Evidence map›Paper›PMID 21589935›Full record

ArticlePloS one2011

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

Christopher J Johnson, James P Bennett, Steven M Biro, Juan Camilo Duque-Velasquez, Cynthia M Rodriguez, Richard A Bessen, Tonie E Rocke

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.7field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. The Ecology of Prions.Microbiology and molecular biology reviews : MMBR · 2017
    Review
  11. Prions: Beyond a Single Protein.Clinical microbiology reviews · 2016
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 6 institutions in 3 countries.

Christopher J JohnsonPrion Research Laboratory, United States Geological Survey National Wildlife Health Center, Madison, Wisconsin, United States of America. cjjohnson@usgs.gov
James P Bennett
Steven M Biro
Juan Camilo Duque-Velasquez
Cynthia M Rodriguez
Richard A Bessen
Tonie E Rocke
National Wildlife Health Center · USInstituto de Investigaciones en Ciencias Agrarias de Rosario · ARMontana Molecular (United States) · USUnited States Geological Survey · USUniversity of Wisconsin–Madison · USWisconsin Institutes for Discovery · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

AnimalsCricetinaeDeerHydrogen-Ion ConcentrationLichensMicePlant ExtractsPrion DiseasesPrionsSerine ProteasesPlant ExtractsPrionsSerine Proteases

Identifiers

PMID21589935
PMCPMC3092769
OpenAlexW2146561813

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.