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Monoclonal antibody against a peptide of human prion protein discriminates between Creutzfeldt-Jacob's disease-affected and normal brain tissue
Čurin-Šerbec, Vladka ...
Current methods for diagnosing transmissible spongiform encephalopathies rely on degradation of PrPC and subsequent detection of the protease-resistant remnant of the PrPSc by antibodies that react ...with all forms of PrP. We report a monoclonal antibody V5B2, raised against a peptide from the C-terminalpart of PrP, which recognizes an epitope specific to PrPSc. In cryostat sections from CJD patientsć brains, V5B2 selectively labels various deposits of PrPSc, without any pretreatment for removal of PrPC. V5B2 does not bind to non-CJD brain samples or to recombinant PrP, either in its native or denatured form. Specificity for PrP is confirmed by sandwich ELISA utilizing V5B2, which discriminates between CJD and normal samples without proteinase K treatment and by immunoprecipitation from CJD brain homogenate. The PrPSc specific epitope is disrupted by denaturation. We conclude that the C-terminal part of PrP in disease-associated PrPSc aggregates forms a structural epitope whose conformation is distinct from that of PrPC.
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