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Volume 17, Number 9—September 2011

Research

Classical Bovine Spongiform Encephalopathy by Transmission of H-Type Prion in Homologous Prion Protein Context

Juan-María TorresComments to Author , Olivier Andréoletti, Caroline Lacroux, Irene Prieto, Patricia Lorenzo, Magdalena Larska, Thierry Baron, and Juan-Carlos Espinosa
Author affiliations: Author affiliations: Centro de Investigación en Sanidad Animal, Madrid, Spain (J.-M. Torres, I. Prieto, P. Lorenzo, M. Larska, J.-C. Espinosa); Ecole Nationale Vétérinaire de Toulouse, Toulouse, France (O. Andréoletti, C. Lacroux); Agence Francaise de Sécurité Sanitaire des Aliments, Lyon, France (T. Baron)

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Figure 4

Western blot analyses of brain protease-resistant prion protein (PrPres) from BSE-H infected mice by using Saf84 monoclonal antibody. Tg110 mice infected with isolate 02-2695 (lanes 2 and 3) or 45 (lane 4) at first passage showing either high-type (lane 2) or classical BSE–like PrPres molecular profile (lanes 3 and 4). The BSE-H isolate (02–2695) (lane 1) and a BSE-C isolate (lane 5) were included for comparison. Similar quantities of PrPres were loaded in each lane. Values to the left indicate

Figure 4. Western blot analyses of brain protease-resistant prion protein (PrPres) from BSE-H infected mice by using Saf84 monoclonal antibody. Tg110 mice infected with isolate 02-2695 (lanes 2 and 3) or 45 (lane 4) at first passage showing either high-type (lane 2) or classical BSE–like PrPres molecular profile (lanes 3 and 4). The BSE-H isolate (02–2695) (lane 1) and a BSE-C isolate (lane 5) were included for comparison. Similar quantities of PrPres were loaded in each lane. Values to the left indicate molecular mass in kDa. BSE, bovine spongiform encephalopathy; BSE-H, unglycosylated PrPres that is higher than BSE-C; BSE-C, classical BSE.

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