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Bone marrow stromal antigen 2 (BST-2), also known as CD317, Tetherin, or HM1.24, is a type II single-pass transmembrane glycoprotein expressed at high levels on myelocytes, malignant plasma cells, and several tumor types[1][3][6]. It functions as an interferon-induced antiviral restriction factor by inhibiting the release of enveloped viruses from infected cells and is targeted by certain viral proteins such as HIV-1 Vpu[1]. BST-2/HM1.24 is efficiently internalized from the cell surface, localizes to membrane lipid rafts, and is subject to regulation via N-terminal polyubiquitination[1][6]. In oncology, it is a promising therapeutic target for immunotoxins and monoclonal antibodies due to its overexpression in multiple myeloma and certain leukemia cells, with reduced but notable expression in some normal cell types[3][1]. Its biology and membrane localization are strongly linked to its antiviral and immunomodulatory functions, though its exact ubiquitination mechanism is still under study[1].
Antibody-dependent cell targeting and cytotoxicity, Immunotoxin-mediated apoptosis, Antiviral restriction by tethering viral particles to the membrane
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