ReviewFEMS microbiology reviews2015
One cannot rule them all: Are bacterial toxins-antitoxins druggable?
Review in FEMS microbiology reviews, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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.
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.
Who cites it
42 citing papers in PubMed, 73 citations in OpenAlex.
- Beyond bactericidal: targeting plasmid-mediated antibiotic resistance with natural product-based plasmid curing agents.Frontiers in microbiology · 2026Review
- Bacterial programmed cell death and toxin-antitoxin system in bacteria.Archives of microbiology · 2025Review
- The Vibrio cholerae CBASS phage defence system modulates resistance and killing by antifolate antibiotics.Nature microbiology · 2024Article
- One Earth: The Equilibrium between the Human and the Bacterial Worlds.International journal of molecular sciences · 2023Review
- Type II bacterial toxin-antitoxins: hypotheses, facts, and the newfound plethora of the PezAT system.FEMS microbiology reviews · 2023Article
- Article
- Discovery of Small-Molecule VapC1 Nuclease Inhibitors by Virtual Screening and Scaffold Hopping from an Atomic Structure Revealing Protein-Protein Interactions with a Native VapB1 Inhibitor.Journal of chemical information and modeling · 2022Article
- MqsR toxin as a biotechnological tool for plant pathogen bacterial control.Scientific reports · 2022Article
- Functional and Structural Diversity of Bacterial Contact-Dependent Growth Inhibition Effectors.Frontiers in molecular biosciences · 2022Review
- Modulators of protein-protein interactions as antimicrobial agents.RSC chemical biology · 2021Review
- Expression of type II toxin-antitoxin systems and ClpP protease of methicillin-resistantIranian journal of microbiology · 2021Article
- Toxin-antitoxin systems and their medical applications: current status and future perspective.Applied microbiology and biotechnology · 2021Review
- Novel Treatments and Preventative Strategies Against Food-Poisoning Caused by Staphylococcal Species.Pathogens (Basel, Switzerland) · 2021Review
- Comparative genome analysis of Salmonella enterica serovar Gallinarum biovars Pullorum and Gallinarum decodes strain specific genes.PloS one · 2021Article
- Depletion of the DarG antitoxin in Mycobacterium tuberculosis triggers the DNA-damage response and leads to cell death.Molecular microbiology · 2020Article
- Review
- Review
- Characterization of a toxin-antitoxin system in Mycobacterium tuberculosis suggests neutralization by phosphorylation as the antitoxicity mechanism.Communications biology · 2020Article
- Towards Exploring Toxin-Antitoxin Systems inInternational journal of molecular sciences · 2019Article
- Microbial ageing and longevity.Nature reviews. Microbiology · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type II (proteic) toxin-antitoxin (TA) operons are widely spread in bacteria and archaea. They are organized as operons in which, usually, the antitoxin gene precedes the cognate toxin gene. The antitoxin generally acts as a transcriptional self-repressor, whereas the toxin acts as a co-repressor, both proteins constituting a harmless complex. When bacteria encounter a stressful environment, TAs are triggered. The antitoxin protein is unstable and will be degraded by host proteases, releasing the free toxin to halt essential processes. The result is a cessation of cell growth or even death. Because of their ubiquity and the essential processes targeted, TAs have been proposed as good candidates for development of novel antimicrobials. We discuss here the possible druggability of TAs as antivirals and antibacterials, with focus on the potentials and the challenges that their use may find in the 'real' world. We present strategies to develop TAs as antibacterials in view of novel technologies, such as the use of very small molecules (fragments) as inhibitors of protein-protein interactions. Appropriate fragments could disrupt the T:A interfaces leading to the release of the targeted TA pair. Possible ways of delivery and formulation of Tas are also discussed.
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What OpenQuestion holds
Registered trials
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.