CLEC4M

CLEC4M encodes a C-type lectin receptor crucially involved in cell adhesion and diverse pathogen recognition. This receptor notably binds a wide array of evolutionarily divergent and clinically significant pathogens, including Mycobacterium tuberculosis, as well as viruses such as Ebola, Hepatitis C (HCV), HIV-1, Influenza A, West Nile virus, and the SARS-CoV acute respiratory syndrome coronavirus. Structurally, the protein is organized into four distinct domains: an N-terminal cytoplasmic domain implicated in internalization, a transmembrane region, a flexible tandem-repeat neck domain of variable length, and a C-terminal carbohydrate recognition domain (CRD). CLEC4M shares close sequence and functional homology with the neighboring gene CD209 (DC-SIGN), though they differ in specific viral recognition profiles and tissue expression patterns. CLEC4M exhibits high expression in the endothelial cells of the liver, lymph node, and placenta, and crucially, polymorphisms within its tandem-repeat neck domain have been associated with resistance to SARS infection.