Constant Transmission Properties of Variant Creutzfeldt-Jakob Disease in 5 Countries
Abigail B. Diack, Diane Ritchie, Matthew Bishop, Victoria Pinion, Jean-Philippe Brandel, Stephane Haik, Fabrizio Tagliavini, Cornelia Van Duijn, Ermias D. Belay, Pierluigi Gambetti, Lawrence B. Schonberger, Pedro Piccardo, Robert G. Will1, and Jean C. Manson1
Author affiliations: The Roslin Institute, Easter Bush, Scotland, UK (A.B. Diack, V. Pinion, J.C. Manson); University of Edinburgh, Edinburgh, Scotland, UK (D. Ritchie, M. Bishop, R.G. Will); Cellule Nationale de Référence des Maladies de Creutzfeldt-Jakob, Universite Pierre et Marie Curie-Paris 6, INSERM, and CNRS, Paris, France (J.-P. Brandel, S. Haik); Fdazione IRCCS Istituto Neurologico Carlo Besta, Milan, Italy (F. Tagliavini); Erasmus University Medical School, Rotterdam, the Netherlands (C. Van Duijn); Centers for Disease Control and Prevention, Atlanta, Georgia, USA (E.D. Belay, L.B. Schonberger); Case Western Reserve University, Cleveland, Ohio, USA (P. Gambetti); and Food and Drug Administration, Rockville, Maryland, USA (P. Piccardo)
Figure 4. . Western blot analysis of brain extracts from RIII (A) and VM (B) wild-type mice inoculated with variant Creutzfeldt-Jakob disease (vCJD) brain tissue. Lane M, positive control; lane 1, human vCJD brain homogenate (UK origin) showing the typical abnormal prion protein (PrPSc) type 2B; lane 2, United Kingdom; lane 3, The Netherlands; lane 4: Italy (cortex); lane 5, Italy (cerebellum); lane 6, France; lane 7, United States; lane 8, human sporadic Creutzfeldt-Jakob disease brain homogenate showing the typical PrPSc type 1. Type 2B and 1 differ in mobility of the unglycosylated band (≈19 kDa and ≈20 kDa, respectively). All samples were treated with proteinase K. The anti–prion protein detection antibody used was 6H4.
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