Biomaterial Database

Comparison of scrapie-associated fibril detection and Western immunoblotting for the diagnosis of natural ovine scrapie. 1998

W A Cooley, and J K Clark, and M J Stack

Veterinary Laboratories Agency, Central Veterinary Laboratory, Weybridge, Surrey, UK.

Detergent- and proteinase K-treated extracts of grey matter were prepared from four regions of the brains of 106 sheep with scrapie, diagnosed clinically and by the demonstration of spongiform encephalopathy. The extracts were examined by electron microscopy for the presence of scrapie-associated fibrils and by Western immunoblotting for the disease-specific abnormal prion protein (PrPSc). As a diagnostic method, Western immunoblotting proved to be more sensitive than electron microscopy, the detection rates in the 106 sheep being 97 and 91% respectively (medulla), 99 and 76% (cerebellum), 95 and 88% (frontal cerebral cortex) and 93 and 61% (occipital cerebral cortex). Neither fibrils nor PrPSc could be detected in comparable brain extracts from 25 control sheep which had shown no clinical or histopathological evidence of scrapie.

UI	MeSH Term	Description	Entries
D008854	Microscopy, Electron	Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.	Electron Microscopy
D002531	Cerebellum	The part of brain that lies behind the BRAIN STEM in the posterior base of skull (CRANIAL FOSSA, POSTERIOR). It is also known as the "little brain" with convolutions similar to those of CEREBRAL CORTEX, inner white matter, and deep cerebellar nuclei. Its function is to coordinate voluntary movements, maintain balance, and learn motor skills.	Cerebella,Corpus Cerebelli,Parencephalon,Cerebellums,Parencephalons
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D012608	Scrapie	A fatal disease of the nervous system in sheep and goats, characterized by pruritus, debility, and locomotor incoordination. It is caused by proteinaceous infectious particles called PRIONS.	Rida
D012756	Sheep	Any of the ruminant mammals with curved horns in the genus Ovis, family Bovidae. They possess lachrymal grooves and interdigital glands, which are absent in GOATS.	Ovis,Sheep, Dall,Dall Sheep,Ovis dalli
D015153	Blotting, Western	Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.	Immunoblotting, Western,Western Blotting,Western Immunoblotting,Blot, Western,Immunoblot, Western,Western Blot,Western Immunoblot,Blots, Western,Blottings, Western,Immunoblots, Western,Immunoblottings, Western,Western Blots,Western Blottings,Western Immunoblots,Western Immunoblottings
D017096	Prion Diseases	A group of genetic, infectious, or sporadic degenerative human and animal nervous system disorders associated with abnormal PRIONS. These diseases are characterized by conversion of the normal prion protein to an abnormal configuration via a post-translational process. In humans, these conditions generally feature DEMENTIA; ATAXIA; and a fatal outcome. Pathologic features include a spongiform encephalopathy without evidence of inflammation. The older literature occasionally refers to these as unconventional SLOW VIRUS DISEASES. (From Proc Natl Acad Sci USA 1998 Nov 10;95(23):13363-83)	Dementias, Transmissible,Spongiform Encephalopathies, Transmissible,Transmissible Dementias,Encephalopathies, Spongiform, Transmissible,Human Transmissible Spongiform Encephalopathies, Inherited,Inherited Human Transmissible Spongiform Encephalopathies,Prion Disease,Prion Protein Diseases,Prion-Associated Disorders,Prion-Induced Disorder,Prion-Induced Disorders,Transmissible Spongiform Encephalopathies,Dementia, Transmissible,Disorder, Prion-Induced,Disorders, Prion-Induced,Encephalopathies, Transmissible Spongiform,Encephalopathy, Transmissible Spongiform,Prion Induced Disorder,Prion Protein Disease,Spongiform Encephalopathy, Transmissible,Transmissible Dementia,Transmissible Spongiform Encephalopathy
D018622	PrP 27-30 Protein	Protease-resistant core of PrPSc, the abnormal isoform of PRION PROTEINS. PrP 27-30 is produced by limited proteolysis of the N-terminus of PrPSc.	Scrapie-Associated Fibrils,Fibril-Protein, Scrapie-Associated,Fibrils, Scrapie-Associated,Scrapie Associated Fibril-Protein,Scrapie PrP 27-30 Protein,Scrapie-Associated Fibril-Protein,Associated Fibril-Protein, Scrapie,Fibril Protein, Scrapie Associated,Fibril-Protein, Scrapie Associated,Fibrils, Scrapie Associated,PrP 27 30 Protein,Scrapie Associated Fibril Protein,Scrapie Associated Fibrils,Scrapie PrP 27 30 Protein

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