Evidence map›Paper›PMID 33345717›Full record

ArticlePrion2020

Involvement of N- and C-terminal region of recombinant cervid prion protein in its reactivity to CWD and atypical BSE prions in real-time quaking-induced conversion reaction in the presence of high concentrations of tissue homogenates.

Akio Suzuki, Kazuhei Sawada, Takeshi Yamasaki, Nathaniel D Denkers, Candace K Mathiason, Edward A Hoover, Motohiro Horiuchi

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Prion, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 45% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
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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 2 institutions in 2 countries.

Akio SuzukiLaboratory of Veterinary Hygiene, Graduate School of Infectious Diseases, Hokkaido University , Kita-ku, Sapporo, Japan.
Kazuhei SawadaLaboratory of Veterinary Hygiene, Graduate School of Infectious Diseases, Hokkaido University , Kita-ku, Sapporo, Japan.
Takeshi YamasakiLaboratory of Veterinary Hygiene, Graduate School of Infectious Diseases, Hokkaido University , Kita-ku, Sapporo, Japan.
Nathaniel D DenkersPrion Research Center, Department of Microbiology, Immunology, and Pathology, College of Veterinary Medicine and Biomedical Sciences, Colorado State University , Fort Collins, Colorado, USA.
Candace K MathiasonPrion Research Center, Department of Microbiology, Immunology, and Pathology, College of Veterinary Medicine and Biomedical Sciences, Colorado State University , Fort Collins, Colorado, USA.
Edward A HooverPrion Research Center, Department of Microbiology, Immunology, and Pathology, College of Veterinary Medicine and Biomedical Sciences, Colorado State University , Fort Collins, Colorado, USA.
Motohiro HoriuchiLaboratory of Veterinary Hygiene, Graduate School of Infectious Diseases, Hokkaido University , Kita-ku, Sapporo, Japan.
Hokkaido University · JPColorado State University · US

Funding

Transmission and Pathogenesis of Chronic Wasting Disease (CWD)R01NS061902 · NINDS · COLORADO STATE UNIVERSITY · PI MATHIASON, CANDACE K. · 2009 to 2022
$5.3M
Detection and Characterization of Blood-borne PrionsR01AI112956 · NIAID · COLORADO STATE UNIVERSITY · PI MATHIASON, CANDACE K. · 2014 to 2024
$4.6M
NIAID NIH HHS R01 AI112956NINDS NIH HHS R01 NS061902
6 · The paper itself

Abstract

The real-time quaking-induced conversion (RT-QuIC) reaction is a sensitive and specific method for detecting prions. However, inhibitory factors present in tissue homogenates can easily interfere with this reaction. To identify the RT-QuIC condition under which low levels of chronic wasting disease (CWD) and bovine spongiform encephalopathy (BSE) prions can be detected in the presence of high concentrations of brain tissue homogenates, reactivities of various recombinant prion proteins (rPrPs) were tested. Among the tested rPrPs, recombinant cervid PrP (rCerPrP) showed a unique reactivity: the reactivity of rCerPrP to CWD and atypical BSE prions was not highly affected by high concentrations of normal brain homogenates. The unique reactivity of rCerPrP disappeared when the N-terminal region (aa 25-93) was truncated. Replacement of aa 23-149 of mouse (Mo) PrP with the corresponding region of CerPrP partially restored the unique reactivity of rCerPrP in RT-QuIC. Replacement of the extreme C-terminal region of MoPrP aa 219-231 to the corresponding region of CerPrP partially conferred the unique reactivity of rCerPrP to rMoPrP, suggesting the involvement of both N- and C-terminal regions. Additionally, rCer

Indexed as

Amino AcidsAnimalsBrainCattleDeerEncephalopathy, Bovine SpongiformModels, BiologicalPrion ProteinsRecombinant ProteinsWasting Disease, ChronicAmino AcidsPrion ProteinsRecombinant Proteinsbovine spongiform encephalopathycervid prion proteinchronic wasting diseaseprionreal-time quaking-induced conversion

Identifiers

PMID33345717
PMCPMC7757825
OpenAlexW3117833330

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.