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An Antibody to the Aggregated Synthetic Prion Protein Peptide (PrP106–126) Selectively Recognizes Disease-Associated Prion Protein (PrPSc) from Human Brain Specimens

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Human prion diseases are characterized by the conversion of the normal host cellular prion protein (PrPC) into an abnormal misfolded form [disease-associated prion protein (PrPSc)]. Antibodies that are capable of distinguishing between PrPC and PrPSc may prove to be useful, not only for the diagnosis of these diseases, but also for a better understanding of the molecular mechanisms involved in disease pathogenesis. In an attempt to produce such antibodies, we immunized mice with an aggregated peptide spanning amino acid residues 106 to 126 of human PrP (PrP106–126). We were able to isolate and single cell clone a hybridoma cell line (P1:1) which secreted an IgM isotype antibody [monoclonal antibody (mAb P1:1)] that recognized the aggregated, but not the monomeric form of the immunogen. When used in immunoprecipitation assays, the antibody did not recognize normal PrPC from non-prion disease brain specimens, but did selectively immunoprecipitate full-length PrPSc from cases of variant and sporadic Creutzfeldt–Jakob disease and Gerstmann–Straussler–Scheinker disease. These results suggest that P1:1 recognizes an epitope formed during the structural rearrangement or aggregation of the PrP that is common to the major PrPSc types found in the most common forms of human prion disease.
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Keywords: Creutzfeldt-Jakob disease; PrP106–126; immunoprecipitation; monoclonal antibody; prion protein

Document Type: Research Article

Affiliations: 1: National CJD Surveillance Unit, School of Molecular and Clinical Medicine (Pathology), University of Edinburgh, Western General Hospital, Edinburgh, UK. 2: Strathclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, Glasgow, UK. 3: Neuropathogenesis Unit, Roslin Institute and R (D) SVS, University of Edinburgh, Edinburgh, UK. 4: SNBTS Products and Components R & D, National Science Laboratory, Edinburgh, UK.

Publication date: April 1, 2009

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