Evidence map›Paper›PMID 27043629›Full record

ArticleToxins2016

EGA Protects Mammalian Cells from Clostridium difficile CDT, Clostridium perfringens Iota Toxin and Clostridium botulinum C2 Toxin.

Leonie Schnell, Ann-Katrin Mittler, Mirko Sadi, Michel R Popoff, Carsten Schwan, Klaus Aktories, Andrea Mattarei, Domenico Azarnia Tehran, Cesare Montecucco, Holger Barth

Open access · goldAbstract read
In one paragraph

Article in Toxins, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

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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

10 authors at 4 institutions in 3 countries.

Leonie SchnellInstitute of Pharmacology and Toxicology, University of Ulm Medical Center, Albert-Einstein-Allee 11, 89081 Ulm, Germany. leonie.schnell@uni-ulm.de.
Ann-Katrin MittlerInstitute of Pharmacology and Toxicology, University of Ulm Medical Center, Albert-Einstein-Allee 11, 89081 Ulm, Germany. ann-katrin.mittler@uni-ulm.de.
Mirko SadiInstitute of Pharmacology and Toxicology, University of Ulm Medical Center, Albert-Einstein-Allee 11, 89081 Ulm, Germany. mirko.sadi@uni-ulm.de.
Michel R PopoffDepartment of Anaerobic Bacteria, Pasteur Institute, 75015 Paris, France. michel-robert.popoff@pasteur.fr.
Carsten SchwanInstitute of Experimental and Clinical Pharmacology and Toxicology, University of Freiburg, 79104 Freiburg, Germany. carsten.schwan@pharmakol.uni-freiburg.de.
Klaus AktoriesInstitute of Experimental and Clinical Pharmacology and Toxicology, University of Freiburg, 79104 Freiburg, Germany. klaus.aktories@pharmakol.uni-freiburg.de.
Andrea MattareiDepartment of Chemical Sciences, University of Padova, 35121 Padova, Italy. andrea.mattarei@unipd.it.
Domenico Azarnia TehranDepartment of Biomedical Sciences, University of Padova, 35121 Padova, Italy. doazte@gmail.com.
Cesare MontecuccoDepartment of Biomedical Sciences, University of Padova, 35121 Padova, Italy. cesare.montecucco@gmail.com.
Holger BarthInstitute of Pharmacology and Toxicology, University of Ulm Medical Center, Albert-Einstein-Allee 11, 89081 Ulm, Germany. holger.barth@uni-ulm.de.
Universität Ulm · DEUniversity of Padua · ITUniversity of Freiburg · DEInstitut Pasteur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The pathogenic bacteria Clostridium difficile, Clostridium perfringens and Clostridium botulinum produce the binary actin ADP-ribosylating toxins CDT, iota and C2, respectively. These toxins are composed of a transport component (B) and a separate enzyme component (A). When both components assemble on the surface of mammalian target cells, the B components mediate the entry of the A components via endosomes into the cytosol. Here, the A components ADP-ribosylate G-actin, resulting in depolymerization of F-actin, cell-rounding and eventually death. In the present study, we demonstrate that 4-bromobenzaldehyde N-(2,6-dimethylphenyl)semicarbazone (EGA), a compound that protects cells from multiple toxins and viruses, also protects different mammalian epithelial cells from all three binary actin ADP-ribosylating toxins. In contrast, EGA did not inhibit the intoxication of cells with Clostridium difficile toxins A and B, indicating a possible different entry route for this toxin. EGA does not affect either the binding of the C2 toxin to the cells surface or the enzyme activity of the A components of CDT, iota and C2, suggesting that this compound interferes with cellular uptake of the toxins. Moreover, for C2 toxin, we demonstrated that EGA inhibits the pH-dependent transport of the A component across cell membranes. EGA is not cytotoxic, and therefore, we propose it as a lead compound for the development of novel pharmacological inhibitors against clostridial binary actin ADP-ribosylating toxins.

Indexed as

ActinsAdenosine Diphosphate RiboseADP Ribose TransferasesAnimalsBacterial ProteinsBacterial ToxinsBotulinum ToxinsCell MembraneChlorocebus aethiopsHeLa CellsHumansProtein TransportSemicarbazonesVero CellsActinsactin-specific ADP-ribosyltransferase, ClostridiumAdenosine Diphosphate RiboseADP Ribose TransferasesBacterial ProteinsBacterial ToxinsBotulinum Toxinsbotulinum toxin type Ciota toxin, Clostridium perfringensSemicarbazonesbinary toxinClostridium botulinum C2 toxinClostridium difficile CDTClostridium perfringens iota toxinEGA

Identifiers

PMID27043629
PMCPMC4848627
OpenAlexW2315840978

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.