Immunoaffinity purification and neutralization of scrapie prion infectivity.
نویسندگان
چکیده
منابع مشابه
Immunoaffinity purification and neutralization of scrapie prion infectivity.
Prions are unusual infectious pathogens causing scrapie of sheep and goats as well as Creutzfeldt-Jakob disease of humans. Biochemical and genetic studies contend that the scrapie isoform of the prion protein (PrPSc) is a major component of the prion. Limited proteinase K digestion of PrPSc produced a protein of 27-30 kDa. After dispersion of brain microsomes isolated from scrapie-infected hams...
متن کاملPurified prion proteins and scrapie infectivity copartition into liposomes.
Considerable evidence indicates that the scrapie prion protein (PrP 27-30) is required for infectivity. Aggregates of PrP 27-30 form insoluble amyloid rods that resist dissociation by nondenaturing detergents. Mixtures of the detergent cholate and phospholipids were found to solubilize purified PrP 27-30 in the form of detergent-lipid-protein complexes. Removal of the cholate by dialysis result...
متن کاملTransfer of Scrapie Prion Infectivity by Cell Contact in Culture
BACKGROUND When a cell is infected with scrapie prions, newly synthesized molecules of the prion protein PrP(C) are expressed at the cell surface and may subsequently be converted to the abnormal form PrP(Sc). In an experimental scrapie infection of an animal, the initial innoculum of PrP(Sc) is cleared relatively rapidly, and the subsequent propagation of the infection depends on the ability o...
متن کاملDetection of Prion Infectivity in Fat Tissues of Scrapie-Infected Mice
Distribution of prion infectivity in organs and tissues is important in understanding prion disease pathogenesis and designing strategies to prevent prion infection in animals and humans. Transmission of prion disease from cattle to humans resulted in banning human consumption of ruminant nervous system and certain other tissues. In the present study, we surveyed tissue distribution of prion in...
متن کاملPerturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity.
Limited proteolysis of the scrapie prion protein (PrPSc) generates PrP 27-30, which polymerizes into amyloid. By attenuated total reflection-Fourier transform infrared spectroscopy, PrP 27-30 polymers contained 54% beta-sheet, 25% alpha-helix, 10% turns, and 11% random coil; dispersion into detergent-lipid-protein-complexes preserved infectivity and secondary structure. Almost 60% of the beta-s...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1988
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.85.18.6617