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Stability of Bovine Spongiform Encephalopathy Prions: Absence of Prion Protein Degradation by Bovine Gut Microbiota
Author(s) -
Böhnlein C.,
Groschup M. H.,
Maertlbauer E.,
Pichner R.,
Gareis M.
Publication year - 2012
Publication title -
zoonoses and public health
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.87
H-Index - 65
eISSN - 1863-2378
pISSN - 1863-1959
DOI - 10.1111/j.1863-2378.2012.01455.x
Subject(s) - bovine spongiform encephalopathy , feces , biology , prion protein , microbiology and biotechnology , blot , incubation , gastrointestinal tract , virology , medicine , biochemistry , pathology , gene , disease
Summary Bovine spongiform encephalopathy (BSE) is transmitted by the oral route. However, the impacts of anaerobic fermentation processes in cattle on the stability of BSE‐associated prion protein (PrP Sc ) are still unresolved. In this study, experiments were designed to assess the ability of complex ruminal and colonic contents of bovines to degrade BSE‐derived PrP Sc . No significant decrease in PrP Sc levels in BSE brain homogenates was detected by Western blotting after up to 66 h of co‐incubation with intestinal fluids. These results indicate that BSE‐associated PrP Sc survive gastrointestinal digestion processes in cattle and might be excreted via faeces.