizes the pathogen into Birbeck granules, where it is degraded and processed for antigen presentation to T-cells .
CD207 is a valuable tool in immunological research, particularly in the study of LCs and their interactions with pathogens . It is also used in drug testing and the development of therapeutic strategies for diseases involving LCs, such as Langerhans cell histiocytosis (LCH) . The recombinant form of CD207 allows researchers to investigate the molecular mechanisms underlying LC function and their role in immune responses .