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Infection‐specific Prion Protein (PrP) Accumulates on Neuronal Plasmalemma in Scrapie‐infected Mice
Author(s) -
JEFFREY M.,
GOODSIR C. M.,
BRUCE M. E.,
McBRIDE P. A.,
SCOTT J. R.
Publication year - 1994
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1994.tb38923.x
Subject(s) - scrapie , immunogold labelling , neuropil , electron microscope , fibril , neurite , negative stain , biology , amyloid (mycology) , microbiology and biotechnology , chemistry , biophysics , prion protein , pathology , ultrastructure , biochemistry , anatomy , in vitro , neuroscience , medicine , disease , physics , botany , optics , central nervous system
Prion protein (PrP) is an abundant membrane-associated host protein which accumulates in abnormal, relatively protease-resistant forms in the brains of animals with scrapie and related diseases. Using correlative light and electron microscopy we determined the sites of subcellular localization of PrP in mice infected with the 87V strain of scrapie. Disease-specific accumulation of PrP was observed at light microscopy as amyloid plaques or as diffuse or granular staining within the neuropil, often clearly associated with individual neurons. Serial electron microscopical preparations were immunostained for PrP by the immunogold method. Gold particles were located on amyloid fibrils and on the plasmalemma of neurites at the periphery of plaques and in the neuropil, irrespective of the morphological form of PrP accumulation when viewed by light microscopy. This suggests the amyloid fibrils are formed following the accumulation and aggregation of sub-unit proteins at the plasmalemma and, furthermore, that normal PrP may be converted to its pathological form at this site.