Protease-resistant and Detergent-insoluble Prion Protein Is Not Necessarily Associated with Prion Infectivity

Shaked, Gideon M.; Fridlander, Gilgi; Meiner, Zeev; Taraboulos, Albert; Gabizon, Ruth

doi:10.1074/jbc.274.25.17981

Cited by 63 publications

(35 citation statements)

References 44 publications

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“…Therefore, the levels of PK-resistant PrP species, as quantified by immunoblotting, may not be directly proportional to the infectivity titer, an observation that has also been reported by others (43).…”

Section: Prpmentioning

confidence: 55%

Biochemical Fingerprints of Prion Infection: Accumulations of Aberrant Full-Length and N-Terminally Truncated PrP Species Are Common Features in Mouse Prion Disease

Pan

Wong

Chang

et al. 2005

J Virol

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Section: Prpmentioning

confidence: 55%

Biochemical Fingerprints of Prion Infection: Accumulations of Aberrant Full-Length and N-Terminally Truncated PrP Species Are Common Features in Mouse Prion Disease

Pan

Wong

Chang

et al. 2005

J Virol

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“…Indeed, in vitro conversion experiments of PrP C to PrP Sc , in which protease resistance was achieved by a denaturation/ renaturation procedure, resulted in a protease-resistant but not infectious PrP isoform (33,34). Contrarily, UPrP Sc may resemble the new protease-resistant soluble isoform we have identified lately, which is associated with very low levels of infectivity, if any (35,36). The latest possibility is consistent with the fact that UPrP Sc is found in urine, because an aggregated molecule could not filter through the kidney.…”

Section: Why Is Uprpmentioning

confidence: 99%

A Protease-resistant Prion Protein Isoform Is Present in Urine of Animals and Humans Affected with Prion Diseases

Shaked

Kariv-Inbal

et al. 2001

Journal of Biological Chemistry

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174

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Prion protein (PrP)Sc , the only known component of the prion, is present mostly in the brains of animals and humans affected with prion diseases. We now show that a protease-resistant PrP isoform can also be detected in the urine of hamsters, cattle, and humans suffering from transmissible spongiform encephalopathies. Most important, this PrP isoform (UPrP Sc ) was also found in the urine of hamsters inoculated with prions long before the appearance of clinical signs. Interestingly, intracerebrally inoculation of hamsters with UPrP Sc did not cause clinical signs of prion disease even after 270 days, suggesting it differs in its pathogenic properties from brain PrP Sc . We propose that the detection of UPrP Sc can be used to diagnose humans and animals incubating prion diseases, as well as to increase our understanding on the metabolism of PrP Sc in vivo.

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“…However, conflicting results have also been reported. PK resistance of detergent-treated PrP res did not correlate with scrapie infectivity when isolated prion rods were exposed to different solvents (Shaked et al, 1999;Wille et al, 2000) and PrP…”

Section: Lrf~log Initial Prp Res Titrementioning

confidence: 99%

Sodium hydroxide renders the prion protein PrPSc sensitive to proteinase K

Käsermann

Kempf

2003

Journal of General Virology

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Sodium hydroxide (NaOH) solutions are widely used for the purification of contaminated equipment, as they are known to inactivate a variety of pathogens. However, information about their effect on agents causing transmissible spongiform encephalopathy (TSE) is sparse and contradictory. Scrapie hamster brain homogenate, containing the disease-associated form of the prion protein (PrP Sc ), was exposed to NaOH. Kinetics studies showed that treatment of brain homogenate with millimolar concentrations of NaOH rapidly abolished the proteinase K-resistant form of the prion protein (PrP res ). NaOH treatment converted PrP Sc into a protease-sensitive form, either in solution or when adsorbed to a metallic surface. If infectivity of TSEs is linked with PrP res , the results imply that inactivation of TSE occurs more efficiently than currently assumed.

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Protease-resistant and Detergent-insoluble Prion Protein Is Not Necessarily Associated with Prion Infectivity

Abstract: PrPSc , an abnormal isoform of PrP C , is the only known component of the prion, an agent causing fatal neurodegenerative disorders such as bovine spongiform encephalopathy (BSE) and Creutzfeldt-Jakob disease (CJD

Cited by 63 publications

References 44 publications

Biochemical Fingerprints of Prion Infection: Accumulations of Aberrant Full-Length and N-Terminally Truncated PrP Species Are Common Features in Mouse Prion Disease

Biochemical Fingerprints of Prion Infection: Accumulations of Aberrant Full-Length and N-Terminally Truncated PrP Species Are Common Features in Mouse Prion Disease

A Protease-resistant Prion Protein Isoform Is Present in Urine of Animals and Humans Affected with Prion Diseases

Sodium hydroxide renders the prion protein PrPSc sensitive to proteinase K

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