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. 2006 Sep-Oct;37(5):695-703.
doi: 10.1051/vetres:2006024. Epub 2006 Jul 6.

Degradation of scrapie associated prion protein (PrPSc) by the gastrointestinal microbiota of cattle

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Degradation of scrapie associated prion protein (PrPSc) by the gastrointestinal microbiota of cattle

Christina Scherbel et al. Vet Res. 2006 Sep-Oct.
Free article

Abstract

A food-borne origin of the transmission of bovine spongiform encephalopathy (BSE) to cattle is commonly assumed. However, the fate of infectious prion protein during polygastric digestion remains unclear. It is unknown at present, whether infectious prion proteins, considered to be very stable, are degraded or inactivated by microbial processes in the gastrointestinal tract of cattle. In this study, rumen and colon contents from healthy cattle, taken immediately after slaughter, were used to assess the ability of these microbial consortia to degrade PrP(Sc). Therefore, the consortia were incubated with brain homogenates of scrapie (strain 263K) infected hamsters under physiological anaerobic conditions at 37 degrees C. Within 20 h, PrP(Sc) was digested both with ruminal and colonic microbiota up to immunochemically undetectable levels. Especially polymyxin resistant (mainly gram-positive) bacteria expressed PrP(Sc) degrading activity. These data demonstrate the ability of bovine gastrointestinal microbiota to degrade PrP(Sc) during digestion.

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