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Updated: May 8, 2026

Assessing Transmissible Spongiform Encephalopathy Species Barriers with an In Vitro Prion Protein Conversion Assay
Published on: March 10, 2015
Cellular prion proteins in humans and cattle but not sheep are characterized by a low-solubility phenotype
Thorsten Kuczius1, Martin H Groschup
1Institute for Hygiene, Westfälische Wilhelms-University and University Hospital Münster, Robert Koch-Strasse 41, 48149 Münster, Germany.
Abstract:
A feature of transmissible spongiform encephalopathies is the accumulation of infectious prion proteins (PrP(Sc)), which are formed by the conversion of physiological prion proteins (PrP(C)). As PrP(C), which is modified posttranslationally with various types of glycoproteins, serves as the substrates for PrP(Sc) conversion, various PrP(C) subtypes may play a role in the formation of PrP(Sc) and species-specific transmission; the cattle disease BSE is transmissible naturally to humans, but the sheep disease scrapie is not. To reveal new mechanisms modulating prion conversion, we analyzed the PrP(C) profiles by determining the differential PrP(C) protein solubilities in the anionic and nonionic detergents N-lauroylsarcosine, N-octyl-β-D-glucopyranoside, CHAPS and deoxycholic acid. We compared the resulting solubility profiles of human PrP(C) with the solubility profiles of PrP(C) from sheep and cattle. The PrP(C) subtypes were differentially soluble. However, non-glycosylated PrP(C) from cattle and human was found explicitly in the insoluble fraction, while non-glycosylated ovine PrP(C) was detected in the soluble fraction. These findings indicate the existence of low-solubility PrP(C) phenotypes in cattle and humans.
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