Evidence map›Paper›PMID 24105336›Full record

ArticleScientific reports2013

Recombinant human prion protein inhibits prion propagation in vitro.

Jue Yuan, Yi-An Zhan, Romany Abskharon, Xiangzhu Xiao, Manuel Camacho Martinez, Xiaochen Zhou, Geoff Kneale, Jacqueline Mikol, Sylvain Lehmann, Witold K Surewicz and 7 more

Abstract read
In one paragraph

Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
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  14. Journal of virology · 2017
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Prions: Beyond a Single Protein.Clinical microbiology reviews · 2016
    Review
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

17 authors.

Jue Yuan1] Department of Pathology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA [2] National Prion Disease Pathology Surveillance Center, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA [3].
Yi-An Zhan
Romany Abskharon
Xiangzhu Xiao
Manuel Camacho Martinez
Xiaochen Zhou
Geoff Kneale
Jacqueline Mikol
Sylvain Lehmann
Witold K Surewicz
Joaquín Castilla
Jan Steyaert
Shulin Zhang
Qingzhong Kong
Robert B Petersen
Alexandre Wohlkonig
Wen-Quan Zou

Funding

Clinical and Translational Science Collaborative of ClevelandUL1TR000439 · NCATS · CASE WESTERN RESERVE UNIVERSITY · PI KONSTAN, MICHAEL W. · 2012 to 2016
$50.0M
TRANSGENIC MODELS OF PRION DISEASES LINKED TO D178N MUTATIONP01AG014359 · NIA · CASE WESTERN RESERVE UNIVERSITY · PI GAMBETTI, PIERLUIGI · 1997 to 2013
$22.2M
Pathogenicity of prion protein aggregates from uninfected cells and brainsR01NS062787 · NINDS · CASE WESTERN RESERVE UNIVERSITY · PI ZOU, WEN-QUAN · 2009 to 2013
$1.4M
Generating iPSC-derived Neurons to Explore Formation & Inhibition of Human PrionsR21NS087588 · NINDS · CASE WESTERN RESERVE UNIVERSITY · PI QI, XIN, TESAR, PAUL JOSEPH · 2014 to 2015
$436k
NCATS NIH HHS UL1 TR000439NIA NIH HHS AG-14359NINDS NIH HHS R01 NS062787NINDS NIH HHS R01NS062787NINDS NIH HHS R21 NS087588PHS HHS UR8/CCU515004
6 · The paper itself

Abstract

Prion diseases are associated with the conformational conversion of the cellular prion protein (PrP(C)) into the pathological scrapie isoform (PrP(Sc)) in the brain. Both the in vivo and in vitro conversion of PrP(C) into PrP(Sc) is significantly inhibited by differences in amino acid sequence between the two molecules. Using protein misfolding cyclic amplification (PMCA), we now report that the recombinant full-length human PrP (rHuPrP23-231) (that is unglycosylated and lacks the glycophosphatidylinositol anchor) is a strong inhibitor of human prion propagation. Furthermore, rHuPrP23-231 also inhibits mouse prion propagation in a scrapie-infected mouse cell line. Notably, it binds to PrP(Sc), but not PrP(C), suggesting that the inhibitory effect of recombinant PrP results from blocking the interaction of brain PrP(C) with PrP(Sc). Our findings suggest a new avenue for treating prion diseases, in which a patient's own unglycosylated and anchorless PrP is used to inhibit PrP(Sc) propagation without inducing immune response side effects.

Indexed as

AnimalsBrainGlycosylationHumansIn Vitro TechniquesMiceNeuroblastomaPrion ProteinsPrionsProtein FoldingPrPC ProteinsPrPSc ProteinsRecombinant ProteinsScrapieSpecies SpecificityPrion ProteinsPrionsPrnp protein, mousePrPC ProteinsPrPSc ProteinsRecombinant Proteins

Identifiers

PMID24105336
PMCPMC3793212

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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.