Abstract
Mincle, the macrophage-inducible C-type lectin also known as CLEC-4E, binds to the mycobacterial glycolipid trehalose dimycolate and initiates a signaling cascade by serving as a receptor for Mycobacterium tuberculosis and other pathogenic mycobacterial species. Studies of the biological functions of human mincle often rely on mouse models, based on the assumption that the biological properties of the mouse receptor mimic those of the human protein. Experimental support for this assumption has been obtained by expression of the carbohydrate-recognition domain of mouse mincle and characterization of its interaction with small molecule analogs of trehalose dimycolate. The results confirm that the ligand-binding properties of mouse mincle closely parallel those of the human receptor. These findings are consistent with the conservation of key amino acid residues that have been shown to form the ligand-binding site in human and cow mincle. Sequence alignment reveals that these residues are conserved in a wide range of mammalian species, suggesting that mincle has a conserved function in binding ligands that may include endogenous mammalian glycans or pathogen glycans in addition to trehalose dimycolate.
Highlights
After many years as an orphan receptor, the macrophage inducible C-type lectin, known as mincle or CLEC-4E, has recently been recognized as a receptor for glycans on pathogens [1,2,3]. It is of particular interest because it can bind to trehalose dimycolate, an unusual glycolipid in the outer wall of mycobacteria
Mincle is a prototype for a novel subgroup of animal glycan-binding receptors, because in addition to containing a Ca2+-dependent carbohydrate-recognition domain (C-type CRD) it initiates signaling in macrophages by interacting with the common Fc receptor γ subunit (FcRγ subunit) [4]
The region of the polypeptide to be expressed was selected based on previous studies of human mincle (Figure 1C)
Summary
After many years as an orphan receptor, the macrophage inducible C-type lectin, known as mincle or CLEC-4E, has recently been recognized as a receptor for glycans on pathogens [1,2,3]. It is of particular interest because it can bind to trehalose dimycolate, an unusual glycolipid in the outer wall of mycobacteria. Mincle is a prototype for a novel subgroup of animal glycan-binding receptors, because in addition to containing a Ca2+-dependent carbohydrate-recognition domain (C-type CRD) it initiates signaling in macrophages by interacting with the common Fc receptor γ subunit (FcRγ subunit) [4]. One of the two glucose residues in the trehalose headgroup binds in a primary sugar-binding site that resembles that seen in other C-type
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