Isolates of atypical scrapie recently identified in sheep and goats in France were compared with Nor98 isolates reported in Norway. Western blot methods for characterization of the protease-resistant prion protein showed that all these isolates shared a unique biochemical signature: 5 groups of bands, including a characteristic band of apparent low molecular weight (11 kDa). This pattern could originate from the presence of 3 different protease cleavage products, including the 11 kDa most likely cleaved at both N- and C-sides of the protein. Genetic data, which strongly suggested the higher susceptibility of AHQ and AF141RQ animals in French cases, resembled earlier data from Nor98 scrapie.
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Arsac et al. (2007) studied this question.
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