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Updated: Jun 21, 2026

High-throughput Screening for Protein-based Inheritance in S. cerevisiae
Published on: August 8, 2017
Differential solubility of prions is associated in manifold phenotypes
Thorsten Kuczius1, Helge Karch, Martin H Groschup
1Institute for Hygiene, Westfälische Wilhelms-University Münster and University Hospital Münster, Robert Koch-Strasse 41, 48149 Münster, Germany. tkuczius@uni-muenster.de
Abstract:
The main feature of prion diseases is the accumulation of infectious proteins (PrP(Sc)). Since PrP(Sc) results from conversion of cellular prion proteins (PrP(C)), differential expressed PrP(C) types may play an important role in the formation and conversion efficiency to specific PrP(Sc) forms. However, little is known about the PrP(C) expression, regulation and differentiation. Here, we demonstrate a new type of differentiation of overlapping PrP(C) isoforms in brain homogenates using differential SDS solubility. Low and highly soluble PrP(C) were detected along with various types of protein which are present in the brain of non-infected humans, sheep and cattle. Our findings provide evidence for the existence of several overlapping PrP(C) proteins exhibiting distinct glycotypes. The selection of defined PrP(C) types offers new possibilities for identifying highly efficient converting proteins and provides the potential for disease control.
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