Evidence map›Paper›PMID 26739160›Full record

ArticleJournal of clinical microbiology2016

Detection of Atypical H-Type Bovine Spongiform Encephalopathy and Discrimination of Bovine Prion Strains by Real-Time Quaking-Induced Conversion.

Kentaro Masujin, Christina D Orrú, Kohtaro Miyazawa, Bradley R Groveman, Lynne D Raymond, Andrew G Hughson, Byron Caughey

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Journal of clinical microbiology, 2016. 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 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
5.0field-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

34 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Tracking Prions by RT-QuIC: An Update.Sub-cellular biochemistry · 2025
    Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Real-Time Quaking-Induced Conversion Detection of PrPFrontiers in veterinary science · 2021
    Article
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  13. Review
  14. Review
  15. Review
  16. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 2 countries.

Kentaro MasujinLaboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana, USA Influenza and Prion Disease Research Center, National Institute of Animal Health, National Agriculture and Food Research Organization, Tsukuba, Japan.
Christina D OrrúLaboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana, USA.
Kohtaro MiyazawaInfluenza and Prion Disease Research Center, National Institute of Animal Health, National Agriculture and Food Research Organization, Tsukuba, Japan.
Bradley R GrovemanLaboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana, USA.
Lynne D RaymondLaboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana, USA.
Andrew G HughsonLaboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana, USA.
Byron CaugheyLaboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana, USA bcaughey@nih.gov.
National Institute of Allergy and Infectious Diseases · USNational Institutes of Health · USNational Institute of Animal Health · JP

Funding

Detection of PrionsZIAAI001086 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI CAUGHEY, BYRON · 2009 to 2025
$18.1M
Intramural NIH HHS
6 · The paper itself

Abstract

Prion diseases of cattle include the classical bovine spongiform encephalopathy (C-BSE) and the atypical H-type BSE (H-BSE) and L-type BSE (L-BSE) strains. Although the C- and L-BSE strains can be detected and discriminated by ultrasensitive real-time quaking-induced conversion (RT-QuIC) assays, no such test has yet been described for the detection of H-BSE or the discrimination of each of the major bovine prion strains. Here, we demonstrate an RT-QuIC assay for H-BSE that can detect as little as 10(-9) dilutions of brain tissue and neat cerebrospinal fluid samples from clinically affected cattle. Moreover, comparisons of the reactivities with different recombinant prion protein substrates and/or immunoblot band profiles of proteinase K-treated RT-QuIC reaction products indicated that H-, L-, and C-BSE have distinctive prion seeding activities and can be discriminated by RT-QuIC on this basis.

Indexed as

AnimalsCattleEncephalopathy, Bovine SpongiformImmunoblottingPrion ProteinsRecombinant ProteinsPrion ProteinsRecombinant Proteins

Identifiers

PMID26739160
PMCPMC4768002
OpenAlexW2281681714

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.