Sodium hydroxide renders the prion protein PrPSc sensitive to proteinase K | Zendy

Fabian Käsermann | Zendy; Christoph Kempf | Zendy

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Sodium hydroxide renders the prion protein PrPSc sensitive to proteinase K

Author(s) -

Fabian Käsermann,

Christoph Kempf

Publication year - 2003

Publication title -

journal of general virology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.55

H-Index - 167

eISSN - 1465-2099

pISSN - 0022-1317

DOI - 10.1099/vir.0.19355-0

Subject(s) - scrapie , proteinase k , infectivity , transmissible spongiform encephalopathy , hamster , biology , sodium hydroxide , virology , protease , molar concentration , sodium , prion protein , amyloid (mycology) , biochemistry , microbiology and biotechnology , chemistry , enzyme , virus , disease , organic chemistry , medicine , botany , pathology

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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