The major polypeptide of scrapie-associated fibrils (SAF) has the same size, charge distribution and N-terminal protein sequence as predicted for the normal brain protein (PrP)

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Hope, J. ORCID: https://orcid.org/0000-0003-2015-2389, Morton, L. J., Farquhar, C. F., Multhaup, G., Beyreuther, K. and Kimberlin, R. H. (1986) The major polypeptide of scrapie-associated fibrils (SAF) has the same size, charge distribution and N-terminal protein sequence as predicted for the normal brain protein (PrP). The EMBO Journal, 5 (10). pp. 2591-2597. ISSN 0261-4189

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Abstract

Scrapie-associated fibrils (SAF) are unique structures characteristic of the group of unconventional slow infections which includes scrapie and Creutzfeldt-Jakob disease. A major component of hamster fibrils has been described as a protease-resistant glycoprotein with an apparent mol. wt of 27,000-30,000 (PrP27-30). However, we report here that if fibrils are prepared by procedures designed to minimise proteolysis the PrP proteins co-purifying with hamster SAF have mol. wts of 33,000-35,000 (PrP33-35) and 26,000-29,000 (PrP26-29). We find a Lys-Lys-Arg-Pro-Lys sequence at the amino terminus of these SAF proteins, that is absent from PrP27-30, and which has recently been predicted to be the N-terminal sequence of the native PrP protein of uninfected brain. The major SAF protein (PrP33-35) and its normal brain homologue are shown to have the same apparent mol. wt and ionic charge distribution by two-dimensional gel analysis, silver staining and immunoblotting. These results support our view that PrP33-35 and the normal brain PrP protein may have the same covalent structure, and that the PrP protein is recruited into these amyloid-like SAF or into association with a non-protein component of SAF by an irreversible event initiated directly or indirectly by scrapie infection.

Item Type: Article
Uncontrolled Keywords: general neuroscience,molecular biology,general biochemistry,genetics and molecular biology,general immunology and microbiology ,/dk/atira/pure/subjectarea/asjc/2800/2800
Faculty \ School: Faculty of Science > School of Biological Sciences
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Depositing User: LivePure Connector
Date Deposited: 28 Nov 2025 11:30
Last Modified: 18 Jun 2026 20:48
URI: https://ueaeprints.uea.ac.uk/id/eprint/101142
DOI: 10.1002/j.1460-2075.1986.tb04539.x

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