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Prion protein degradation by lichens of the genus Cladonia

Lichenologist

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Abstract

It has recently been discovered that lichens contain a serine protease capable of degrading the pathogenic prion protein, the etiological agent of prion diseases such as sheep scrapie and cervid chronic wasting disease. Limited methods are available to degrade or inactivate prion disease agents, especially in the environment, and lichens or their serine protease could prove important for management of these diseases. Scant information is available regarding the presence or absence of the protease responsible for degrading prion protein (PrP) in lichen species and, in this study, we tested the hypothesis that PrP degradation activity in lichens is phylogenetically-based by testing 44 species of Cladonia lichens, a genus for which a significant portion of the phylogeny is well established. We categorized PrP degradation activity among the 44 species (high, moderate, low or none) and found that activity in Cladonia species did not correspond with phylogenetic position of the species. Degradation of PrP did correspond, however, with three classical taxonomic characters within the genus: species with brown apothecia, no usnic acid, and the presence of a cortex. Of the 44 species studied, 18 (41%) had either high or moderate PrP degradation activity, suggesting the protease may be frequent in this genus of lichens.

Additional Publication Details

Publication type:
Article
Publication Subtype:
Journal Article
Title:
Prion protein degradation by lichens of the genus Cladonia
Series title:
Lichenologist
Volume
44
Issue:
4
Year Published:
2012
Language:
English
Publisher:
Cambridge University Press
Publisher location:
Cambridge, U.K.
Contributing office(s):
National Wildlife Health Center
Description:
9 p.
Larger Work Type:
Article
Larger Work Subtype:
Journal Article
First page:
523
Last page:
531