Evidence map›Paper›PMID 25304654›Full record

ArticleThe Journal of general virology2015

Quantitative assessment of prion infectivity in tissues and body fluids by real-time quaking-induced conversion.

Davin M Henderson, Kristen A Davenport, Nicholas J Haley, Nathaniel D Denkers, Candace K Mathiason, Edward A Hoover

Open access · greenAbstract read
In one paragraph

Article in The Journal of general virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

86 citing papers in PubMed, 130 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Prion Partitioning and Persistence in Environmental Waters.Environmental science & technology · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Chronic Wasting Disease: State of the Science.Pathogens (Basel, Switzerland) · 2024
    Review
  17. Article
  18. Article
  19. Article
  20. Article

26 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 1 country.

Davin M HendersonPrion Research Center, College of Veterinary Medicine and Biomedical Sciences, Colorado State University, Fort Collins, CO 80523, USA.
Kristen A DavenportPrion Research Center, College of Veterinary Medicine and Biomedical Sciences, Colorado State University, Fort Collins, CO 80523, USA.
Nicholas J HaleyDepartment of Diagnostic Medicine and Pathobiology, Kansas State University, College of Veterinary Medicine, Manhattan, KS 66506, USA.
Nathaniel D DenkersPrion Research Center, College of Veterinary Medicine and Biomedical Sciences, Colorado State University, Fort Collins, CO 80523, USA.
Candace K MathiasonPrion Research Center, College of Veterinary Medicine and Biomedical Sciences, Colorado State University, Fort Collins, CO 80523, USA.
Edward A HooverPrion Research Center, College of Veterinary Medicine and Biomedical Sciences, Colorado State University, Fort Collins, CO 80523, USA.
Colorado State University · USKansas State University · US

Funding

Biomedical Research Training for VeterinariansT32OD010437 · OD · COLORADO STATE UNIVERSITY · PI Gregg A Dean, KELLY S SANTANGELO · 2012 to 2026
$6.2M
Transmission and Pathogenesis of Chronic Wasting Disease (CWD)R01NS061902 · NINDS · COLORADO STATE UNIVERSITY · PI MATHIASON, CANDACE K. · 2009 to 2022
$5.3M
Characterizing the Role of Protein Interactions in Prion Disease Species BarriersF30OD021442 · OD · COLORADO STATE UNIVERSITY · PI DAVENPORT, KRISTEN ANNE · 2015 to 2018
$166k
NIH HHS F30 OD021442NIH HHS T32 OD010437NINDS NIH HHS R01 NS-061902NINDS NIH HHS R01 NS061902
6 · The paper itself

Abstract

Prions are amyloid-forming proteins that cause transmissible spongiform encephalopathies through a process involving the templated conversion of the normal cellular prion protein (PrP(C)) to a pathogenic misfolded conformation. Templated conversion has been modelled in several in vitro assays, including serial protein misfolding amplification, amyloid seeding and real-time quaking-induced conversion (RT-QuIC). As RT-QuIC measures formation of amyloid fibrils in real-time, it can be used to estimate the rate of seeded conversion. Here, we used samples from deer infected with chronic wasting disease (CWD) in RT-QuIC to show that serial dilution of prion seed was linearly related to the rate of amyloid formation over a range of 10(-3) to 10(-8) µg. We then used an amyloid formation rate standard curve derived from a bioassayed reference sample (CWD+ brain homogenate) to estimate the prion seed concentration and infectivity in tissues, body fluids and excreta. Using these methods, we estimated that urine and saliva from CWD-infected deer both contained 1-5 LD50 per 10 ml. Thus, over the 1-2 year course of an infection, a substantial environmental reservoir of CWD prion contamination accumulates.

Indexed as

AmyloidAnimalsBiological AssayBody FluidsBrainDeerPrion DiseasesPrionsSalivaUrineWasting Disease, ChronicAmyloidPrions

Identifiers

PMID25304654
PMCPMC4268821
OpenAlexW2063623360

What OpenQuestion holds

Textmetadata
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.