The octarepeat region of the prion protein is conformationally altered in PrP(Sc).

ABSTRACT:

Background

Prion diseases are fatal neurodegenerative disorders characterized by misfolding and aggregation of the normal prion protein PrP(C). Little is known about the details of the structural rearrangement of physiological PrP(C) into a still-elusive disease-associated conformation termed PrP(Sc). Increasing evidence suggests that the amino-terminal octapeptide sequences of PrP (huPrP, residues 59-89), though not essential, play a role in modulating prion replication and disease presentation.

Methodology/principal findings

Here, we report that trypsin digestion of PrP(Sc) from variant and sporadic human CJD results in a disease-specific trypsin-resistant PrP(Sc) fragment including amino acids approximately 49-231, thus preserving important epitopes such as the octapeptid

SUBMITTER: Yam AY 

PROVIDER: S-EPMC2827544 | biostudies-literature | 2010 Feb

REPOSITORIES: biostudies-literature