A Protein Misfolding Shaking Amplification-based method for the spontaneous generation of hundreds of bona fide prions

Hasier Eraña, Cristina Sampedro-Torres-Quevedo, Jorge M. Charco, Carlos M. Díaz-Domínguez, Francesca Peccati, Maitena San-Juan-Ansoleaga, Enric Vidal, Nuno Gonçalves-Anjo, Miguel A. Pérez-Castro, Ezequiel González-Miranda, Patricia Piñeiro, Leire Fernández-Veiga, Josu Galarza-Ahumada, Eva Fernández-Muñoz, Guiomar Perez de Nanclares, Glenn Telling, Mariví Geijo, Gonzalo Jiménez-Osés and Joaquín Castilla ()
Additional contact information
Hasier Eraña: Basque Research and Technology Alliance (BRTA)
Cristina Sampedro-Torres-Quevedo: Basque Research and Technology Alliance (BRTA)
Jorge M. Charco: Basque Research and Technology Alliance (BRTA)
Carlos M. Díaz-Domínguez: Basque Research and Technology Alliance (BRTA)
Francesca Peccati: Basque Research and Technology Alliance (BRTA)
Maitena San-Juan-Ansoleaga: Basque Research and Technology Alliance (BRTA)
Enric Vidal: IRTA. Programa de Sanitat Animal. Centre de Recerca en Sanitat Animal (CReSA). Campus de la Universitat Autònoma de Barcelona (UAB)
Nuno Gonçalves-Anjo: Basque Research and Technology Alliance (BRTA)
Miguel A. Pérez-Castro: Basque Research and Technology Alliance (BRTA)
Ezequiel González-Miranda: Basque Research and Technology Alliance (BRTA)
Patricia Piñeiro: Basque Research and Technology Alliance (BRTA)
Leire Fernández-Veiga: Basque Research and Technology Alliance (BRTA)
Josu Galarza-Ahumada: Basque Research and Technology Alliance (BRTA)
Eva Fernández-Muñoz: Basque Research and Technology Alliance (BRTA)
Guiomar Perez de Nanclares: Araba University Hospital
Glenn Telling: Colorado State University
Mariví Geijo: NEIKER-Basque Institute for Agricultural Research and Development. Basque Research and Technology Alliance (BRTA)
Gonzalo Jiménez-Osés: Basque Research and Technology Alliance (BRTA)
Joaquín Castilla: Basque Research and Technology Alliance (BRTA)

Nature Communications, 2024, vol. 15, issue 1, 1-14

Abstract: Abstract Prion diseases are a group of rapidly progressing neurodegenerative disorders caused by the misfolding of the endogenous prion protein (PrPC) into a pathogenic form (PrPSc). This process, despite being the central event underlying these disorders, remains largely unknown at a molecular level, precluding the prediction of new potential outbreaks or interspecies transmission incidents. In this work, we present a method to generate bona fide recombinant prions de novo, allowing a comprehensive analysis of protein misfolding across a wide range of prion proteins from mammalian species. We study more than 380 different prion proteins from mammals and classify them according to their spontaneous misfolding propensity and their conformational variability. This study aims to address fundamental questions in the prion research field such as defining infectivity determinants, interspecies transmission barriers or the structural influence of specific amino acids and provide invaluable information for future diagnosis and therapy applications.

Date: 2024
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-46360-2

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DOI: 10.1038/s41467-024-46360-2

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