Evidence map›Paper›PMID 28128281›Full record

ArticleScientific reports2017

Targeted delivery of an ADP-ribosylating bacterial toxin into cancer cells.

N-I Zahaf, A E Lang, L Kaiser, C D Fichter, S Lassmann, A McCluskey, A Augspach, K Aktories, G Schmidt

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. 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
1.5field-weighted citation impact, top 20% 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, 27 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Evaluating TcAs for Use in Biotechnology Applications.Biotech (Basel (Switzerland)) · 2025
    Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. International journal of molecular sciences · 2020
    Article
  14. Targeted Delivery ofFrontiers in pharmacology · 2020
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. 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

9 authors at 3 institutions in 2 countries.

N-I ZahafInstitute for Experimental and Clinical Pharmacology and Toxicology, University of Freiburg, Albertstr. 25, 79104 Freiburg, Germany.
A E LangInstitute for Experimental and Clinical Pharmacology and Toxicology, University of Freiburg, Albertstr. 25, 79104 Freiburg, Germany.
L KaiserInstitute for Experimental and Clinical Pharmacology and Toxicology, University of Freiburg, Albertstr. 25, 79104 Freiburg, Germany.
C D FichterInstitute of Surgical Pathology, Medical Center - University of Freiburg, Breisacherstr. 115a, 79106 Freiburg, Germany.
S LassmannInstitute of Surgical Pathology, Medical Center - University of Freiburg, Breisacherstr. 115a, 79106 Freiburg, Germany.
A McCluskeyDepartment of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA02115, USA.
A AugspachInstitute for Experimental and Clinical Pharmacology and Toxicology, University of Freiburg, Albertstr. 25, 79104 Freiburg, Germany.
K AktoriesInstitute for Experimental and Clinical Pharmacology and Toxicology, University of Freiburg, Albertstr. 25, 79104 Freiburg, Germany.
G SchmidtInstitute for Experimental and Clinical Pharmacology and Toxicology, University of Freiburg, Albertstr. 25, 79104 Freiburg, Germany.
University of Freiburg · DEHarvard University · USUniversity Medical Center Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The actin cytoskeleton is an attractive target for bacterial toxins. The ADP-ribosyltransferase TccC3 from the insect bacterial pathogen Photorhabdus luminescence modifies actin to force its aggregation. We intended to transport the catalytic part of this toxin preferentially into cancer cells using a toxin transporter (Protective antigen, PA) which was redirected to Epidermal Growth Factor Receptors (EGFR) or to human EGF receptors 2 (HER2), which are overexpressed in several cancer cells. Protective antigen of anthrax toxin forms a pore through which the two catalytic parts (lethal factor and edema factor) or other proteins can be transported into mammalian cells. Here, we used PA as a double mutant (N682A, D683A; mPA) which cannot bind to the two natural anthrax receptors. Each mutated monomer is fused either to EGF or to an affibody directed against the human EGF receptor 2 (HER2). We established a cellular model system composed of two cell lines representing HER2 overexpressing esophageal adenocarcinomas (EACs) and EGFR overexpressing esophageal squamous cell carcinomas (ESCCs). We studied the specificity and efficiency of the re-directed anthrax pore for transport of TccC3 toxin and established Photorhabdus luminescence TccC3 as a toxin suitable for the development of a targeted toxin selectively killing cancer cells.

Indexed as

Actin CytoskeletonADP Ribose TransferasesADP-RibosylationAntigens, BacterialBacterial ToxinsCarcinoma, Squamous CellCell Line, TumorErb-b2 Receptor Tyrosine KinasesErbB ReceptorsEsophageal NeoplasmsEsophageal Squamous Cell CarcinomaGene Expression RegulationHumansPhotorhabdusADP Ribose Transferasesanthrax toxinAntigens, BacterialBacterial ToxinsEGFR protein, humanERBB2 protein, humanErb-b2 Receptor Tyrosine KinasesErbB Receptors

Identifiers

PMID28128281
PMCPMC5269596
OpenAlexW2583072273

What OpenQuestion holds

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Registered trials

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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.