Evidence map›Paper›PMID 22807452›Full record

ArticleThe Journal of biological chemistry2012

Stabilization of a prion strain of synthetic origin requires multiple serial passages.

Natallia Makarava, Gabor G Kovacs, Regina Savtchenko, Irina Alexeeva, Herbert Budka, Robert G Rohwer, Ilia V Baskakov

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

48 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
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  14. Review
  15. Article
  16. Cofactor molecules: Essential partners for infectious prions.Progress in molecular biology and translational science · 2020
    Review
  17. Synthetic Prion Selection and Adaptation.Molecular neurobiology · 2019
    Article
  18. Article
  19. Article
  20. Article
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 3 institutions in 2 countries.

Natallia MakaravaCenter for Biomedical Engineering and Technology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Gabor G Kovacs
Regina Savtchenko
Irina Alexeeva
Herbert Budka
Robert G Rohwer
Ilia V Baskakov
University of Maryland, Baltimore · USMedical University of Vienna · ATVA Maryland Health Care System · US

Funding

Self-Propagating Mechanism of Prion DiseasesR01NS045585 · NINDS · UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE · PI Ilia V Baskakov · 2003 to 2026
$9.6M
Elucidating molecular structure of mammalian prionsR01NS074998 · NINDS · UNIVERSITY OF MARYLAND BALTIMORE · PI BASKAKOV, ILIA V · 2012 to 2015
$1.4M
Elucidating molecular structure of mammalian prionsR56NS074998 · NINDS · UNIVERSITY OF MARYLAND BALTIMORE · PI BASKAKOV, ILIA V · 2011 to 2011
$405k
NINDS NIH HHS NS045585NINDS NIH HHS NS074998NINDS NIH HHS R01 NS045585NINDS NIH HHS R01 NS074998NINDS NIH HHS R56 NS074998
6 · The paper itself

Abstract

Transmission of prions to a new host is frequently accompanied by strain adaptation, a phenomenon that involves reduction of the incubation period, a change in neuropathological features and, sometimes, tissue tropism. Here we show that a strain of synthetic origin (SSLOW), although serially transmitted within the same species, displayed the key attributes of the strain adaptation process. At least four serial passages were required to stabilize the strain-specific SSLOW phenotype. The biological titration of SSLOW revealed a correlation between clinical signs and accumulation of PrP(Sc) in brains of animals inoculated with high doses (10(-1)-10(-5) diluted brain material), but dissociation between the two processes at low dose inocula (10(-6)-10(-8) diluted brain material). At low doses, several asymptomatic animals harbored large amounts of PrP(Sc) comparable with those seen in the brains of terminally ill animals, whereas one clinically ill animal had very little, if any, PrP(Sc). In summary, the current study illustrates that the phenomenon of prion strain adaptation is more common than generally thought and could be observed upon serial transmission without changing the host species. When PrP(Sc) is seeded by recombinant PrP structures different from that of authentic PrP(Sc), PrP(Sc) properties continued to evolve for as long as four serial passages.

Indexed as

AnimalsBrainCricetinaePrion DiseasesProtein StabilityPrPSc ProteinsPrPSc Proteins

Identifiers

PMID22807452
PMCPMC3436274
OpenAlexW2022051519

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.