Evidence map›Paper›PMID 26086786›Full record

ArticlePLoS pathogens2015

Bank Vole Prion Protein As an Apparently Universal Substrate for RT-QuIC-Based Detection and Discrimination of Prion Strains.

Christina D Orrú, Bradley R Groveman, Lynne D Raymond, Andrew G Hughson, Romolo Nonno, Wenquan Zou, Bernardino Ghetti, Pierluigi Gambetti, Byron Caughey

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 134 papers.

0numbers the graph read from it
0cells of the map it votes in
134citing papers in PubMed
9.5field-weighted citation impact, top 1% 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

134 citing papers in PubMed, 173 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Novel Prion Protein Gene (bioRxiv : the preprint server for biology · 2026
    Article
  8. Article
  9. Article
  10. Enhanced lysosomal activity prevents infection with PrPThe Journal of biological chemistry · 2026
    Article
  11. Insights into the Diagnosis, Treatment, and Management of Prion Diseases.CNS & neurological disorders drug targets · 2026
    Review
  12. Article
  13. Review
  14. Article
  15. Partial Deletion of the Carboxyl-Terminal Signal Sequence of the Cellular Prion Protein Alters Protein Expression via Endoplasmic Reticulum-Associated Degradation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 5 institutions in 2 countries.

Christina D OrrúLaboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Hamilton, Montana, United States of America.
Bradley R GrovemanLaboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Hamilton, Montana, United States of America.
Lynne D RaymondLaboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Hamilton, Montana, United States of America.
Andrew G HughsonLaboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Hamilton, Montana, United States of America.
Romolo NonnoDepartment of Veterinary Public Health and Food Safety, Istituto Superiore di Sanità, Rome, Italy.
Wenquan ZouDepartment of Pathology, Case Western Reserve University, Cleveland, Ohio, United States of America.
Bernardino GhettiDepartment of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, Indiana, United States of America.
Pierluigi GambettiDepartment of Pathology, Case Western Reserve University, Cleveland, Ohio, United States of America.
Byron CaugheyLaboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Hamilton, Montana, United States of America.
National Institutes of Health · USCase Western Reserve University · USNational Institute of Allergy and Infectious Diseases · USIndiana University School of MedicineIstituto Superiore di Sanità · IT

Funding

Research Education ComponentP30AG010133 · NIA · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI SAYKIN, ANDREW J · 1991 to 2020
$37.3M
Detection of PrionsZIAAI001086 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI CAUGHEY, BYRON · 2009 to 2025
$18.1M
Neuropathology Core - P GambettiP01AI106705 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI GAMBETTI, PIERLUIGI · 2014 to 2018
$7.7M
Structural correlates of prion strain, phenotype and infectivity in human prion dR01NS083687 · NINDS · CASE WESTERN RESERVE UNIVERSITY · PI GAMBETTI, PIERLUIGI, SUREWICZ, WITOLD K · 2014 to 2018
$2.9M
Pathogenicity of prion protein aggregates from uninfected cells and brainsR01NS062787 · NINDS · CASE WESTERN RESERVE UNIVERSITY · PI ZOU, WEN-QUAN · 2009 to 2013
$1.4M
Intramural NIH HHS ZIA AI001086NCEZID CDC HHS 1051CK000100NCEZID CDC HHS U51 CK000100NIAID NIH HHS AI001086-06NIAID NIH HHS P01 1AI106705-01AINIAID NIH HHS P01 AI106705NIA NIH HHS P30 AG10133NINDS NIH HHS R01 NS062787NINDS NIH HHS R01 NS083687
6 · The paper itself

Abstract

Prions propagate as multiple strains in a wide variety of mammalian species. The detection of all such strains by a single ultrasensitive assay such as Real Time Quaking-induced Conversion (RT-QuIC) would facilitate prion disease diagnosis, surveillance and research. Previous studies have shown that bank voles, and transgenic mice expressing bank vole prion protein, are susceptible to most, if not all, types of prions. Here we show that bacterially expressed recombinant bank vole prion protein (residues 23-230) is an effective substrate for the sensitive RT-QuIC detection of all of the different prion types that we have tested so far--a total of 28 from humans, cattle, sheep, cervids and rodents, including several that have previously been undetectable by RT-QuIC or Protein Misfolding Cyclic Amplification. Furthermore, comparison of the relative abilities of different prions to seed positive RT-QuIC reactions with bank vole and not other recombinant prion proteins allowed discrimination of prion strains such as classical and atypical L-type bovine spongiform encephalopathy, classical and atypical Nor98 scrapie in sheep, and sporadic and variant Creutzfeldt-Jakob disease in humans. Comparison of protease-resistant RT-QuIC conversion products also aided strain discrimination and suggested the existence of several distinct classes of prion templates among the many strains tested.

Indexed as

AnimalsArvicolinaeCricetinaeHumansImmunoblottingMicePrionsPrions

Identifiers

PMID26086786
PMCPMC4472236
OpenAlexW1533232091

What OpenQuestion holds

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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.