Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria.

ABSTRACT:

Background

An increasing number of proteins are being shown to assemble into amyloid structures that lead to pathological states. Among them, mammalian prions outstand due to their ability to transmit the pathogenic conformation, becoming thus infectious. The structural conversion of the cellular prion protein (PrP(C)), into its misfolded pathogenic form (PrP(Sc)) is the central event of prion-driven pathologies. The study of the structural properties of intracellular amyloid aggregates in general and of prion-like ones in particular is a challenging task. In this context, the evidence that the inclusion bodies formed by amyloid proteins in bacteria display amyloid-like structural and functional properties make them a privileged system to model intracellular amyloid aggregation.

SUBMITTER: Macedo B 

PROVIDER: S-EPMC4634817 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature