Dimerization of the cellular prion protein inhibits propagation of scrapie prions.

ABSTRACT: A central step in the pathogenesis of prion diseases is the conformational transition of the cellular prion protein (PrP^C) into the scrapie isoform, denoted PrP^Sc Studies in transgenic mice have indicated that this conversion requires a direct interaction between PrP^C and PrP^Sc; however, insights into the underlying mechanisms are still missing. Interestingly, only a subfraction of PrP^C is converted in scrapie-infected cells, suggesting that not all PrP^C species are suitable substrates for the conversion. On the basis of the observation that PrP^C can form homodimers under physiological conditions with the internal hydrophobic domain (HD) serving as a putative dimerization domain, we wondered whether PrP dimerizati

SUBMITTER: Engelke AD 

PROVIDER: S-EPMC5971439 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature