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      Lichens: unexpected anti-prion agents?

      1 , ,

      Prion

      Informa UK Limited

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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 twenty 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.

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          Author and article information

          Journal
          Prion
          Prion
          Informa UK Limited
          1933-690X
          1933-6896
          March 29 2012
          : 6
          : 1
          Affiliations
          [1 ] USGS National Wildlife Health Center; Department of Bacteriology, University of Wisconsin, Madison, WI, USA.
          Article
          17414
          10.4161/pri.6.1.17414
          3338958
          22453171

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