Degradation of the disease-associated prion protein by a serine protease from lichens.

The disease-associated prion protein (PrP(TSE)), the probable etiological agent of the transmissible spongiform encephalopathies (TSEs), is resistant to degradation and can persist in the environment. Lichens, mutualistic symbioses containing fungi, algae, bacteria and occasionally cyanobacteria, ar...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Christopher J Johnson, James P Bennett, Steven M Biro, Juan Camilo Duque-Velasquez, Cynthia M Rodriguez, Richard A Bessen, Tonie E Rocke
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/df14b06291c54919a35ed9e4acc4b35c
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:df14b06291c54919a35ed9e4acc4b35c
record_format	dspace
spelling	oai:doaj.org-article:df14b06291c54919a35ed9e4acc4b35c2021-11-18T06:54:08ZDegradation of the disease-associated prion protein by a serine protease from lichens.1932-620310.1371/journal.pone.0019836https://doaj.org/article/df14b06291c54919a35ed9e4acc4b35c2011-05-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21589935/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The disease-associated prion protein (PrP(TSE)), the probable etiological agent of the transmissible spongiform encephalopathies (TSEs), is resistant to degradation and can persist in the environment. Lichens, mutualistic symbioses containing fungi, algae, bacteria and occasionally cyanobacteria, are ubiquitous in the environment and have evolved unique biological activities allowing their survival in challenging ecological niches. We investigated PrP(TSE) inactivation by lichens and found acetone extracts of three lichen species (Parmelia sulcata, Cladonia rangiferina and Lobaria pulmonaria) have the ability to degrade prion protein (PrP) from TSE-infected hamsters, mice and deer. Immunoblots measuring PrP levels and protein misfolding cyclic amplification indicated at least two logs of reductions in PrP(TSE). Degradative activity was not found in closely related lichen species or in algae or a cyanobacterium that inhabit lichens. Degradation was blocked by Pefabloc SC, a serine protease inhibitor, but not inhibitors of other proteases or enzymes. Additionally, we found that PrP levels in PrP(TSE)-enriched preps or infected brain homogenates are also reduced following exposure to freshly-collected P. sulcata or an aqueous extract of the lichen. Our findings indicate that these lichen extracts efficiently degrade PrP(TSE) and suggest that some lichens could have potential to inactivate TSE infectivity on the landscape or be a source for agents to degrade prions. Further work to clone and characterize the protease, assess its effect on TSE infectivity and determine which organism or organisms present in lichens produce or influence the protease activity is warranted.Christopher J JohnsonJames P BennettSteven M BiroJuan Camilo Duque-VelasquezCynthia M RodriguezRichard A BessenTonie E RockePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 5, p e19836 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Christopher J Johnson James P Bennett Steven M Biro Juan Camilo Duque-Velasquez Cynthia M Rodriguez Richard A Bessen Tonie E Rocke Degradation of the disease-associated prion protein by a serine protease from lichens.
description	The disease-associated prion protein (PrP(TSE)), the probable etiological agent of the transmissible spongiform encephalopathies (TSEs), is resistant to degradation and can persist in the environment. Lichens, mutualistic symbioses containing fungi, algae, bacteria and occasionally cyanobacteria, are ubiquitous in the environment and have evolved unique biological activities allowing their survival in challenging ecological niches. We investigated PrP(TSE) inactivation by lichens and found acetone extracts of three lichen species (Parmelia sulcata, Cladonia rangiferina and Lobaria pulmonaria) have the ability to degrade prion protein (PrP) from TSE-infected hamsters, mice and deer. Immunoblots measuring PrP levels and protein misfolding cyclic amplification indicated at least two logs of reductions in PrP(TSE). Degradative activity was not found in closely related lichen species or in algae or a cyanobacterium that inhabit lichens. Degradation was blocked by Pefabloc SC, a serine protease inhibitor, but not inhibitors of other proteases or enzymes. Additionally, we found that PrP levels in PrP(TSE)-enriched preps or infected brain homogenates are also reduced following exposure to freshly-collected P. sulcata or an aqueous extract of the lichen. Our findings indicate that these lichen extracts efficiently degrade PrP(TSE) and suggest that some lichens could have potential to inactivate TSE infectivity on the landscape or be a source for agents to degrade prions. Further work to clone and characterize the protease, assess its effect on TSE infectivity and determine which organism or organisms present in lichens produce or influence the protease activity is warranted.
format	article
author	Christopher J Johnson James P Bennett Steven M Biro Juan Camilo Duque-Velasquez Cynthia M Rodriguez Richard A Bessen Tonie E Rocke
author_facet	Christopher J Johnson James P Bennett Steven M Biro Juan Camilo Duque-Velasquez Cynthia M Rodriguez Richard A Bessen Tonie E Rocke
author_sort	Christopher J Johnson
title	Degradation of the disease-associated prion protein by a serine protease from lichens.
title_short	Degradation of the disease-associated prion protein by a serine protease from lichens.
title_full	Degradation of the disease-associated prion protein by a serine protease from lichens.
title_fullStr	Degradation of the disease-associated prion protein by a serine protease from lichens.
title_full_unstemmed	Degradation of the disease-associated prion protein by a serine protease from lichens.
title_sort	degradation of the disease-associated prion protein by a serine protease from lichens.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/df14b06291c54919a35ed9e4acc4b35c
work_keys_str_mv	AT christopherjjohnson degradationofthediseaseassociatedprionproteinbyaserineproteasefromlichens AT jamespbennett degradationofthediseaseassociatedprionproteinbyaserineproteasefromlichens AT stevenmbiro degradationofthediseaseassociatedprionproteinbyaserineproteasefromlichens AT juancamiloduquevelasquez degradationofthediseaseassociatedprionproteinbyaserineproteasefromlichens AT cynthiamrodriguez degradationofthediseaseassociatedprionproteinbyaserineproteasefromlichens AT richardabessen degradationofthediseaseassociatedprionproteinbyaserineproteasefromlichens AT tonieerocke degradationofthediseaseassociatedprionproteinbyaserineproteasefromlichens
_version_	1718424261290360832

Degradation of the disease-associated prion protein by a serine protease from lichens.

Ejemplares similares