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Scrapie-associated precursor proteins

Antigenic relationship between species and immunocytochemical localization in normal, scrapie, and Creutzfeldt-Jakob disease brains

Laboratory of Central Nervous System Studies, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD.

We describe the antigenic properties and detection of a normal isoform of scrapie-associated precursor protein (PrP33–35^C) in normal, and both normal and scrapie isoforms in scrapie- or Creutzfeldt-Jakob disease (CJD)-infected mouse, hamster, and human brains, using a variety of specific antibodies. Polyclonal antibodies raised against mouse and hamster PrP27–30 and against a synthetic peptide of the N-terminal sequence of this protein were used as immunologic probes. PrP27–30 purified as a primary immunogen corresponded to the lower molecular mass peptide, with M, between 9.3 and 13.5 kd as estimated by size-exclusion high-pressure liquid chromatography. ELISA and immunoblot techniques demonstrated that antibodies recognized homologous antigens as well as precursor proteins from normal brains (PrP33–35^C) and the scrapie isoform of scrapie-associated proteins (PrP33–35^Sc/CJD and PrP27–30) from scrapie- and CJD-infected brains. The normal, scrapie, and CJD isoforms of scrapie-associated proteins share common epitopes with varying degrees of interspecies homology. Specific antigen detected in neurons indicated that these proteins are synthesized primarily in these cells. In infected brains, extracellular amyloid deposits formed by the scrapie isoform of PrP protein also strongly reacted with anti-PrP antibodies.

Address correspondence and reprint requests to Dr. Clarence J. Gibbs, Jr., Laboratory of Central Nervous System Studies, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892.

Received March 28, 1989. Accepted for publication in final form August 25, 1989.