Abstract
The risks posed to human health 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 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.
Highlights
Publisher Rights Statement: Emerging Infectious Diseases is published by the Centers for Disease Control and Prevention, a U.S Government agency
We have previously reported the use of protein misfolding cyclic amplification (PMCA) as a model of cross-species prion transmission of C-type bovine spongiform encephalopathy (BSE) in cattle and sheep to humans [10]
PrPres was most abundant in classical scrapie and chronic wasting disease (CWD) samples; lower levels were seen in C, H- and L-type BSE samples and were barely detectable at this level of sensitivity in atypical scrapie (Figure 1, panel B)
Summary
Publisher Rights Statement: Emerging Infectious Diseases is published by the Centers for Disease Control and Prevention, a U.S Government agency. 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 in converting human prion protein. In the case of chronic wasting disease, there was no absolute barrier to conversion of the human prion protein. Prion diseases are rare fatal neurodegenerative conditions that affect humans and animals. Most cases of human prion disease are apparently spontaneously occurring (sporadic CJD [sCJD]) or are associated with mutations in the human prion protein gene, designated PRNP (genetic CJD, Gerstmann-Sträussler-Scheinker disease, or fatal familial insomnia). A small minority of cases are acquired by inadvertent human-to-human transmission during medical or surgical treatments (iatrogenic CJD)
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