CD368 antibody targets the CD368 antigen, a C-type lectin receptor also known as CLEC4M or L-SIGN (Liver/lymph node-Specific ICAM-3 Grabbing Non-integrin). Identified in the early 2000s, CD368 is primarily expressed on endothelial cells in liver sinusoids and lymph nodes. It plays a role in pathogen recognition, binding high-mannose glycans on viral envelope proteins, including those from HIV, HCV, SARS-CoV, and Ebola virus, facilitating viral entry or immune modulation. Structurally, CD368 contains a carbohydrate-recognition domain (CRD) critical for interactions with pathogens and immune cells, such as ICAM-3 on T cells, suggesting a dual role in pathogen capture and T-cell adhesion.
Research on CD368 antibodies has focused on their therapeutic and diagnostic potential. Antibodies blocking CD368-pathogen interactions may inhibit viral infection, while others could enhance antigen presentation by targeting viral glycans to immune cells. CD368 is also implicated in immune tolerance and inflammatory diseases, with studies exploring its role in liver fibrosis, cancer metastasis, and autoimmune disorders. However, functional redundancy with DC-SIGN (CD209), a related lectin, complicates its specific pathway analysis. Current efforts aim to develop CD368-specific monoclonal antibodies for targeted therapies or as biomarkers for disease progression, particularly in viral infections and immune-mediated conditions.