Mannose receptor and Dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (Mannose receptor (MR or CD206); Dendritic cell-specific ICAM-3-grabbing non-integrin (DC-SIGN or CD209))

The Mannose receptor (CD206) and DC-SIGN (CD209) are both C-type lectin receptors expressed on dendritic cells (DCs) as well as on certain macrophages and endothelial cells[6][2]. Both receptors mediate pathogen recognition via binding to mannose-rich and related glycans typically found on viral, bacterial, fungal, and parasitic pathogens[6][1][3]. The mannose receptor is a large type I transmembrane protein involved primarily in endocytosis, antigen processing, and immune regulation, and its soluble form can serve as a biomarker for inflammatory disease[6]. DC-SIGN is a type II transmembrane protein that forms clusters (tetramers) on the DC surface and is important for both cell adhesion (via binding to ICAM-3 and ICAM-2) and immune recognition or evasion by several pathogens (notably HIV and HCV)[1][2][3]. Both receptors are the focus of vaccine and immunotherapy research as potential targets for antigen targeting or modulation of immune responses, but challenges exist due to their roles in immune suppression, complex glycan recognition, and the risk of hijacking by pathogens[7][1][2].

Other names

CD206MRC1Macrophage mannose receptorCD209DCSIGNCLEC4LDendritic cell-specific ICAM-3-grabbing non-integrin

Targeting for antigen delivery to enhance immunogenicity (vaccine platforms); Blocking pathogen binding to prevent infection or immune evasion; Modulating antigen uptake and presentation to alter immune tolerance or activation.