Prion protein degradation by lichens of the genusCladonia
| Autor: | Cynthia M. Rodriguez, Christopher J. Johnson, James P. Bennett |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Serine protease
Protease Transmissible spongiform encephalopathy Cladonia biology medicine.medical_treatment Usnic acid Scrapie biology.organism_classification medicine.disease Microbiology chemistry.chemical_compound chemistry Phylogenetics Botany medicine biology.protein Lichen Ecology Evolution Behavior and Systematics |
| Zdroj: | The Lichenologist. 44:523-531 |
| ISSN: | 1096-1135 0024-2829 |
| DOI: | 10.1017/s0024282912000102 |
| Popis: | 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 ofCladonialichens, 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 inCladoniaspecies 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. |
| Databáze: | OpenAIRE |
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