The Mannose Receptor (MR), a member of the vertebrate C-type lectin family, is a pattern recognition receptor that is involved in both innate and adaptive immunity. The 180 kDa transmembrane protein consists of 5 domains: an amino-terminal cysteine-rich region, a fibronectin type II repeat, a series of eight tandem lectin-like carbohydrate recognition domains (responsible for the recognition of mannose and fucose), a transmembrane domain, and an intracellular carboxy-terminal tail. The structure is shared by the family of multi lectin mannose receptors: the phospholipase A2-receptor, DEC 205 and the novel C-type lectin receptor (mannose receptor X). The MR recognises a wide range of gram positive and gram negative bacteria, yeasts, parasites and mycobacteria. The MR has also been shown to bind and internalize tissue-type plasminogen activator. MR's are present on monocytes and dendritic cells (DC) and are presumed to play a role in innate and adaptive immunity, the latter via processing by DC. The expression of MR as observed in immunohistology is present on tissue macrophages, dendritic cells, a subpopulation of endothelial cells, Kupffer cells and sperm cells.

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