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Volume 20, Number 12—December 2014
Research

Variably Protease-Sensitive Prionopathy, a Unique Prion Variant with Inefficient Transmission Properties

Abigail B. Diack1, Diane Ritchie1, Alexander H. Peden, Deborah Brown, Aileen Boyle, Laura Morabito, David Maclennan, Paul Burgoyne, Casper Jansen, Richard S. Knight, Pedro Piccardo, James W. Ironside1, and Jean C. Manson1Comments to Author 
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)

Main Article

Figure 2

Western blot analysis of PrPres in extracts of frontal cortex tissue prepared from postmortem samples from 2 persons with sCJD (subtypes MM1 and VV2) and the 3 persons with VPSPr whose brain samples were used for experimental transmission studies in transgenic mice (patients NL-VV, UK-VV, and UK-MV). Extracts from another patient who had VPSPr of UK origin (codon 129VV genotype) was also included on the blot (lane 6). Duplicate blots were probed with the following monoclonal antibodies: Anti-Pri

Figure 2. Western blot analysis of PrPres in extracts of frontal cortex tissue prepared from postmortem samples from 2 persons with sCJD (subtypes MM1 and VV2) and the 3 persons with VPSPr whose brain samples were used for experimental transmission studies in transgenic mice (patients NL-VV, UK-VV, and UK-MV). Extracts from another patient who had VPSPr of UK origin (codon 129VV genotype) was also included on the blot (lane 6). Duplicate blots were probed with the following monoclonal antibodies: Anti-Prion Protein Antibody monoclonal antibody 3F4 (Millipore, Watford, UK) (A) and 1E4 (provided by J. Langeveld) (B). The 2 antibodies detected PrPres equally well in extracts from persons with sCJD or with VPSPr. All lanes were loaded with 5 μL of a 10% (wt/vol) brain homogenate. Brain homogenates were analyzed after digestion with Proteinase K. Lane 1, molecular weight marker (sizes indicated at left in kDa); lane 2, sCJD MM1; lane 3, VPSPr UK-VV; lane 4, VPSPr UK-MV; lane 5, VPSPr NL-VV; lane 6, additional VPSPr of UK origin; lane 7, sCJD VV2. MM, homozygous for methionine; PrPres, protease-resistant isoform of the disease-specific prion protein; NL-VV, patient from the Netherlands who had VPSPr and the codon 129VV genotype; sCJD, sporadic Creutzfeldt-Jakob disease; UK-VV and UK-MV, patients from the United Kingdom who had VPSPr and the codon 129VV and 129MV genotypes, respectively; VPSPr, variably protease-sensitive prionopathy; VV, homozygous for valine.

Main Article

1These authors contributed equally to this article.

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