Evidence map›Paper›PMID 24608105›Full record

ArticlePloS one2014

Prion protein-specific antibodies that detect multiple TSE agents with high sensitivity.

Sandra McCutcheon, Jan P M Langeveld, Boon Chin Tan, Andrew C Gill, Christopher de Wolf, Stuart Martin, Lorenzo Gonzalez, James Alibhai, A Richard Alejo Blanco, Lauren Campbell and 2 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

13 citing papers in PubMed, 27 citations in OpenAlex.

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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

12 authors at 3 institutions in 2 countries.

Sandra McCutcheonNeurobiology Division, The Roslin Institute and Royal (Dick) School of Veterinary Sciences, Easter Bush, Edinburgh, Scotland, United Kingdom.
Jan P M LangeveldCentral Veterinary Institute of Wageningen UR, Lelystad, The Netherlands.
Boon Chin TanNeurobiology Division, The Roslin Institute and Royal (Dick) School of Veterinary Sciences, Easter Bush, Edinburgh, Scotland, United Kingdom.
Andrew C GillNeurobiology Division, The Roslin Institute and Royal (Dick) School of Veterinary Sciences, Easter Bush, Edinburgh, Scotland, United Kingdom.
Christopher de WolfNeurobiology Division, The Roslin Institute and Royal (Dick) School of Veterinary Sciences, Easter Bush, Edinburgh, Scotland, United Kingdom.
Stuart MartinAnimal Health and Veterinary Laboratories Agency, Lasswade Laboratory, Edinburgh, Scotland, United Kingdom.
Lorenzo GonzalezAnimal Health and Veterinary Laboratories Agency, Lasswade Laboratory, Edinburgh, Scotland, United Kingdom.
James AlibhaiNeurobiology Division, The Roslin Institute and Royal (Dick) School of Veterinary Sciences, Easter Bush, Edinburgh, Scotland, United Kingdom.
A Richard Alejo BlancoNeurobiology Division, The Roslin Institute and Royal (Dick) School of Veterinary Sciences, Easter Bush, Edinburgh, Scotland, United Kingdom.
Lauren CampbellNeurobiology Division, The Roslin Institute and Royal (Dick) School of Veterinary Sciences, Easter Bush, Edinburgh, Scotland, United Kingdom.
Nora HunterNeurobiology Division, The Roslin Institute and Royal (Dick) School of Veterinary Sciences, Easter Bush, Edinburgh, Scotland, United Kingdom.
E Fiona HoustonNeurobiology Division, The Roslin Institute and Royal (Dick) School of Veterinary Sciences, Easter Bush, Edinburgh, Scotland, United Kingdom.
Roslin Institute · GBAnimal and Plant Health Agency · GBWageningen University & Research · NL

Funding

Biotechnology and Biological Sciences Research Council 201/BS3 09722Biotechnology and Biological Sciences Research Council BBS/E/D/20251967Biotechnology and Biological Sciences Research Council BBS/E/D/20251968
6 · The paper itself

Abstract

This paper describes the generation, characterisation and potential applications of a panel of novel anti-prion protein monoclonal antibodies (mAbs). The mAbs were generated by immunising PRNP null mice, using a variety of regimes, with a truncated form of recombinant ovine prion protein spanning residues 94-233. Epitopes of specific antibodies were mapped using solid-phase Pepscan analysis and clustered to four distinct regions within the PrP molecule. We have demonstrated the utility of these antibodies by use of Western blotting and immunohistochemistry in tissues from a range of different species affected by transmissible spongiform encephalopathy (TSE). In comparative tests against extensively-used and widely-published, commercially available antibodies, similar or improved results can be obtained using these new mAbs, specifically in terms of sensitivity of detection. Since many of these antibodies recognise native PrPC, they could also be applied to a broad range of immunoassays such as flow cytometry, DELFIA analysis or immunoprecipitation. We are using these reagents to increase our understanding of TSE pathogenesis and for use in potential diagnostic screening assays.

Indexed as

Amino Acid SequenceAnimalsAntibodies, MonoclonalAntibody SpecificityArginineBinding SitesCodonImmunoglobulin IsotypesImmunohistochemistryMiceMolecular Sequence DataPrion DiseasesPrionsProtein BindingProtein KinasesPrPSc ProteinsAntibodies, MonoclonalArginineCodonImmunoglobulin IsotypesPrionsProtein KinasesPrPSc ProteinsRecombinant Proteins

Identifiers

PMID24608105
PMCPMC3946747
OpenAlexW2143291306

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.