Infectivity of Scrapie Prion Protein (PrPSc) Following In vitro Digestion with Bovine Gastrointestinal Microbiota

Summary The influence of a complex microflora residing in the gastrointestinal tract of cattle on the prion protein plays a crucial role with respect to early pathogenesis and the potential infectivity of faeces resulting in contamination of the environment. It is unknown whether infectious prion pr...

Full description

Saved in:
Bibliographic Details
Published in:Zoonoses and public health 2007-06, Vol.54 (5), p.185-190
Main Authors: Scherbel, C., Pichner, R., Groschup, M. H., Mueller-Hellwig, S., Scherer, S., Dietrich, R., Maertlbauer, E., Gareis, M.
Format: Article
Language:English
Subjects:
Animals
Bacteria - metabolism
bioassays
Cattle
Colon - microbiology
Cricetinae
degradation
Digestion
Encephalopathy, Bovine Spongiform - metabolism
Encephalopathy, Bovine Spongiform - transmission
gastrointestinal
infectivity
Prion
PrPSc Proteins - metabolism
PrPSc Proteins - pathogenicity
rumen
Rumen - microbiology
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Summary The influence of a complex microflora residing in the gastrointestinal tract of cattle on the prion protein plays a crucial role with respect to early pathogenesis and the potential infectivity of faeces resulting in contamination of the environment. It is unknown whether infectious prion proteins, considered to be very stable, are inactivated by microbial processes in the gastrointestinal tract of animals during digestion. In our previous study it was shown that the scrapie‐associated prion protein was degraded by ruminal and colonic microbiota of cattle, as indicated by a loss of anti‐prion antibody 3F4 immunoreactivity in Western blot. Subsequently, in this study hamster bioassays with the pre‐treated samples were performed. Although the PrPSc signal was reduced up to immunochemically undetectable levels within 40 h of pre‐treatment, significant residual prion infectivity was retained after degradation of infected hamster brain through the gastrointestinal microflora of cattle. The data presented here show that the loss of anti‐prion antibody 3F4 immunoreactivity is obviously not correlated with a biological inactivation of PrPSc. These results highlight the deficiency of using Western blot in transmissible spongiform encephalopathies inactivation assessment studies and, additionally, point to the possibility of environmental contamination with faeces containing PrPSc following an oral ingestion of prions.
ISSN:1863-1959
1863-2378
DOI:10.1111/j.1863-2378.2007.01040.x