A Rapid Bioassay for Classical and L-Type Bovine Spongiform Encephalopathies

Abstract

The rapid detection of infectivity of several agents that cause Creutzfeldt-Jakob disease has previously been achieved by assaying for deposits of abnormal prion protein (PrP Sc ) in follicular dendritic cells in the spleens of transgenic mice carrying the human prion protein gene. In this study, transgenic mice expressing the bovine prion protein were inoculated intraperitoneally with classical (C-type) or atypical L-type bovine spongiform encephalopathies (BSE). Proteinase-resistant PrP Sc were detected in the spleens of all transgenic mice at 75 days after inoculation with both types of BSE. Infectivity in PrP Sc -positive spleens of the transgenic mice revealed that prions of C-and L-type BSE replicated. These results suggest that bioassay system by the transgenic mice could be useful for the rapid detection of BSE infectivity with discriminating between C-and L-type BSEs.

Experimental Infection of Cattle With a Novel Prion Derived From Atypical H-Type Bovine Spongiform Encephalopathy

“…20 Half of the spleen was frozen for Western blotting, and the remaining half was fixed for histopathology and IHC. PrP Sc accumulation in the FDC of the spleen of wild-type mice inoculated with C-BSE at 60 days after inoculation has been confirmed 26 but not with H-BSE at the end of their life span. 5…”