Porcine Prion Protein as a Paradigm of Limited Susceptibility to Prion Strain Propagation
10 Pág. Centro de Investigación en Sanidad Animal (CISA)
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| Format: | artículo biblioteca |
| Language: | English |
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Oxford University Press
2021-03-15
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| Subjects: | BSE, PrP, Atypical/Nor98 scrapie, Classic scrapie, Pig, Prion conversion, Prion strains, Swine, |
| Online Access: | http://hdl.handle.net/10261/286725 http://dx.doi.org/10.13039/501100011033 http://dx.doi.org/10.13039/501100003329 http://dx.doi.org/10.13039/501100000354 http://dx.doi.org/10.13039/501100000780 https://api.elsevier.com/content/abstract/scopus_id/85103682065 |
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dig-inia-es-10261-2867252023-02-06T21:35:43Z Porcine Prion Protein as a Paradigm of Limited Susceptibility to Prion Strain Propagation Espinosa, Juan Carlos Marín-Moreno, Alba Aguilar-Calvo, Patricia Benestad, Sylvie L Andreoletti, Olivier Torres, Juan María Ministerio de Economía y Competitividad (España) Agencia Estatal de Investigación (España) European Commission Food Standards Agency (UK) Espinosa, Juan Carlos [0000-0002-6719-9902] Marín-Moreno, Alba (0000-0002-4023-6398) Benestad, Sylvie L (0000-0002-3011-0484) Andreoletti, Olivier (0000-0002-7369-6016) Torres, Juan María (0000-0003-0443-9232) BSE PrP Atypical/Nor98 scrapie Classic scrapie Pig Prion conversion Prion strains Swine 10 Pág. Centro de Investigación en Sanidad Animal (CISA) Although experimental transmission of bovine spongiform encephalopathy (BSE) to pigs and transgenic mice expressing pig cellular prion protein (PrPC) (porcine PrP [PoPrP]-Tg001) has been described, no natural cases of prion diseases in pig were reported. This study analyzed pig-PrPC susceptibility to different prion strains using PoPrP-Tg001 mice either as animal bioassay or as substrate for protein misfolding cyclic amplification (PMCA). A panel of isolates representatives of different prion strains was selected, including classic and atypical/Nor98 scrapie, atypical-BSE, rodent scrapie, human Creutzfeldt-Jakob-disease and classic BSE from different species. Bioassay proved that PoPrP-Tg001-mice were susceptible only to the classic BSE agent, and PMCA results indicate that only classic BSE can convert pig-PrPC into scrapie-type PrP (PrPSc), independently of the species origin. Therefore, conformational flexibility constraints associated with pig-PrP would limit the number of permissible PrPSc conformations compatible with pig-PrPC, thus suggesting that pig-PrPC may constitute a paradigm of low conformational flexibility that could confer high resistance to the diversity of prion strains. This work was supported by the Spanish Ministerio de Economía y Competitividad (grants AGL2012- 37988-C04-04 and AGL2016-78054-R [Agencia Estatal de Investigación/Fondo Europeo de Desarrollo Regional, Unión Europea] to J. C. E. and J. M. T., fellowship BES-2010–040922 to P. A. C., and fellowship INIA-FPI-SGIT-2015-02 to A. M. M.), the UK Food Standards Agency (project FS231051 [“Permeability of the Human Species Barriers to TSE Circulating Agents”]), and the Fonds Europeens de Developpement Regional Programme Operationnel de Cooperation Territoriale Espagne France Andorre REDPRION (project EFA148/16 [REDPRION] to O. A.) Peer reviewed 2023-01-13T09:17:23Z 2023-01-13T09:17:23Z 2021-03-15 artículo Journal of Infectious Diseases 223(6): 1103–1112 (2021) 0022-1899 http://hdl.handle.net/10261/286725 10.1093/infdis/jiz646 http://dx.doi.org/10.13039/501100011033 http://dx.doi.org/10.13039/501100003329 http://dx.doi.org/10.13039/501100000354 http://dx.doi.org/10.13039/501100000780 31919511 2-s2.0-85103682065 https://api.elsevier.com/content/abstract/scopus_id/85103682065 en #PLACEHOLDER_PARENT_METADATA_VALUE# #PLACEHOLDER_PARENT_METADATA_VALUE# #PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/MINECO//AGL2012-37988-C04-04/ES/DISECCION IN VITRO E IN VIVO DE LOS MECANISMOS MOLECULARES IMPLICADOS EN LA REPLICACION DE LOS PRIONES SUPERANDO BARRERAS DE TRANSMISION EXISTENTES EN LA NATURALEZA/ info:eu-repo/grantAgreement/AEI-EC//AGL2016-78054-R info:eu-repo/grantAgreement/INIA-FPI-SGIT-2015-02//BES-2010–040922 The Journal of infectious diseases Publisher's version https://doi.org/10.1093/infdis/jiaa073 Sí open Oxford University Press |
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BSE PrP Atypical/Nor98 scrapie Classic scrapie Pig Prion conversion Prion strains Swine BSE PrP Atypical/Nor98 scrapie Classic scrapie Pig Prion conversion Prion strains Swine |
| spellingShingle |
BSE PrP Atypical/Nor98 scrapie Classic scrapie Pig Prion conversion Prion strains Swine BSE PrP Atypical/Nor98 scrapie Classic scrapie Pig Prion conversion Prion strains Swine Espinosa, Juan Carlos Marín-Moreno, Alba Aguilar-Calvo, Patricia Benestad, Sylvie L Andreoletti, Olivier Torres, Juan María Porcine Prion Protein as a Paradigm of Limited Susceptibility to Prion Strain Propagation |
| description |
10 Pág.
Centro de Investigación en Sanidad Animal (CISA) |
| author2 |
Ministerio de Economía y Competitividad (España) |
| author_facet |
Ministerio de Economía y Competitividad (España) Espinosa, Juan Carlos Marín-Moreno, Alba Aguilar-Calvo, Patricia Benestad, Sylvie L Andreoletti, Olivier Torres, Juan María |
| format |
artículo |
| topic_facet |
BSE PrP Atypical/Nor98 scrapie Classic scrapie Pig Prion conversion Prion strains Swine |
| author |
Espinosa, Juan Carlos Marín-Moreno, Alba Aguilar-Calvo, Patricia Benestad, Sylvie L Andreoletti, Olivier Torres, Juan María |
| author_sort |
Espinosa, Juan Carlos |
| title |
Porcine Prion Protein as a Paradigm of Limited Susceptibility to Prion Strain Propagation |
| title_short |
Porcine Prion Protein as a Paradigm of Limited Susceptibility to Prion Strain Propagation |
| title_full |
Porcine Prion Protein as a Paradigm of Limited Susceptibility to Prion Strain Propagation |
| title_fullStr |
Porcine Prion Protein as a Paradigm of Limited Susceptibility to Prion Strain Propagation |
| title_full_unstemmed |
Porcine Prion Protein as a Paradigm of Limited Susceptibility to Prion Strain Propagation |
| title_sort |
porcine prion protein as a paradigm of limited susceptibility to prion strain propagation |
| publisher |
Oxford University Press |
| publishDate |
2021-03-15 |
| url |
http://hdl.handle.net/10261/286725 http://dx.doi.org/10.13039/501100011033 http://dx.doi.org/10.13039/501100003329 http://dx.doi.org/10.13039/501100000354 http://dx.doi.org/10.13039/501100000780 https://api.elsevier.com/content/abstract/scopus_id/85103682065 |
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