The risks posed to human health Water Bottle by individual animal prion diseases cannot be determined a priori and are difficult to address empirically.The fundamental event in prion disease pathogenesis is thought to be the seeded conversion of normal prion protein to its pathologic isoform.We used a rapid molecular conversion assay (protein misfolding cyclic amplification) to test whether brain homogenates from specimens of classical bovine spongiform encephalopathy (BSE), atypical BSE (H-type BSE and L-type BSE), classical scrapie, atypical scrapie, and chronic wasting disease can convert normal human prion protein to the abnormal disease-associated form.
None of the tested prion isolates from diseased animals were as efficient as classical BSE L-GLUTAMINE POWDER in converting human prion protein.However, in the case of chronic wasting disease, there was no absolute barrier to conversion of the human prion protein.