Variably Protease-Sensitive Prionopathy, a Unique Prion Variant with Inefficient Transmission Properties
Abigail B. Diack
1, Diane Ritchie
1, Alexander H. Peden, Deborah Brown, Aileen Boyle, Laura Morabito, David Maclennan, Paul Burgoyne, Casper Jansen, Richard S. Knight, Pedro Piccardo, James W. Ironside
1, and Jean C. Manson
1
Author affiliations: The Roslin Institute, University of Edinburgh, Easter Bush, Scotland, UK (A.B. Diack, D. Brown, A, Boyle, L. Morabito, D. Maclennan, P. Burgoyne, J.C. Manson); School of Clinical Sciences, University of Edinburgh, Edinburgh, Scotland, UK (D.L. Ritchie, A.H. Peden, R.S. Knight, J.W. Ironside); Food and Drug Administration, Rockville, Maryland, USA (P. Piccardo); University Medical Centre Utrecht, Utrecht, the Netherlands (C. Jansen)
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Figure 5
Figure 5. Gliosis in transgenic mice following inoculation with brain homogenate prepared from a postmortem sample from a person with variably protease-sensitive prionopathy. A) Immunohistochemical staining for GFAP in the hippocampus of a HuVV mouse showing microplaque-like deposits. Arrows indicate areas of reactive astrocytosis. B) A serial section from the same HuVV mouse immunolabeled for PrP by using monoclonal antibody (Purified [3F4], Cambridge Bioscience, Cambridge, UK). C) Immunohistochemical staining for GFAP in the hippocampus of a HuVV mouse showing plaque-like deposits. No reactive astrocytosis is seen in the vicinity of plaques. D) A serial section from the same HuVV mouse immunolabeled for PrP by using monoclonal antibody 3F4. GFAP, glial fibrillary acid protein; HuVV, transgenic mouse expressing human PrP gene sequence coding for the valine-homozygous codon 129 genotype; PrP, prion protein. Scale bars indicate 50 μm.
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