Macrophage inducible Ca2+-dependent lectin, (abbreviated to mincle), is a member of the C-type lectin superfamily encoded by the gene CLEC4E. It is a receptor for mycobacterial cord factor, trehalose-6,6'-dimycolate (TDM). As a C-type lectin, the mincle receptor binds a range of carbohydrate structures, predominantly containing glucose or mannose, and play an important role in recognition of bacterial glycolipids by the immune system. Upon activation by cord factor, Mincle binds the Fc receptor FcRγ and Syk. Cord factor also binds and activates the related C-type lectin MCL.
A wide range of ligands promote signalling through Mincle. These include glucose and trehalose mycolates, and their closely related corynomycolates from mycobacteria and corynebacteria. Glycosyl diglycerides from various pathogenic and commensal bacteria and fungi such as Lactobacillus plantarum, Streptococcus pneumoniae, Mycobacterium tuberculosis and Malassezia sp. Crystalline cholesterol and the protein SAP130 also signal through Mincle.