Scrapie and Cellular Prion Proteins Share Polypeptide Epitopes

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Abstract
Purified preparations of scrapie prions contain one major protein, PrP 27–30, and aggregates of rod-shaped structures. On the basis of the NH2-terminal amino acid sequence of PrP 27–30, a synthetic peptide (PrP-P1) was constructed. Monospecific rabbit antisera to PrP-P1 were found by immunoblotting to react with PrP 27–30 and its precursor (PrP 33–35Sc) , as well as with a related protease-sensitive cellular homologue (PrP 33–35C) . An enzyme-linked immunosorbent assay showed that rabbit antiserum to PrP 27–30 was more reactive with PrP 27–30 than with PrP-P1; conversely, antiserum to PrP-P1 was more reactive with the peptide than with the prion proteins. In addition, antibodies to PrP-Pl decorate purified prion rods and stain amyloid plaques in scrapie-infected hamster brain. The peptide epitopes shared by PrP 27–30, PrP 33-35Sc, and PrP 33–35C clearly establish a relationship among these three proteins.