Biomaterial Database

Properties of scrapie prion proteins in liposomes and amyloid rods. 1988

R Gabizon, and M P McKinley, and S B Prusiner

Department of Neurology, University of California, San Francisco 94143.

The scrapie prion protein (PrP 27-30) has been demonstrated to be required for infectivity. Aggregates of PrP 27-30 form insoluble amyloid rods which resist dissociation by non-denaturing detergents. Mixtures of the detergent cholate and phospholipids were found to solubilize PrP 27-30 with full retention of scrapie prion infectivity. No evidence for a prion-associated nucleic acid could be found when the phospholipid vesicles with PrP 27-30 were digested with nucleases and Zn2+. Under digestion conditions which allowed hydrolysis of exogenous nucleic acids, no diminution of prion infectivity was observed. Tobacco mosaic virions added to the liposomes at a concentration 100 times lower than the scrapie prion titre could be seen by electron microscopy. These studies indicate that there is no subpopulation of filamentous scrapie viruses hidden amongst the prion rods - indeed, they would have been observed among the liposomes. The partitioning of PrP 27-30 and scrapie infectivity into phospholipid vesicles argues for a central role of PrP 27-30 in scrapie pathogenesis and establishes that the prion amyloid rods are not essential for infectivity.

UI	MeSH Term	Description	Entries
D008081	Liposomes	Artificial, single or multilaminar vesicles (made from lecithins or other lipids) that are used for the delivery of a variety of biological molecules or molecular complexes to cells, for example, drug delivery and gene transfer. They are also used to study membranes and membrane proteins.	Niosomes,Transferosomes,Ultradeformable Liposomes,Liposomes, Ultra-deformable,Liposome,Liposome, Ultra-deformable,Liposome, Ultradeformable,Liposomes, Ultra deformable,Liposomes, Ultradeformable,Niosome,Transferosome,Ultra-deformable Liposome,Ultra-deformable Liposomes,Ultradeformable Liposome
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
D011328	Prions	Small proteinaceous infectious particles which resist inactivation by procedures that modify NUCLEIC ACIDS and contain an abnormal isoform of a cellular protein which is a major and necessary component. The abnormal (scrapie) isoform is PrPSc (PRPSC PROTEINS) and the cellular isoform PrPC (PRPC PROTEINS). The primary amino acid sequence of the two isoforms is identical. Human diseases caused by prions include CREUTZFELDT-JAKOB SYNDROME; GERSTMANN-STRAUSSLER SYNDROME; and INSOMNIA, FATAL FAMILIAL.	Mink Encephalopathy Virus,Prion,Encephalopathy Virus, Mink
D002627	Chemistry, Physical	The study of CHEMICAL PHENOMENA and processes in terms of the underlying PHYSICAL PHENOMENA and processes.	Physical Chemistry,Chemistries, Physical,Physical Chemistries
D000682	Amyloid	A fibrous protein complex that consists of proteins folded into a specific cross beta-pleated sheet structure. This fibrillar structure has been found as an alternative folding pattern for a variety of functional proteins. Deposits of amyloid in the form of AMYLOID PLAQUES are associated with a variety of degenerative diseases. The amyloid structure has also been found in a number of functional proteins that are unrelated to disease.	Amyloid Fibril,Amyloid Fibrils,Amyloid Substance,Fibril, Amyloid,Fibrils, Amyloid,Substance, Amyloid
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
D014764	Viral Proteins	Proteins found in any species of virus.	Gene Products, Viral,Viral Gene Products,Viral Gene Proteins,Viral Protein,Protein, Viral,Proteins, Viral
D055598	Chemical Phenomena	The composition, structure, conformation, and properties of atoms and molecules, and their reaction and interaction processes.	Chemical Concepts,Chemical Processes,Physical Chemistry Concepts,Physical Chemistry Processes,Physicochemical Concepts,Physicochemical Phenomena,Physicochemical Processes,Chemical Phenomenon,Chemical Process,Physical Chemistry Phenomena,Physical Chemistry Process,Physicochemical Phenomenon,Physicochemical Process,Chemical Concept,Chemistry Process, Physical,Chemistry Processes, Physical,Concept, Chemical,Concept, Physical Chemistry,Concept, Physicochemical,Concepts, Chemical,Concepts, Physical Chemistry,Concepts, Physicochemical,Phenomena, Chemical,Phenomena, Physical Chemistry,Phenomena, Physicochemical,Phenomenon, Chemical,Phenomenon, Physicochemical,Physical Chemistry Concept,Physicochemical Concept,Process, Chemical,Process, Physical Chemistry,Process, Physicochemical,Processes, Chemical,Processes, Physical Chemistry,Processes, Physicochemical
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