Characterization of prion proteins with monospecific antisera to synthetic peptides.
The prion protein (PrP) 27-30 is the major macromolecular component in highly purified preparations of prions derived from scrapie-infected hamster brain. Immunoblotting studies demonstrated that this protein is generated by partial protease digestion of a larger precursor (PrPSc) with an apparent Mr of 33 to 35 kDa, and that a protease-sensitive cellular PrP isoform, designated PrPC, is present in normal hamster brain. To characterize the relationships among these proteins, ELISA and immunoblotting studies were undertaken with rabbit antisera raised against three synthetic PrP peptides. All three antisera were found to specifically react with the prion proteins, and failed to identify other lower or higher m.w. PrP proteins. Our results provide evidence that the primary structures of PrP 27-30, PrPSc, and PrPC are related; this conclusion supports molecular cloning studies indicating that these proteins are encoded by the same chromosomal gene.
D000818:Animals; D000914:Antibodies, Viral / Q000276:immunology; D006224:Cricetinae; D008970:Molecular Weight; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000276:immunology*; D011328:Prions / Q000235:genetics / Q000276:immunology*; D011498:Protein Precursors / Q000378:metabolism; D014764:Viral Proteins / Q000096:biosynthesis / Q000235:genetics / Q000276:immunology*
D000914:Antibodies, Viral; D010446:Peptide Fragments; D011328:Prions; D011498:Protein Precursors; D014764:Viral Proteins