Evidence map›Paper›PMID 27440899›Full record

ArticleJournal of virology2016

Guinea Pig Prion Protein Supports Rapid Propagation of Bovine Spongiform Encephalopathy and Variant Creutzfeldt-Jakob Disease Prions.

Joel C Watts, Kurt Giles, Daniel J Saltzberg, Brittany N Dugger, Smita Patel, Abby Oehler, Sumita Bhardwaj, Andrej Sali, Stanley B Prusiner

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

Article in Journal of virology, 2016. 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
0.2field-weighted citation impact, top 35% 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
  2. Article
  3. Prion Strains and Transmission Barrier Phenomena.Pathogens (Basel, Switzerland) · 2018
    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

9 authors at 2 institutions in 1 country.

Joel C WattsInstitute for Neurodegenerative Diseases, University of California, San Francisco, San Francisco, California, USA Department of Neurology, University of California, San Francisco, San Francisco, California, USA.
Kurt GilesInstitute for Neurodegenerative Diseases, University of California, San Francisco, San Francisco, California, USA Department of Neurology, University of California, San Francisco, San Francisco, California, USA.
Daniel J SaltzbergCalifornia Institute for Quantitative Biosciences (QB3), University of California, San Francisco, San Francisco, California, USA.
Brittany N DuggerInstitute for Neurodegenerative Diseases, University of California, San Francisco, San Francisco, California, USA Department of Neurology, University of California, San Francisco, San Francisco, California, USA.
Smita PatelInstitute for Neurodegenerative Diseases, University of California, San Francisco, San Francisco, California, USA.
Abby OehlerInstitute for Neurodegenerative Diseases, University of California, San Francisco, San Francisco, California, USA.
Sumita BhardwajInstitute for Neurodegenerative Diseases, University of California, San Francisco, San Francisco, California, USA.
Andrej SaliCalifornia Institute for Quantitative Biosciences (QB3), University of California, San Francisco, San Francisco, California, USA Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, San Francisco, California, USA Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, California, USA.
Stanley B PrusinerInstitute for Neurodegenerative Diseases, University of California, San Francisco, San Francisco, California, USA Department of Neurology, University of California, San Francisco, San Francisco, California, USA Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, California, USA stanley.prusiner@ucsf.edu.
University of California, San Francisco · USInstitute for Neurodegenerative Disorders · US

Funding

VIRAL DEGENERATIVE DEMENTING DISEASE IN AGING (SUPP)P01AG002132 · NIA · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI PRUSINER, STANLEY B · 1985 to 2024
$51.7M
UNDERSTANDING AND IMPROVING SMALL MOLECULE INHIBITORS OF PRION REPLICATIONP01AG021601 · NIA · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI PRUSINER, STANLEY B · 2003 to 2013
$31.9M
SYNTHETIC AND RECOMBINANT PRP PEPTIDES AND PROTEINSP01AG010770 · NIA · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI PRUSINER, STANLEY B · 1993 to 2015
$30.3M
Towards Therapeutics for Neurodegenerative DiseasesR37AG031220 · NIA · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI PRUSINER, STANLEY B · 2008 to 2017
$6.2M
Delineating conformational variants of the Abeta peptideK99AG042453 · NIA · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WATTS, JOEL · 2012 to 2013
$180k
NIA NIH HHS K99 AG042453NIA NIH HHS P01 AG002132NIA NIH HHS P01 AG010770NIA NIH HHS P01 AG021601NIA NIH HHS R37 AG031220
6 · The paper itself

Abstract

The biochemical and neuropathological properties of bovine spongiform encephalopathy (BSE) and variant Creutzfeldt-Jakob disease (vCJD) prions are faithfully maintained upon transmission to guinea pigs. However, primary and secondary transmissions of BSE and vCJD in guinea pigs result in long incubation periods of ∼450 and ∼350 days, respectively. To determine if the incubation periods of BSE and vCJD prions could be shortened, we generated transgenic (Tg) mice expressing guinea pig prion protein (GPPrP). Inoculation of Tg(GPPrP) mice with BSE and vCJD prions resulted in mean incubation periods of 210 and 199 days, respectively, which shortened to 137 and 122 days upon serial transmission. In contrast, three different isolates of sporadic CJD prions failed to transmit disease to Tg(GPPrP) mice. Many of the strain-specified biochemical and neuropathological properties of BSE and vCJD prions, including the presence of type 2 protease-resistant PrP IMPORTANCE: Variant Creutzfeldt-Jakob disease (vCJD) and bovine spongiform encephalopathy (BSE) prions are two of the prion strains most relevant to human health. However, propagating these strains in mice expressing human or bovine prion protein has been difficult because of prolonged incubation periods or inefficient transmission. Here, we show that transgenic mice expressing guinea pig prion protein are fully susceptible to vCJD and BSE prions but not to sporadic CJD prions. Our results suggest that the guinea pig prion protein is a better, more rapid substrate than either bovine or human prion protein for propagating BSE and vCJD prions.

Indexed as

AnimalsBrainCattleCreutzfeldt-Jakob SyndromeEncephalopathy, Bovine SpongiformGuinea PigsHumansMiceMice, TransgenicPrion ProteinsPrionsPrion ProteinsPrions

Identifiers

PMID27440899
PMCPMC5068510
OpenAlexW2481375805

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.