Macrophage galactose-type lectin (MGL)

Macrophage galactose-type lectin (MGL) is a C-type (calcium-dependent) lectin receptor primarily expressed on immature monocyte-derived dendritic cells and activated macrophages[1][2][3][5]. It recognizes glycans terminated with N-acetylgalactosamine (GalNAc) and galactose, enabling the binding and endocytosis of glycoproteins present on pathogens (such as bacteria and viruses), tumor cells, and self glycoproteins displaying the Tn and sialyl-Tn antigens[1][2][4][5][6]. Through its extracellular carbohydrate recognition domain, MGL modulates innate and adaptive immune responses by mediating antigen uptake and influencing antigen presentation pathways, including MHC class I and II loading[3]. Beyond pathogen recognition, MGL has a role in tumor immunology by interacting with aberrantly glycosylated cancer-associated antigens and can contribute to immune tolerance and regulation[3][5]. It is studied as a potential target for cancer immunotherapy, infectious disease intervention, and as a biomarker of immune function or tumor microenvironmental status[2][3][5].

Other names

C-type lectin domain family 10 member ACD301CLEC10AHMLMGL1 (mouse)MGL2 (mouse)

Targeting by glycan-modified ligands to modulate antigen uptake and immune response; Exploitation by pathogens and tumors for immune evasion via glycosylation patterns