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Lichens: unexpected anti-prion agents?

Prion

By:
, ,
DOI: 10.4161/pri.6.1.17414

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Abstract

The prion diseases sheep scrapie and cervid chronic wasting disease are transmitted, in part, via an environmental reservoir of infectivity; prions released from infected animals persist in the environment and can cause disease years later. Central to controlling disease transmission is the identification of methods capable of inactivating these agents on the landscape. We have found that certain lichens, common, ubiquitous, symbiotic organisms, possess a serine protease capable of degrading prion protein (PrP) from prion-infected animals. The protease functions against a range of prion strains from various hosts and reduces levels of abnormal PrP by at least two logs. We have now tested more than 20 lichen species from several geographical locations and from various taxa and found that approximately half of these species degrade PrP. Critical next steps include examining the effect of lichens on prion infectivity and cloning the protease responsible for PrP degradation. The impact of lichens on prions in the environment remains unknown. We speculate that lichens could have the potential to degrade prions when they are shed from infected animals onto lichens or into environments where lichens are abundant. In addition, lichens are frequently consumed by cervids and many other animals and the effect of dietary lichens on prion disease transmission should also be considered.

Additional Publication Details

Publication type:
Article
Publication Subtype:
Journal Article
Title:
Lichens: unexpected anti-prion agents?
Series title:
Prion
DOI:
10.4161/pri.6.1.17414
Volume
6
Issue:
1
Year Published:
2012
Language:
English
Publisher:
Landes Bioscience
Contributing office(s):
National Wildlife Health Center
Description:
6 p.
Larger Work Type:
Article
Larger Work Subtype:
Journal Article
Larger Work Title:
Prion
First page:
11
Last page:
16