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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 3

Comparative Western blot analyses with Sha31 and 12B2 monoclonal antibodies (mAbs) of brain protease-resistant prion protein (PrPres) from BSE-H–infected mice. Mice infected with isolate 07-644 (lane 1), 02-2695 (lanes 2 and 3), or 45 (lanes 4 and 5) at first passage showing either high-type (lanes 1, 2, and 4) or classical BSE–like PrPres molecular profile (lanes 3 and 5). Panel A was shown with Sha31 mAb; panel B was shown with 12B2 mAb. The same quantities of PrPres were loaded in both panels

Figure 3. Comparative Western blot analyses with Sha31 and 12B2 monoclonal antibodies (mAbs) of brain protease-resistant prion protein (PrPres) from BSE-H–infected mice. Mice infected with isolate 07-644 (lane 1), 02-2695 (lanes 2 and 3), or 45 (lanes 4 and 5) at first passage showing either high-type (lanes 1, 2, and 4) or classical BSE–like PrPres molecular profile (lanes 3 and 5). Panel A was shown with Sha31 mAb; panel B was shown with 12B2 mAb. The same quantities of PrPres were loaded in both panels A and B. Values to the left indicate molecular mass in kDa. BSE, bovine spongiform encephalopathy; BSE-H, unglycosylated PrPres that is higher than classical BSE.

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