Similar biochemical signatures and prion protein genotypes in atypical scrapie and Nor98 cases, France and Norway.

Abstract

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.