Molecular Model of Prion Transmission to Humans

To assess interspecies barriers to transmission of transmissible spongiform encephalopathies, we investigated the ability of disease-associated prion proteins (PrP(d)) to initiate conversion of the human normal cellular form of prion protein of the 3 major PRNP polymorphic variants in vitro. Protein...

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Detalles Bibliográficos
Autores principales: Jones, Michael, Wight, Darren, Barron, Rona, Jeffrey, Martin, Manson, Jean, Prowse, Christopher, Ironside, James W., Head, Mark W.
Formato: Texto
Lenguaje:English
Publicado: Centers for Disease Control and Prevention 2009
Materias:
Dispatch
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3044515/
https://www.ncbi.nlm.nih.gov/pubmed/19961689
http://dx.doi.org/10.3201/eid1512.090194
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author Jones, Michael
Wight, Darren
Barron, Rona
Jeffrey, Martin
Manson, Jean
Prowse, Christopher
Ironside, James W.
Head, Mark W.
author_facet Jones, Michael
Wight, Darren
Barron, Rona
Jeffrey, Martin
Manson, Jean
Prowse, Christopher
Ironside, James W.
Head, Mark W.
author_sort Jones, Michael
collection PubMed
description To assess interspecies barriers to transmission of transmissible spongiform encephalopathies, we investigated the ability of disease-associated prion proteins (PrP(d)) to initiate conversion of the human normal cellular form of prion protein of the 3 major PRNP polymorphic variants in vitro. Protein misfolding cyclic amplification showed that conformation of PrP(d) partly determines host susceptibility.
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spelling pubmed-30445152011-03-07 Molecular Model of Prion Transmission to Humans Jones, Michael Wight, Darren Barron, Rona Jeffrey, Martin Manson, Jean Prowse, Christopher Ironside, James W. Head, Mark W. Emerg Infect Dis Dispatch To assess interspecies barriers to transmission of transmissible spongiform encephalopathies, we investigated the ability of disease-associated prion proteins (PrP(d)) to initiate conversion of the human normal cellular form of prion protein of the 3 major PRNP polymorphic variants in vitro. Protein misfolding cyclic amplification showed that conformation of PrP(d) partly determines host susceptibility. Centers for Disease Control and Prevention 2009-12 /pmc/articles/PMC3044515/ /pubmed/19961689 http://dx.doi.org/10.3201/eid1512.090194 Text en https://creativecommons.org/licenses/by/4.0/This is a publication of the U.S. Government. This publication is in the public domain and is therefore without copyright. All text from this work may be reprinted freely. Use of these materials should be properly cited.
spellingShingle Dispatch
Jones, Michael
Wight, Darren
Barron, Rona
Jeffrey, Martin
Manson, Jean
Prowse, Christopher
Ironside, James W.
Head, Mark W.
Molecular Model of Prion Transmission to Humans
title Molecular Model of Prion Transmission to Humans
title_full Molecular Model of Prion Transmission to Humans
title_fullStr Molecular Model of Prion Transmission to Humans
title_full_unstemmed Molecular Model of Prion Transmission to Humans
title_short Molecular Model of Prion Transmission to Humans
title_sort molecular model of prion transmission to humans
topic Dispatch
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3044515/
https://www.ncbi.nlm.nih.gov/pubmed/19961689
http://dx.doi.org/10.3201/eid1512.090194
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