Mannose receptor (macrophage) (CD206 (also MRC1))

The **mannose receptor (CD206)** is a type I transmembrane C-type lectin predominantly expressed on the surface of macrophages, immature dendritic cells, and certain endothelial cells[1][2][3][4][5]. It binds carbohydrate motifs such as mannose, fucose, and N-acetylglucosamine on pathogens and endogenous glycoproteins, mediating endocytosis and phagocytosis. Structurally, it possesses a cysteine-rich domain, a fibronectin type II domain, and multiple C-type lectin carbohydrate binding domains[1][2][5]. Functionally, it plays diverse roles in innate and adaptive immunity, homeostasis, and the clearance of circulating glycoproteins (including hormones). The mannose receptor is exploited by various pathogens (including bacteria, viruses, and fungi) for cell entry and survival within macrophages, and is also a key marker for macrophage polarization and phenotyping[3][4][5]. As a therapeutic target, it is being investigated primarily as a route for targeted delivery to macrophages and manipulation of immune responses. There are no currently approved drugs targeting the receptor itself, but its role in drug delivery, tissue fibrosis, infection, and tumor microenvironment makes it a significant research focus[2][3][5].

Other names

Macrophage mannose receptorMRC1 (mannose receptor C-type 1)Cluster of Differentiation 206 (CD206)CLEC13D

Ligand-mediated endocytosis for drug/nanoparticle delivery targeting macrophages[3]. Exploitation by pathogens (e.g., Mycobacterium tuberculosis, HIV) for host cell entry[3][5].