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Ronald A. Barry, Stephen B. H. Kent, Michael P. McKinley, Rudolf K. Meyer, Stephen J. DeArmond, Leroy E. Hood, Stanley B. Prusiner, Scrapie and Cellular Prion Proteins Share Polypeptide Epitopes, The Journal of Infectious Diseases, Volume 153, Issue 5, May 1986, Pages 848–854, https://doi.org/10.1093/infdis/153.5.848
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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.