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The B-cell receptor (BCR) is a membrane-bound immunoglobulin molecule expressed on the surface of B lymphocytes that specifically recognizes antigens and initiates adaptive immune signaling[1][3]. Upon activation, B cells proliferate and differentiate into plasma cells that secrete soluble antibodies with identical antigen specificity, including those directed against the prion protein (PrP). Anti-PrP antibodies (derived from immunized animals, recombinant libraries, or natural human repertoires) specifically bind to either native or misfolded forms of cellular prion protein (PrP^C^ and PrP^Sc^), and can block the pathological conversion of PrP or clear prion aggregates, showing therapeutic promise in prion diseases[4][6][7]. While BCR is targeted in B-cell lymphomas and certain autoimmune diseases, anti-PrP antibodies are primarily researched as potential therapies for neurodegenerative prion disorders. Note: The submitted target string describes two mechanistically linked immunological entities rather than a standard single molecular target; it combines an immune receptor (BCR) and a derived antibody class (anti-PrP). For precise structured data and biomedical usage, these should ideally be separated, but both are valid therapeutic targets in their respective settings.
BCR inhibitors: Block BCR signaling to halt B-cell survival/proliferation (e.g., kinase inhibitors, anti-CD20 antibodies) Anti-PrP antibodies: Bind prion protein (PrP^C^), prevent conversion to PrP^Sc^ or facilitate clearance, inhibit prion propagation and neurotoxicity
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