Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro.

Prion diseases like Creutzfeldt-Jakob disease in humans, Scrapie in sheep or bovine spongiform encephalopathy are fatal neurodegenerative diseases, which can be of sporadic, genetic, or infectious origin. Prion diseases are transmissible between different species, however, with a variable species ba...

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Autores principales:	Giannantonio Panza, Lars Luers, Jan Stöhr, Luitgard Nagel-Steger, Jürgen Weiss, Detlev Riesner, Dieter Willbold, Eva Birkmann
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/b2431ef0d6374eac9693093cffcd8333
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spelling	oai:doaj.org-article:b2431ef0d6374eac9693093cffcd83332021-11-18T07:01:55ZMolecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro.1932-620310.1371/journal.pone.0014283https://doaj.org/article/b2431ef0d6374eac9693093cffcd83332010-12-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21151607/?tool=EBIhttps://doaj.org/toc/1932-6203Prion diseases like Creutzfeldt-Jakob disease in humans, Scrapie in sheep or bovine spongiform encephalopathy are fatal neurodegenerative diseases, which can be of sporadic, genetic, or infectious origin. Prion diseases are transmissible between different species, however, with a variable species barrier. The key event of prion amplification is the conversion of the cellular isoform of the prion protein (PrP(C)) into the pathogenic isoform (PrP(Sc)). We developed a sodiumdodecylsulfate-based PrP conversion system that induces amyloid fibril formation from soluble α-helical structured recombinant PrP (recPrP). This approach was extended applying pre-purified PrP(Sc) as seeds which accelerate fibrillization of recPrP. In the present study we investigated the interspecies coherence of prion disease. Therefore we used PrP(Sc) from different species like Syrian hamster, cattle, mouse and sheep and seeded fibrillization of recPrP from the same or other species to mimic in vitro the natural species barrier. We could show that the in vitro system of seeded fibrillization is in accordance with what is known from the naturally occurring species barriers.Giannantonio PanzaLars LuersJan StöhrLuitgard Nagel-StegerJürgen WeissDetlev RiesnerDieter WillboldEva BirkmannPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 5, Iss 12, p e14283 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Giannantonio Panza Lars Luers Jan Stöhr Luitgard Nagel-Steger Jürgen Weiss Detlev Riesner Dieter Willbold Eva Birkmann Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro.
description	Prion diseases like Creutzfeldt-Jakob disease in humans, Scrapie in sheep or bovine spongiform encephalopathy are fatal neurodegenerative diseases, which can be of sporadic, genetic, or infectious origin. Prion diseases are transmissible between different species, however, with a variable species barrier. The key event of prion amplification is the conversion of the cellular isoform of the prion protein (PrP(C)) into the pathogenic isoform (PrP(Sc)). We developed a sodiumdodecylsulfate-based PrP conversion system that induces amyloid fibril formation from soluble α-helical structured recombinant PrP (recPrP). This approach was extended applying pre-purified PrP(Sc) as seeds which accelerate fibrillization of recPrP. In the present study we investigated the interspecies coherence of prion disease. Therefore we used PrP(Sc) from different species like Syrian hamster, cattle, mouse and sheep and seeded fibrillization of recPrP from the same or other species to mimic in vitro the natural species barrier. We could show that the in vitro system of seeded fibrillization is in accordance with what is known from the naturally occurring species barriers.
format	article
author	Giannantonio Panza Lars Luers Jan Stöhr Luitgard Nagel-Steger Jürgen Weiss Detlev Riesner Dieter Willbold Eva Birkmann
author_facet	Giannantonio Panza Lars Luers Jan Stöhr Luitgard Nagel-Steger Jürgen Weiss Detlev Riesner Dieter Willbold Eva Birkmann
author_sort	Giannantonio Panza
title	Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro.
title_short	Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro.
title_full	Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro.
title_fullStr	Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro.
title_full_unstemmed	Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro.
title_sort	molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/b2431ef0d6374eac9693093cffcd8333
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Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro.

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