Evidence map›Paper›PMID 21345946›Full record

ArticleJournal of virology2011

Biological effects and use of PrPSc- and PrP-specific antibodies generated by immunization with purified full-length native mouse prions.

Benjamin Petsch, Andreas Müller-Schiffmann, Anna Lehle, Elizabeta Zirdum, Ingrid Prikulis, Franziska Kuhn, Alex J Raeber, James W Ironside, Carsten Korth, Lothar Stitz

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

20 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Immunotherapy against Prion Disease.Pathogens (Basel, Switzerland) · 2020
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. The immunobiology of prion diseases.Nature reviews. Immunology · 2013
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Could immunomodulation be used to prevent prion diseases?Expert review of anti-infective therapy · 2012
    Article
  20. 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

10 authors at 3 institutions in 3 countries.

Benjamin PetschFriedrich-Loeffler-Institut, Institute of Immunology, Tuebingen, Germany. benjamin.petsch@fli.bund.de
Andreas Müller-Schiffmann
Anna Lehle
Elizabeta Zirdum
Ingrid Prikulis
Franziska Kuhn
Alex J Raeber
James W Ironside
Carsten Korth
Lothar Stitz
Friedrich-Loeffler-Institut · DEHeinrich Heine University Düsseldorf · DEUniversity of Edinburgh · GB

Funding

Medical Research Council G0600953Medical Research Council G0900580
6 · The paper itself

Abstract

The prion agent is the infectious particle causing spongiform encephalopathies in animals and humans and is thought to consist of an altered conformation (PrP(Sc)) of the normal and ubiquitous prion protein PrP(C). The interaction of the prion agent with the immune system, particularly the humoral immune response, has remained unresolved. Here we investigated the immunogenicity of full-length native and infectious prions, as well as the specific biological effects of the resulting monoclonal antibodies (MAbs) on the binding and clearance of prions in cell culture and in in vivo therapy. Immunization of prion knockout (Prnp(0/0)) mice with phosphotungstic acid-purified mouse prions resulted in PrP-specific monoclonal antibodies with binding specificities selective for PrP(Sc) or for both PrP(C) and PrP(Sc). PrP(Sc)-specific MAb W261, of the IgG1 isotype, reacted with prions from mice, sheep with scrapie, deer with chronic wasting disease (CWD), and humans with sporadic and variant Creutzfeldt-Jakob disease (CJD) in assays including a capture enzyme-linked immunosorbent assay (ELISA) system. This PrP(Sc)-specific antibody was unable to clear prions from mouse neuroblastoma cells (ScN2a) permanently infected with scrapie, whereas the high-affinity MAb W226, recognizing both isoforms, PrP(Sc) and PrP(C), did clear prions from ScN2a cells, as determined by a bioassay. However, an attempt to treat intraperitoneally prion infected mice with full-length W226 or with a recombinant variable-chain fragment (scFv) from W226 could only slightly delay the incubation time. We conclude that (i) native, full-length PrP(Sc) elicits a prion-specific antibody response in PrP knockout mice, (ii) a PrP(Sc)-specific antibody had no prion-clearing effect, and (iii) even a high-affinity MAb that clears prions in vitro (W226) may not necessarily protect against prion infection, contrary to previous reports using different antibodies.

Indexed as

AnimalsAntibodies, MonoclonalCell LineInfectious Disease Incubation PeriodMiceMice, Inbred BALB CMice, KnockoutPrion DiseasesPrion ProteinsPrionsProtein BindingTime FactorsAntibodies, MonoclonalPrion ProteinsPrionsPrnp protein, mouse

Identifiers

PMID21345946
PMCPMC3126253
OpenAlexW2166560871

What OpenQuestion holds

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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.