Classic Scrapie in Sheep with the ARR/ARR Prion Genotype in Germany and France
Martin H. Groschup*1 , Caroline Lacroux†1, Anne Buschmann*, Gesine Lühken‡, Jacinthe Mathey†, Martin Eiden*, Séverine Lugan†, Christine Hoffmann*, Juan Carlos Espinosa§, Thierry G.M. Baron¶, Juan Maria Torres§, Georg Erhardt‡, and Olivier Andreoletti†
Author affiliations: *Friedrich-Loeffler-Institut, Insel Riems, Germany; †Institut National de la Recherche Agronimique, Toulouse, France; ‡Justus-Liebig–University Giessen, Giessen, Germany; §Centro de Investigación en Sanidad Animal, Madrid, Spain; ¶Agence Française de Sécurité Sanitaire des Aliments, Lyon, France;
Figure 2. Biochemical characterization of the prion protein (PrPSc) associated with ARR/ARR cases in France and Germany. A) Western blot (stained by monoclonal antibody L42) illustrating that protein kinase (PK)– treated ovine bovine spongiform encephalopathy (BSE) PrPSc has ≈1-kDa lower molecular mass than PrPSc from the scrapie cases. Lane 1, S115/04, molecular mass (MM) 20.95 kDa; lane 2, S83, MM 19.96 kDa; lane 3, S95 classic scrapie, MM 19.64 kDa; lane 4, ovine BSE, MM 18.85 kDa. B) PrPSc PK sensitivity measured by using brain from S83 scrapie case (▲), ARR/ARR BSE in sheep (○), ARQ/ARQ BSE in sheep (●), BSE from bovines (■), an ARR/ARR atypical scrapie case (▼), and 20 randomly selected isolates from sheep with scrapie in France (2 cases shown, represented as □ and ◆). PrPSc ELISA measurements were performed by using the TeSeE Sheep/Goat rapid test (Bio-Rad) after brain homogenate digestion using a PK concentration ranging from 50 µg/mL to 500 µg/mL. Three tests were performed for each sample and PK concentration.
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