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Substitution of histidine 95 by tyrosine in the prion protein causes spontaneous neurodegeneration in transgenic mice

Title: Substitution of histidine 95 by tyrosine in the prion protein causes spontaneous neurodegeneration in transgenic mice
Authors: Torres, Juan María; Marín-Moreno, Alba; Espinosa, Juan Carlos; Canoyra, Sara; Burato, Anna; Ciullini, Arianna; De Luca, Chiara Maria Giulia; Bistaffa, Edoardo; Moda, F.; Legname, Giuseppe
Contributors: European Commission; Agencia Estatal de Investigación (España); Ministerio de Ciencia, Innovación y Universidades (España); CSIC - Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (INIA); Ministero della Salute; Associazione Italiana Encefalopatie da Prioni; Torres, Juan María; Espinosa, Juan Carlos; Legname, Giuseppe; Consejo Superior de Investigaciones Científicas https://ror.org/02gfc7t72
Publisher Information: Public Library of Science
Publication Year: 2025
Collection: Digital.CSIC (Consejo Superior de Investigaciones Científicas / Spanish National Research Council)
Description: Prion diseases are neurodegenerative disorders caused by a change in conformation of the prion protein from the cellular form (PrPC) to a misfolded isoform (PrPSc). PrPC is a copper binding protein via histidine residues in the octapeptide repeats (OR) and the non-OR region located at the N-terminus. Although the functional implication of copper binding to PrPC is still under investigation, copper may play a role in prion disease. In this study, we describe transgenic mice expressing mouse prion protein replacing histidine 95 by tyrosine (PrP H95Y) to disrupt the non-OR copper-binding site. Transgenic mice overexpressing PrP H95Y showed clinical signs and died at about 100 days with spongiform degeneration and PK-resistant PrP. Inoculation of brain homogenate from mice overexpressing PrP H95Y to Tga20 mice expressing wild-type PrP also causes lethal, spongiform encephalopathy. We conclude that this substitution could promote PrPC-PrPSc conversion and induce spontaneous prion disease in vivo. ; This work was partially supported by the Spanish research projects PID2019-105837RB-I00 (J.M.T., J.C.E., A.M.M. and S.C.) and PID2023-146146NB-I00 (J.M.T., J.C.E., and S.C.), both financed by MCIU/AEI/10.13039/501100011033; fellowship FPU22/03361 (S.C.) financed by the Ministerio de Ciencia, Innovación y Universidades and fellowship SGIT-2015-02 (A.M.M) financed by the Instituto Nacional de Investigación y Tecnología Agraria y Allimentaria; the Italian Ministry of Health (RRC) and Associazione Italiana Encefalopatie da Prioni (AIEnP) (F.M).The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. ; Peer reviewed
Document Type: article in journal/newspaper
File Description: application/pdf
Language: English
Relation: #PLACEHOLDER_PARENT_METADATA_VALUE#; info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2019-105837RB-I00/ES/EVOLUCION A TRAVES DE LA BARRERA DE ESPECIE DEL POTECIAL ZOONOTICO DE LOS PRIONES EMERGENTES/; info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2023-146146NB-I00/ES/EVOLUCION DE CEPAS ATIPICAS (NOR98-LIKE) HACIA PRIONES CLASICOS/; Centro de Investigación en Sanidad Animal, (CISA); Torres, Juan María; Marín-Moreno, Alba; Espinosa, Juan Carlos; Canoyra, Sara; Burato, Anna; Ciullini, Arianna; De Luca, Chiara Maria Giulia; Bistaffa, Edoardo; Moda, F.; Legname, Giuseppe; 2025; The 3F4–epitope tag has no effect on prion conversion [Dataset]; Figshare; https://doi.org/10.1371/journal.ppat.1013554.s001; Torres, Juan María; Marín-Moreno, Alba; Espinosa, Juan Carlos; Canoyra, Sara; Burato, Anna; Ciullini, Arianna; De Luca, Chiara Maria Giulia; Bistaffa, Edoardo; Moda, F.; Legname, Giuseppe; 2025; The histidine substitutions in the OR and non-OR regions are not toxic for cell culture [Dataset]; Figshare; https://doi.org/10.1371/journal.ppat.1013554.s002; Torres, Juan María; Marín-Moreno, Alba; Espinosa, Juan Carlos; Canoyra, Sara; Burato, Anna; Ciullini, Arianna; De Luca, Chiara Maria Giulia; Bistaffa, Edoardo; Moda, F.; Legname, Giuseppe; 2025; Titration of proteinase K digestion of the brain PrPres from MoPrP H95Y mice [Dataset]; Figshare; https://doi.org/10.1371/journal.ppat.1013554.s003; Torres, Juan María; Marín-Moreno, Alba; Espinosa, Juan Carlos; Canoyra, Sara; Burato, Anna; Ciullini, Arianna; De Luca, Chiara Maria Giulia; Bistaffa, Edoardo; Moda, F.; Legname, Giuseppe; 2025; Immunohistochemical analysis of PrPres using different antibodies [Dataset]; Figshare; https://doi.org/10.1371/journal.ppat.1013554.s004; https://doi.org/10.1371/journal.ppat.1013554; Sí; PLoS Pathogens 21(10): e1013554 (2025); https://hdl.handle.net/10261/406714; http://dx.doi.org/10.13039/501100011033; http://dx.doi.org/10.13039/501100000780; http://dx.doi.org/10.13039/501100003196; https://api.elsevier.com/content/abstract/scopus_id/105019008771
DOI: 10.1371/journal.ppat.1013554
DOI: 10.13039/501100011033
DOI: 10.13039/501100000780
DOI: 10.13039/501100003196
Availability: https://hdl.handle.net/10261/406714; https://doi.org/10.1371/journal.ppat.1013554; https://doi.org/10.13039/501100011033; https://doi.org/10.13039/501100000780; https://doi.org/10.13039/501100003196; https://api.elsevier.com/content/abstract/scopus_id/105019008771
Rights: info:eu-repo/semantics/openAccess
Accession Number: edsbas.76BB42C9
Database: BASE