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Brain Advance Access originally published online on January 16, 2006
Brain 2006 129(3):676-685; doi:10.1093/brain/awl013
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© The Author (2006). Published by Oxford University Press on behalf of the Guarantors of Brain. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Distinct glycoform ratios of protease resistant prion protein associated with PRNP point mutations

Andrew F. Hill1, Susan Joiner, Jonathan A. Beck, Tracy A. Campbell, Andrew Dickinson, Mark Poulter, Jonathan D. F. Wadsworth and John Collinge

MRC Prion Unit and Department of Neurodegenerative Disease, Institute of Neurology, University College London, National Hospital for Neurology and Neurosurgery, Queen Square, London, UK 1 Present addresses: Department of Biochemistry & Molecular Biology, Bio21 Molecular Science and Biotechnology Institute and Department of Pathology, University of Melbourne, Parkville, Victoria 3010, Australia

Correspondence to: Professor John Collinge, MRC Prion Unit and Department of Neurodegenerative Disease, Institute of Neurology, University College London, National Hospital for Neurology and Neurosurgery, Queen Square, London WC1N 3BG, UK E-mail: j.collinge{at}prion.ucl.ac.uk

Inherited prion diseases are neurodegenerative disorders caused by autosomal dominant mutations in the human prion protein gene (PRNP). Kindred with inherited prion disease can show remarkable phenotypic variability that has yet to be explained. Here we report analysis of protease resistant disease-related prion protein (PrPSc) isoforms from a range of inherited prion disease cases (point mutations P102L, D178N, E200K and 2-, 4- and 6-octapeptide repeat insertions) and show that the glycoform ratios of PrPSc associated with PRNP point mutations are distinct from those observed in sporadic, iatrogenic and variant Creutzfeldt–Jakob disease. Patients with the same PRNP mutation can also propagate PrPSc with distinct conformations. These data extend the spectrum of recognized PrPSc types seen in human prion diseases and provide further insight into the generation of diverse clinicopathological phenotypes associated with inherited prion disease.

Key Words: Creutzfeldt-Jakob disease; prion disease; prion protein; fatal familial insomnia

Abbreviations: CJD = Creutzfeldt–Jakob disease; FFI = fatal familial insomnia; GSS = Gerstmann–Straüssler–Scheinker syndrome; MHs = methionine homozygotes; vCJD = variant CJD

Received September 5, 2005. Revised November 27, 2005. Accepted December 22, 2005.


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