Central residues in prion protein PrP^C are crucial for its conversion into the pathogenic isoform.

ABSTRACT: Conformational conversion of the cellular prion protein, PrP^C, into the amyloidogenic isoform, PrP^Sc, is a key pathogenic event in prion diseases. However, the conversion mechanism remains to be elucidated. Here, we generated Tg(PrPΔ91-106)-8545/Prnp^0/0 mice, which overexpress mouse PrP lacking residues 91-106. We showed that none of the mice became sick after intracerebral inoculation with RML, 22L, and FK-1 prion strains nor accumulated PrP^ScΔ91-106 in their brains except for a small amount of PrP^ScΔ91-106 detected in one 22L-inoculated mouse. However, they developed disease around 85 days after inoculation with bovine spongiform encephalopathy (BSE) prions with PrP^ScΔ91-106 in their brains. These results suggest that resi

SUBMITTER: Pasiana AD 

PROVIDER: S-EPMC9478402 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature