Human C-Type Lectin Domain Family 4, Member L (CLEC4L) Protein

Background

CD209, commonly known as DC-SIGN (Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Non-integrin), is a type II transmembrane protein receptor primarily expressed on the surface of dendritic cells (DCs) and some macrophage subsets. It plays a crucial role in the immune system by mediating pathogen recognition, cellular adhesion, and antigen capture. CD209 is a member of the C-type lectin receptor (CLR) family and exhibits high affinity for mannose-rich glycans, a feature that enables it to bind to a range of microbial structures, facilitating the immune response against pathogens. One of CD209's defining characteristics is its ability to recognize pathogen-associated molecular patterns (PAMPs), which are specific carbohydrate patterns on pathogens. By binding to these patterns, CD209 captures and internalizes pathogens, aiding in their processing and subsequent antigen presentation to T cells. The receptor is particularly relevant in the context of HIV, Mycobacterium tuberculosis, Ebola, and Dengue virus, as it can interact with these pathogens and contribute to their immune response or facilitate viral entry in certain cases.