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)
Figure 2. Western blot analyses of brain protease-resistant prion protein (PrPres) from BSE-H infected mice by using Sha31 monoclonal antibody. A) Mice infected with isolate 07-644 at first passage (lanes 3–7) showing a homogeneous high-type (H-type) PrPres molecular profile; BSE-H isolate 07-644 (lane 1) and a BSE-C isolate (lane 2) were included for comparison. B) Mice infected with isolate 02-2695 at first passage showing either H-type (lanes 1 and 3) or classical BSE–like (C-like) PrPres molecular profile (lanes 2 and 4); BSE-H isolate 02-2695 (lane 6) and a BSE-C isolate (lane 5) were included for comparison. In panel B, a 10-fold equivalent brain tissue mass was loaded for brains from mice showing H-type PrPres molecular profile (lanes 1 and 3) than from those with a C-like PrPres molecular profile (lanes 2 and 4) to obtain equivalent PrPres signals. 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.
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.