Evidence map›Paper›PMID 22174672›Full record

ArticlePLoS pathogens2011

A receptor-based switch that regulates anthrax toxin pore formation.

Rosemarie M Pilpa, Monika Bayrhuber, John M Marlett, Roland Riek, John A T Young

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
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  13. Designing inhibitors of anthrax toxin.Expert opinion on drug discovery · 2014
    Review
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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

5 authors at 2 institutions in 2 countries.

Rosemarie M PilpaNomis Center for Immunobiology and Microbial Pathogenesis, The Salk Institute for Biological Studies, La Jolla, California, United States of America.
Monika Bayrhuber
John M Marlett
Roland Riek
John A T Young
Salk Institute for Biological Studies · USETH Zurich · CH

Funding

Receptor Decoy Inhibitor of Anthrax ToxinR01AI076852 · NIAID · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI MANCHESTER, MARIANNE, YOUNG, JOHN A T · 2008 to 2012
$2.4M
The structure, dynamics and function of the pore-forming toxin of AnthraxF32AI082935 · NIAID · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI PILPA, ROSEMARIE MELITON · 2009 to 2011
$144k
NIAID NIH HHS AI076852NIAID NIH HHS AI082935-03NIAID NIH HHS F32 AI082935NIAID NIH HHS R01 AI076852
6 · The paper itself

Abstract

Cellular receptors can act as molecular switches, regulating the sensitivity of microbial proteins to conformational changes that promote cellular entry. The activities of these receptor-based switches are only partially understood. In this paper, we sought to understand the mechanism that underlies the activity of the ANTXR2 anthrax toxin receptor-based switch that binds to domains 2 and 4 of the protective antigen (PA) toxin subunit. Receptor-binding restricts structural changes within the heptameric PA prepore that are required for pore conversion to an acidic endosomal compartment. The transfer cross-saturation (TCS) NMR approach was used to monitor changes in the heptameric PA-receptor contacts at different steps during prepore-to-pore conversion. These studies demonstrated that receptor contact with PA domain 2 is weakened prior to pore conversion, defining a novel intermediate in this pathway. Importantly, ANTXR2 remained bound to PA domain 4 following pore conversion, suggesting that the bound receptor might influence the structure and/or function of the newly formed pore. These studies provide new insights into the function of a receptor-based molecular switch that controls anthrax toxin entry into cells.

Indexed as

AnthraxAntigens, BacterialBacillus anthracisBacterial ToxinsMagnetic Resonance SpectroscopyProtein Structure, TertiaryReceptors, PeptideVirulenceanthrax toxinanthrax toxin receptorsAntigens, BacterialBacterial ToxinsReceptors, Peptide

Identifiers

PMID22174672
PMCPMC3234216
OpenAlexW2087312811

What OpenQuestion holds

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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.