Prion Strains and Species Barriers

2004 ◽  
pp. 33-49 ◽  
Author(s):  
A.F. Hill ◽  
J. Collinge
Keyword(s):  
Prion Strains

Genetic Creutzfeldt–Jakob disease‐M232R with the cooccurrence of multiple prion strains, M1 +  M2C +  M2T : Report of an autopsy case

2021 ◽  
Author(s):  
Masayuki Shintaku ◽  
Takeshi Nakamura ◽  
Daita Kaneda ◽  
Akiyo Shinde ◽  
Hirofumi Kusaka ◽  
...  
Keyword(s):  
Autopsy Case ◽  
Prion Strains ◽  
Jakob Disease

scholarly journals Search for a Prion-Specific Nucleic Acid

2005 ◽  
Vol 79 (16) ◽  
pp. 10796-10806 ◽  
Author(s):  
Jiri G. Safar ◽  
Klaus Kellings ◽  
Ana Serban ◽  
Darlene Groth ◽  
James E. Cleaver ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Nucleic Acids ◽  
Uv Irradiation ◽  
Syrian Hamsters ◽  
Variable Sequence ◽  
Intracerebral Inoculation ◽  
Prion Infectivity ◽  
Prion Strains ◽  
Rapid Clearance

ABSTRACT Diversity of prion strains was attributed to an elusive nucleic acid, yet a search spanning nearly two decades has failed to identify a prion-specific polynucleotide. In our search for a prion-specific nucleic acid, we analyzed nucleic acids in purified fractions from the brains of Syrian hamsters infected with Sc237 prions. Purification of Sc237 prions removed nucleic acids larger than 50 nucleotides as measured by return refocusing electrophoresis (RRGE). To determine the size of the largest polynucleotide present in purified fractions at an abundance of one molecule per infectious (ID50) unit, we measured prions present after inoculation. In order to account for the rapid clearance of prions after intracerebral inoculation, we determined the number of PrPSc molecules and ID50 units of prions that were retained in brain. Factoring in clearance after inoculation, we estimate that the largest polynucleotide present in our purified fractions at one molecule per ID50 unit is ≈25 nucleotides in length. In the same fractions, there were ≈3,000 protease-resistant PrPSc molecules per ID50 unit after accounting for clearance of PrPSc following inoculation. We compared the resistance of Sc237 and 139H prions to inactivation by UV irradiation at 254 nm. Irradiation of homogenates and microsomes diminished prion infectivity by a factor of ≈1,000 but did not alter the strain-specified properties of the Sc237 and 139H prions. The data reported here combined with the production of synthetic prions argue that the 25-mer polynucleotides found in purified prion preparations are likely to be host encoded and of variable sequence; additionally, these 25-mers are unlikely to be prion specific.

scholarly journals Coinfecting Prion Strains Compete for a Limiting Cellular Resource

2010 ◽  
Vol 84 (11) ◽  
pp. 5706-5714 ◽  
Author(s):  
Ronald A. Shikiya ◽  
Jacob I. Ayers ◽  
Charles R. Schutt ◽  
Anthony E. Kincaid ◽  
Jason C. Bartz
Keyword(s):  
Protein Misfolding ◽  
Neuronal Loss ◽  
Infectious Agent ◽  
Prion Strain ◽  
Prion Strains ◽  
The Central Nervous System ◽  
Transmissible Mink Encephalopathy ◽  
Prion Conversion ◽  
Cellular Components

ABSTRACT Prion strain interference can influence the emergence of a dominant strain from a mixture; however, the mechanisms underlying prion strain interference are poorly understood. In our model of strain interference, inoculation of the sciatic nerve with the drowsy (DY) strain of the transmissible mink encephalopathy (TME) agent prior to superinfection with the hyper (HY) strain of TME can completely block HY TME from causing disease. We show here that the deposition of PrPSc, in the absence of neuronal loss or spongiform change, in the central nervous system corresponds with the ability of DY TME to block HY TME infection. This suggests that DY TME agent-induced damage is not responsible for strain interference but rather prions compete for a cellular resource. We show that protein misfolding cyclic amplification (PMCA) of DY and HY TME maintains the strain-specific properties of PrPSc and replicates infectious agent and that DY TME can interfere, or completely block, the emergence of HY TME. DY PrPSc does not convert all of the available PrPC to PrPSc in PMCA, suggesting the mechanism of prion strain interference is due to the sequestering of PrPC and/or other cellular components required for prion conversion. The emergence of HY TME in PMCA was controlled by the initial ratio of the TME agents. A higher ratio of DY to HY TME agent is required for complete blockage of HY TME in PMCA compared to several previous in vivo studies, suggesting that HY TME persists in animals coinfected with the two strains. This was confirmed by PMCA detection of HY PrPSc in animals where DY TME had completely blocked HY TME from causing disease.

scholarly journals Radical Change in Zoonotic Abilities of Atypical BSE Prion Strains as Evidenced by Crossing of Sheep Species Barrier in Transgenic Mice

2020 ◽  
Vol 26 (6) ◽  
pp. 1130-1139 ◽  
Author(s):  
Alba Marín-Moreno ◽  
Alvina Huor ◽  
Juan Carlos Espinosa ◽  
Jean Yves Douet ◽  
Patricia Aguilar-Calvo ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Radical Change ◽  
Species Barrier ◽  
Prion Strains

scholarly journals A novel and rapid method for obtaining high titre intact prion strains from mammalian brain

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Adam Wenborn ◽  
Cassandra Terry ◽  
Nathalie Gros ◽  
Susan Joiner ◽  
Laura D’Castro ◽  
...  
Keyword(s):  
Rapid Method ◽  
High Titre ◽  
Mammalian Brain ◽  
Prion Strains
Sign in / Sign up

Export Citation Format

Share Document