Evidence map›Paper›PMID 41901786›Full record

ArticlePathogens (Basel, Switzerland)2026

Practical Real-Time Quaking-Induced Conversion for Detecting Classical Bovine Spongiform Encephalopathy and Classical and Atypical Scrapie Prions.

Akio Suzuki, Kazuhei Sawada, Taku Nakashima, Toyotaka Sato, Kohtaro Miyazawa, Yuichi Matsuura, Keigo Ikeda, Yoshifumi Iwamaru, Motohiro Horiuchi

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Pathogens (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

9 authors.

Akio SuzukiLaboratory of Veterinary Hygiene, Faculty of Veterinary Medicine, Graduate School of Infectious Diseases, Hokkaido University, Kita 18, Nishi 9, Kita-ku, Sapporo 060-0818, Hokkaido, Japan.
Kazuhei SawadaLaboratory of Veterinary Hygiene, Faculty of Veterinary Medicine, Graduate School of Infectious Diseases, Hokkaido University, Kita 18, Nishi 9, Kita-ku, Sapporo 060-0818, Hokkaido, Japan.
Taku NakashimaLaboratory of Veterinary Hygiene, Faculty of Veterinary Medicine, Graduate School of Infectious Diseases, Hokkaido University, Kita 18, Nishi 9, Kita-ku, Sapporo 060-0818, Hokkaido, Japan.
Toyotaka SatoLaboratory of Veterinary Hygiene, Faculty of Veterinary Medicine, Graduate School of Infectious Diseases, Hokkaido University, Kita 18, Nishi 9, Kita-ku, Sapporo 060-0818, Hokkaido, Japan.
Kohtaro MiyazawaDivision of Infectious Animal Diseases, National Institute of Animal Health, Kannondai 3-1-5, Tsukuba 305-0856, Ibaraki, Japan.
Yuichi MatsuuraDivision of Infectious Animal Diseases, National Institute of Animal Health, Kannondai 3-1-5, Tsukuba 305-0856, Ibaraki, Japan.ORCID 0000-0003-3383-7918
Keigo IkedaDivision of Infectious Animal Diseases, National Institute of Animal Health, Kannondai 3-1-5, Tsukuba 305-0856, Ibaraki, Japan.
Yoshifumi IwamaruDivision of Infectious Animal Diseases, National Institute of Animal Health, Kannondai 3-1-5, Tsukuba 305-0856, Ibaraki, Japan.ORCID 0000-0003-3459-7872
Motohiro HoriuchiLaboratory of Veterinary Hygiene, Faculty of Veterinary Medicine, Graduate School of Infectious Diseases, Hokkaido University, Kita 18, Nishi 9, Kita-ku, Sapporo 060-0818, Hokkaido, Japan.

Funding

Ministry of Education, Culture, Sports, Science, and Technology, Japan Grant-in-Aid for Science Research (B) 25K02167Ministry of Education, Culture, Sports, Science, and Technology, Japan World-leading Innovative and Smart Education Program (1801)Ministry of Health, Labour and Welfare of Japan 23KA1004
6 · The paper itself

Abstract

Real-time quaking-induced conversion (RT-QuIC) is highly sensitive for prion detection; however, inhibitory factors present in tissue homogenates readily interfere with the assay. We previously reported that recombinant cervid prion protein (rCerPrP) enabled the establishment of practical RT-QuIC for detecting chronic wasting disease and atypical bovine spongiform encephalopathy (BSE) prions, i.e., detecting low levels of prions in high concentration of brain tissue homogenates. Accordingly, the present study aimed to establish RT-QuIC for detecting classical BSE (C-BSE) and classical and atypical scrapie (C- and A-scrapie, respectively). A single-step lipid extraction using a 3:1 mixture of 2-butanol and methanol was effective as a pretreatment to remove inhibitors from brain homogenates. Among three rPrPs extensively evaluated, recombinant sheep PrP (rShPrP) was the most suitable substrate for practical detection of C-BSE prions. rCerPrP-173S/177N and rCerPrP-98S/173S/177N, which carry sheep-type amino acid substations at codons 173 and 177 and at codons 98, 173, and 177, showed excellent performance for detecting C-scrapie prions. Moreover, rCerPrP-98S/173S/177N, but not rCerPrP-173S/177N, was identified as an optimal substrate for detecting A-scrapie prions. These results suggested that combining inhibitor-removal pretreatment with the optimization of rPrP substrate for each animal prions further enhanced of RT-QuIC performance.

Indexed as

Encephalopathy, Bovine SpongiformPrionsScrapieAnimalsBrainCattleRecombinant ProteinsSheepPrionsRecombinant Proteins2-butanol/methanolC-BSElipid extractionprionRT-QuICscrapietransmissible spongiform encephalopathy

Identifiers

PMID41901786
PMCPMC13028819

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.