Transmissible spongiform encephalopathies (TSEs) or prion diseases are characterized by the accumulation of an aggregated isoform of the prion protein (PrP). This pathological isoform, termed PrP Sc, appears to be the primary component of the TSE infectious agent or prion. However, it is not clear to what extent other protein cofactors may be involved in TSE pathogenesis or whether there are PrP Sc-associated proteins which help to determine TSE strain-specific disease phenotypes. We enriched PrP Sc from the brains of mice infected with either 22L or Chandler TSE strains and examined the protein content of these samples using nanospray LC-MS/MS. These samples were compared with "mock" PrP Sc preparations from uninfected brains. PrP was the major component of the infected samples and ferritin was the most abundant impurity. Mock enrichments contained no detectable PrP but did contain a significant amount of ferritin. Of the total proteins identified, 32% were found in both mock and infected samples. The similarities between PrP Sc samples from 22L and Chandler TSE strains suggest that the non-PrP Sc protein components found in standard enrichment protocols are not strain specific.
- Animal proteomics
- Transmissible spongiform encephalopathies
ASJC Scopus subject areas
- Molecular Biology