Scrapie prion liposomes and rods exhibit target sizes of 55,000 Da
Scrapie is a degenerative neurologic disease in sheep and goats which can be experimentally transmitted to laboratory rodents. Considerable evidence suggests that the scrapie agent is composed largely, if not entirely, of an abnormal isoform of the prion protein (PrPSc). Inactivation of scrapie prions by ionizing radiation exhibited single-hit kinetics and gave a target size of 55,000 +/- 9000 mol wt. The inactivation profile was independent of the form of the prion. Scrapie agent infectivity in brain homogenates, microsomal fractions, detergent-extracted microsomes, purified amyloid rods, and liposomes exhibited the same inactivation profile. Our data are consistent with the hypothesis that the infectious particle causing scrapie contains approximately 2 PrPSc molecules.
- Research Organization:
- Univ. of California, San Francisco (USA)
- OSTI ID:
- 6992437
- Journal Information:
- Virology; (United States), Vol. 164:2
- Country of Publication:
- United States
- Language:
- English
Similar Records
Magnetic microparticle-based multimer detection system for the detection of prion oligomers in sheep
Large-scale survey of prion protein genetic variability in scrapie disease-free goats from the United States
Related Subjects
SHEEP
NERVOUS SYSTEM DISEASES
VIRUSES
BIOLOGICAL RADIATION EFFECTS
INFECTIVITY
BRAIN
IONIZING RADIATIONS
LIPOSOMES
MICROSOMES
MOLECULAR WEIGHT
PROTEINS
RODENTS
ANIMALS
BIOLOGICAL EFFECTS
BODY
CELL CONSTITUENTS
CENTRAL NERVOUS SYSTEM
DISEASES
DOMESTIC ANIMALS
MAMMALS
MICROORGANISMS
NERVOUS SYSTEM
ORGANIC COMPOUNDS
ORGANOIDS
ORGANS
PARASITES
RADIATION EFFECTS
RADIATIONS
RUMINANTS
VERTEBRATES
560130* - Radiation Effects on Microorganisms