Dataset Information

In Vitro Seeding Activity of Glycoform-Deficient Prions from Variably Protease-Sensitive Prionopathy and Familial CJD Associated with PrP^V180I Mutation.

ABSTRACT: Both sporadic variably protease-sensitive prionopathy (VPSPr) and familial Creutzfeldt-Jakob disease linked to the prion protein (PrP) V180I mutation (fCJD^V180I) have been found to share a unique pathological prion protein (PrP^Sc) that lacks the protease-resistant PrP^Sc glycosylated at residue 181 because two of four PrP glycoforms are apparently not converted into the PrP^Sc from their cellular PrP (PrP^C). To investigate the seeding activity of these unique PrP^Sc molecules, we conducted in vitro prion conversion experiments using serial protein misfolding cyclic amplification (sPMCA) and real-time quaking-induced conversion (RT-QuIC) assays with different PrP^C substrates. We observed that the seeding of PrP^Sc

SUBMITTER: Wang Z

PROVIDER: S-EPMC6614145 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature

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Dataset Information

In Vitro Seeding Activity of Glycoform-Deficient Prions from Variably Protease-Sensitive Prionopathy and Familial CJD Associated with PrP^V180I Mutation.

OmicsDI is part of the ELIXIR infrastructure

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Dataset Information

In Vitro Seeding Activity of Glycoform-Deficient Prions from Variably Protease-Sensitive Prionopathy and Familial CJD Associated with PrPV180I Mutation.

OmicsDI is part of the ELIXIR infrastructure

Tweets

In Vitro Seeding Activity of Glycoform-Deficient Prions from Variably Protease-Sensitive Prionopathy and Familial CJD Associated with PrP^V180I Mutation.