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Cluster of differentiation 15 (CD15), also known as Lewis X (LeX) or 3-fucosyl-N-acetyllactosamine, is a carbohydrate antigen primarily expressed on the surface of mature human neutrophils, eosinophils, and monocytes [1, 3]. It serves as a critical adhesion molecule by interacting with selectins (E-, P-, and L-selectin), facilitating the tethering and rolling of leukocytes on vascular endothelium during the inflammatory response [1, 9]. In clinical pathology, CD15 is a vital diagnostic marker for classical Hodgkin lymphoma, where it is characteristically expressed on Reed-Sternberg cells, and it is also utilized in the characterization of certain acute myeloid leukemias [8, 9]. While primarily used for diagnostic purposes, CD15 is an emerging therapeutic target for monoclonal antibodies and immunotherapies designed to inhibit tumor metastasis and modulate immune cell recruitment [1, 3]. However, the development of CD15-targeted therapies faces significant challenges due to its high expression on normal granulocytes, which poses a risk of systemic neutropenia and other myeloid-related toxicities [1, 3].
CD15-targeted agents typically work by binding to the carbohydrate moiety on the cell surface, which can block interactions with selectins (E-, P-, and L-selectin) to inhibit cell adhesion and metastasis, or trigger immune-mediated destruction of the target cell via complement-dependent cytotoxicity (CDC) [1, 3].
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