Stability of BSE infectivity towards heat treatment even after proteolytic removal of prion protein.

ABSTRACT: The unconventional infectious agents of transmissible spongiform encephalopathies (TSEs) are prions. Their infectivity co-appears with PrP^Sc, aberrant depositions of the host's cellular prion protein (PrP^C). Successive heat treatment in the presence of detergent and proteolysis by a keratinase from Bacillus licheniformis PWD-1 was shown before to destroy PrP^Sc from bovine TSE (BSE) and sheep scrapie diseased brain, however data regarding expected reduction of infectivity were still lacking. Therefore, transgenic Tgbov XV mice which are highly BSE susceptible were used to quantify infectivity before and after the bovine brain treatment procedure. Also four immunochemical analyses were applied to compare the levels of PrP^Sc. After heating at 115 °C

SUBMITTER: Langeveld JPM 

PROVIDER: S-EPMC8052740 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature