White-tailed deer S96 prion protein does not support stable in vitro propagation of most common CWD strains

Abstract PrPC variation at residue 96 (G/S) plays an important role in the epidemiology of chronic wasting disease (CWD) in exposed white-tailed deer populations. In vivo studies have demonstrated the protective effect of serine at codon 96, which hinders the propagation of common CWD strains when e...

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Autores principales:	Alicia Otero, Camilo Duque Velásquez, Judd Aiken, Debbie McKenzie
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/feabaed0ca0c469995e0ee56a430bf75
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spelling	oai:doaj.org-article:feabaed0ca0c469995e0ee56a430bf752021-12-02T14:47:31ZWhite-tailed deer S96 prion protein does not support stable in vitro propagation of most common CWD strains10.1038/s41598-021-90606-82045-2322https://doaj.org/article/feabaed0ca0c469995e0ee56a430bf752021-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-90606-8https://doaj.org/toc/2045-2322Abstract PrPC variation at residue 96 (G/S) plays an important role in the epidemiology of chronic wasting disease (CWD) in exposed white-tailed deer populations. In vivo studies have demonstrated the protective effect of serine at codon 96, which hinders the propagation of common CWD strains when expressed in homozygosis and increases the survival period of S96/wt heterozygous deer after challenge with CWD. Previous in vitro studies of the transmission barrier suggested that following a single amplification step, wt and S96 PrPC were equally susceptible to misfolding when seeded with various CWD prions. When we performed serial prion amplification in vitro using S96-PrPC, we observed a reduction in the efficiency of propagation with the Wisc-1 or CWD2 strains, suggesting these strains cannot stably template their conformations on this PrPC once the primary sequence has changed after the first round of replication. Our data shows the S96-PrPC polymorphism is detrimental to prion conversion of some CWD strains. These data suggests that deer homozygous for S96-PrPC may not sustain prion transmission as compared to a deer expressing G96-PrPC.Alicia OteroCamilo Duque VelásquezJudd AikenDebbie McKenzieNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Alicia Otero Camilo Duque Velásquez Judd Aiken Debbie McKenzie White-tailed deer S96 prion protein does not support stable in vitro propagation of most common CWD strains
description	Abstract PrPC variation at residue 96 (G/S) plays an important role in the epidemiology of chronic wasting disease (CWD) in exposed white-tailed deer populations. In vivo studies have demonstrated the protective effect of serine at codon 96, which hinders the propagation of common CWD strains when expressed in homozygosis and increases the survival period of S96/wt heterozygous deer after challenge with CWD. Previous in vitro studies of the transmission barrier suggested that following a single amplification step, wt and S96 PrPC were equally susceptible to misfolding when seeded with various CWD prions. When we performed serial prion amplification in vitro using S96-PrPC, we observed a reduction in the efficiency of propagation with the Wisc-1 or CWD2 strains, suggesting these strains cannot stably template their conformations on this PrPC once the primary sequence has changed after the first round of replication. Our data shows the S96-PrPC polymorphism is detrimental to prion conversion of some CWD strains. These data suggests that deer homozygous for S96-PrPC may not sustain prion transmission as compared to a deer expressing G96-PrPC.
format	article
author	Alicia Otero Camilo Duque Velásquez Judd Aiken Debbie McKenzie
author_facet	Alicia Otero Camilo Duque Velásquez Judd Aiken Debbie McKenzie
author_sort	Alicia Otero
title	White-tailed deer S96 prion protein does not support stable in vitro propagation of most common CWD strains
title_short	White-tailed deer S96 prion protein does not support stable in vitro propagation of most common CWD strains
title_full	White-tailed deer S96 prion protein does not support stable in vitro propagation of most common CWD strains
title_fullStr	White-tailed deer S96 prion protein does not support stable in vitro propagation of most common CWD strains
title_full_unstemmed	White-tailed deer S96 prion protein does not support stable in vitro propagation of most common CWD strains
title_sort	white-tailed deer s96 prion protein does not support stable in vitro propagation of most common cwd strains
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/feabaed0ca0c469995e0ee56a430bf75
work_keys_str_mv	AT aliciaotero whitetaileddeers96prionproteindoesnotsupportstableinvitropropagationofmostcommoncwdstrains AT camiloduquevelasquez whitetaileddeers96prionproteindoesnotsupportstableinvitropropagationofmostcommoncwdstrains AT juddaiken whitetaileddeers96prionproteindoesnotsupportstableinvitropropagationofmostcommoncwdstrains AT debbiemckenzie whitetaileddeers96prionproteindoesnotsupportstableinvitropropagationofmostcommoncwdstrains
_version_	1718389547335680000

White-tailed deer S96 prion protein does not support stable in vitro propagation of most common CWD strains

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