Abstract
Sheep CH1641-like transmissible spongiform encephalopathy isolates have shown molecular similarities to bovine spongiform encephalopathy (BSE) isolates. We report that the prion protein PrPSc from sheep BSE is extremely resistant to denaturation. This feature, combined with the N-terminal PrPSc cleavage, allowed differentiation of classical scrapie, including CH1641-like, from natural goat BSE and experimental sheep BSE.
Highlights
Sheep CH1641-like transmissible spongiform encephalopathy isolates have shown molecular similarities to bovine spongiform encephalopathy (BSE) isolates
We report 2 new CH1641-like isolates; analyze the conformational stability of CH1641-like isolates, BSE, and classical scrapie; and show that a reliable molecular differentiation of these 3 transmissible spongiform encephalopathies (TSEs) sources is possible by an improved discriminatory Western blot (WB) method
Because the discriminatory methods based on differential PrPSc N-terminal proteinase K (PK) cleavage [11] do not enable a clear-cut discrimination of CH1641like from BSE [12], we investigated the potential of denaturation with GdnHCl as a further discriminatory strategy within the framework of the Istituto Superiore di Sanità discriminatory WB [11]
Summary
We report that the prion protein PrPSc from sheep BSE is extremely resistant to denaturation This feature, combined with the N-terminal PrPSc cleavage, allowed differentiation of classical scrapie, including CH1641-like, from natural goat BSE and experimental sheep BSE. We report 2 new CH1641-like isolates; analyze the conformational stability of CH1641-like isolates, BSE, and classical scrapie; and show that a reliable molecular differentiation of these 3 TSE sources is possible by an improved discriminatory WB method. We showed that CSSA could reveal strain-specified PrPSc conformational stability in sheep isolates because it enabled discrimination of Nor from classical scrapie isolates [14].
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