Gerstmann-Sträussler-Scheinker disease subtypes efficiently transmit in bank voles as genuine prion diseases

Gerstmann-Sträussler-Scheinker disease (GSS) is an inherited neurodegenerative disorder associated with mutations in the prion protein gene and accumulation of misfolded PrP with protease-resistant fragments (PrP res ) of 6–8 kDa. With the exception of a few GSS cases characterized by co-accumulatio...

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Published in:Scientific reports 2016-02, Vol.6 (1), p.20443-20443, Article 20443
Main Authors: Pirisinu, Laura, Di Bari, Michele A., D’Agostino, Claudia, Marcon, Stefano, Riccardi, Geraldina, Poleggi, Anna, Cohen, Mark L., Appleby, Brian S., Gambetti, Pierluigi, Ghetti, Bernardino, Agrimi, Umberto, Nonno, Romolo
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Language:English
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631/378/1689/2609
64
692/617/375/1937
82
82/29
82/51
Animals
Arvicolinae
Disease
Disease Models, Animal
Gerstmann-Straussler-Scheinker Disease - genetics
Gerstmann-Straussler-Scheinker Disease - pathology
Humanities and Social Sciences
Humans
Inoculum
multidisciplinary
Mutation
Neurodegenerative diseases
Prion protein
Prion Proteins - genetics
Protein folding
Science
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creator Pirisinu, Laura
Di Bari, Michele A.
D’Agostino, Claudia
Marcon, Stefano
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Poleggi, Anna
Cohen, Mark L.
Appleby, Brian S.
Gambetti, Pierluigi
Ghetti, Bernardino
Agrimi, Umberto
Nonno, Romolo
description Gerstmann-Sträussler-Scheinker disease (GSS) is an inherited neurodegenerative disorder associated with mutations in the prion protein gene and accumulation of misfolded PrP with protease-resistant fragments (PrP res ) of 6–8 kDa. With the exception of a few GSS cases characterized by co-accumulation of PrP res of 21 kDa, efforts to transmit GSS to rodents have been unsuccessful. As a result, GSS subtypes exclusively associated with 6–8 kDa PrP res have often been considered as non-transmissible proteinopathies rather than true prion diseases. We show that GSS with P102L, A117V and F198S mutations transmit efficiently and produce distinct pathological phenotypes in bank voles (M. glareolus ), irrespective of the presence of 21 kDa PrP res in the inoculum, demonstrating that GSS is a genuine prion disease characterized by both transmissibility and strain variation.
doi_str_mv 10.1038/srep20443
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subjects 631/378/1689/2609
64
692/617/375/1937
82
82/29
82/51
Animals
Arvicolinae
Disease
Disease Models, Animal
Gerstmann-Straussler-Scheinker Disease - genetics
Gerstmann-Straussler-Scheinker Disease - pathology
Humanities and Social Sciences
Humans
Inoculum
multidisciplinary
Mutation
Neurodegenerative diseases
Prion protein
Prion Proteins - genetics
Protein folding
Science
title Gerstmann-Sträussler-Scheinker disease subtypes efficiently transmit in bank voles as genuine prion diseases
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