Scrapie and Cellular Prion Proteins Share Polypeptide Epitopes

• Published in: The Journal of infectious diseases Vol. 153; no. 5; pp. 848 - 854
• Main Authors: Barry, Ronald A., Kent, Stephen B. H., McKinley, Michael P., Meyer, Rudolf K., DeArmond, Stephen J., Hood, Leroy E., Prusiner, Stanley B.
• Format: Journal Article
• Language: English
• Published: Chicago, IL The University of Chicago Press 01.05.1986; University of Chicago Press
• Subjects: Amino acids; Amyloid - immunology; Amyloids; Animals; Antibodies; Antigens, Viral - immunology; Antiserum; Biological and medical sciences; Brain - microbiology; Brain Chemistry; Cricetinae; Enzyme-Linked Immunosorbent Assay; Epitopes; Epitopes - immunology; Fundamental and applied biological sciences. Psychology; Immune Sera; Immunoblotting; Microbiology; Morphology, structure, chemical composition, physicochemical properties; Nervous system diseases; Orginal Articles; Peptides - immunology; Prions; Prions - immunology; Proteins; Reactivity; Scrapie - metabolism; Scrapie - microbiology; Virology; Virus; Proteins; Antigenic determinant; Electron microscopy; ELISA assay; Scrapie agent
• ISSN: 0022-1899; 1537-6613
• DOI: 10.1093/infdis/153.5.848

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.