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 4. Biochemical properties of prion protein (PrPSc) associated with the ARR/ARR scrapie case S83 from France after passage in Tg 338 VRQ mice. A) Western blot mobility of the original S83 ARR/ARR case (lane 3) and S83 passaged in Tg338 (lane 4) were similar and comparable to a classic scrapie isolate (Langlade, lane 2). PrPSc WB profile of ARR/ARR bovine spongiform encephalopathy (BSE) in sheep (lane 6) and profiles of atypical scrapie case isolates (lane 5) passaged into Tg338 mice were readily distinguishable by their banding pattern or electromobility. B) PrPsc protein kinase (PK) sensitivity of the original S83 isolate (▼) and a classic scrapie isolate (Langlade) (△) compared with S83 (▽) and Langlade (▲) that had been passaged in Tg338 (2 different mice for each isolate). Triplicate ELISA measurements were performed by using the TeSeE Sheep/Goat rapid test (Bio-Rad), after brain homogenate digestion with PK concentration ranging from 50 µg/mL to 500 µg/mL.
The opinions expressed by authors contributing to this journal do not necessarily reflect the opinions of the U.S. Department of Health and Human Services, the Public Health Service, the Centers for Disease Control and Prevention, or the authors' affiliated institutions. Use of trade names is for identification only and does not imply endorsement by any of the groups named above.