Evidence map›Paper›PMID 16938891›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Polyvalent inhibitors of anthrax toxin that target host receptors.

Saleem Basha, Prakash Rai, Vincent Poon, Arundhati Saraph, Kunal Gujraty, Mandy Y Go, Skanda Sadacharan, Mia Frost, Jeremy Mogridge, Ravi S Kane

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

37 citing papers in PubMed, 77 citations in OpenAlex.

  1. Review
  2. Review
  3. Inhibition of anthrax lethal factor by ssDNA aptamers.Archives of biochemistry and biophysics · 2018
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Inhibitors of the Metalloproteinase Anthrax Lethal Factor.Current topics in medicinal chemistry · 2016
    Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Designing inhibitors of anthrax toxin.Expert opinion on drug discovery · 2014
    Review
  15. Molecular determinants for a cardiovascular collapse in anthrax.Frontiers in bioscience (Elite edition) · 2014
    Review
  16. Review
  17. Review
  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

10 authors at 4 institutions in 2 countries.

Saleem BashaThe Howard P. Isermann Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, 110 Eighth Street, Troy, NY 12180, USA.
Prakash Rai
Vincent Poon
Arundhati Saraph
Kunal Gujraty
Mandy Y Go
Skanda Sadacharan
Mia Frost
Jeremy Mogridge
Ravi S Kane
University of Toronto · CARensselaer Polytechnic Institute · USHarvard University · USCanada Research Chairs · CA

Funding

The Design of Inhibitors of Anthrax ToxinR21AI053506 · NIAID · RENSSELAER POLYTECHNIC INSTITUTE · PI KANE, RAVI S · 2003 to 2004
$507k
NIAID NIH HHS R21 AI053506
6 · The paper itself

Abstract

Resistance of pathogens to antimicrobial therapeutics has become a widespread problem. Resistance can emerge naturally, but it can also be engineered intentionally, which is an important consideration in designing therapeutics for bioterrorism agents. Blocking host receptors used by pathogens represents a powerful strategy to overcome this problem, because extensive alterations to the pathogen may be required to enable it to switch to a new receptor that can still support pathogenesis. Here, we demonstrate a facile method for producing potent receptor-directed antitoxins. We used phage display to identify a peptide that binds both anthrax-toxin receptors and attached this peptide to a synthetic scaffold. Polyvalency increased the potency of these peptides by >50,000-fold in vitro and enabled the neutralization of anthrax toxin in vivo. This work demonstrates a receptor-directed anthrax-toxin inhibitor and represents a promising strategy to combat a variety of viral and bacterial diseases.

Indexed as

AcetylationAnimalsAnthraxAntigens, BacterialBacillus anthracisBacterial ToxinsCell LineCHO CellsCricetinaeFluoresceinFluorescent DyesInhibitory Concentration 50LiposomesMacrophagesMicePeptide Libraryanthrax toxinanthrax toxin receptorsAntigens, BacterialBacterial ToxinsFluoresceinFluorescent DyesLiposomesPeptide LibraryPeptidesReceptors, Peptide

Identifiers

PMID16938891
PMCPMC1569193
OpenAlexW2037004316

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.