Ultrastructural immune-localization of synthetic prion protein peptide antibodies in 87V murine scrapie

Jeffrey, M., Goodsir, C. M., Fowler, N., Hope, J., Bruce, M. E. and McBride, P. A. (1996) Ultrastructural immune-localization of synthetic prion protein peptide antibodies in 87V murine scrapie. Neurodegeneration, 5 (1). pp. 101-109. ISSN 1055-8330

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Abstract

Disease specific forms of a host encoded cell surface sialoglycoprotein called prion protein (PrP) accumulate during the incubation period of the transmissible spongiform encephalopathies. A 33-35 kDa disease specific form of PrP is partially resistant to protease digestion whereas the normal form of PrP can be completely digested. Proteinase K digestion of the murine disease specific form of PrP produces diverse forms of low molecular weight PrP, some of which are N-terminally truncated at amino acid residue 49 or 57 within the octapeptide repeat segment. Amyloid plaques are a pathological feature of many of the transmissible spongiform encephalopathies and are composed of PrP. Using synthetic peptide antibodies to the N-terminus of PrP (which is not present in truncated disease specific PrP) and antibodies to the protease resistant fraction of PrP we have immunostained plaques and pre-amyloid deposits in the brains of mice, experimentally infected with the 87V strain of scrapie, for examination by light and electron microscopy. Classical fibrillar amyloid deposits in plaques as well as pre-amyloid deposits were both immunostained by antibodies to the N-terminus of PrP and to the protease resistant core of the PrP molecule. This suggests that both N-terminal and core amino acid residues are present in disease specific PrP released from scrapie infected cells in vivo. The results also suggest that N-terminal truncation of PrP may not be essential for formation of amyloid fibrils.

Item Type:	Article
Uncontrolled Keywords:	amyloid,immunogold,prion protein,scrapie,ultrastructure,pathology and forensic medicine,neuropsychology and physiological psychology,clinical neurology ,/dk/atira/pure/subjectarea/asjc/2700/2734
Faculty \ School:	Faculty of Science > School of Biological Sciences
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	02 Dec 2025 15:30
Last Modified:	10 Dec 2025 14:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/101193
DOI:	10.1006/neur.1996.0014

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