ReviewmBio2015
New players in the toxin field: polymorphic toxin systems in bacteria.
Review in mBio, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 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
105 citing papers in PubMed, 159 citations in OpenAlex.
- Modular Platform for Recombinant Production of Highly Toxic Bacterial Proteins.Microbial biotechnology · 2026Article
- Article
- Characterization of Two Rhs-Family Nuclease Toxins, YPO3609 and YPO3615, inMicroorganisms · 2026Article
- Global identification of Chromobacterium violaceum T6SS effectors reveals an Rhs antibacterial toxin featuring FIX and ADP-ribosyltransferase domains.The Journal of biological chemistry · 2026Article
- Comparative genomic analysis of clinically relevant human skin-associated fungi.Nature communications · 2026Article
- Single-cell sequencing reveals unexpected genetic diversity amongMicrobial genomics · 2026Article
- Ancestral neuronal receptors are bacterial accessory toxins.Nature communications · 2026Article
- A toxic effector of T7SS facilitates bacterial competition and virulence through membrane damage in Streptococcus suis.Veterinary research · 2026Article
- The yxiD gene from Bacillus subtilis 6633 encodes a polymorphic toxin with tRNase activity and is neutralized by the cognate immunity protein YxxD.Nucleic acids research · 2025Article
- Genetic Diversity ofPathogens (Basel, Switzerland) · 2025Article
- Bacterial warfare is associated with virulence and antimicrobial resistance.Nature communications · 2025Article
- Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2025Review
- Global biogeography and projection of antimicrobial toxin genes.Microbiome · 2025Article
- Article
- Identifying a type of toxic effectors exported by the type VII secretion system to enhance competitive fitness inFrontiers in cellular and infection microbiology · 2025Article
- The type II secretion system as an underappreciated and understudied mediator of interbacterial antagonism.Infection and immunity · 2024Review
- Pangenome Analysis Reveals Novel Contact-Dependent Growth Inhibition System and Phenazine Biosynthesis Operons inMicroorganisms · 2024Article
- Article
- Article
- A toolbox for genetic manipulation in intestinalSynthetic and systems biotechnology · 2024Article
45 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteria have evolved numerous strategies to increase their competitiveness and fight against each other. Indeed, a large arsenal of antibacterial weapons is available in order to inhibit the proliferation of competitor cells. Polymorphic toxin systems (PTS), recently identified by bioinformatics in all major bacterial lineages, correspond to such a system primarily involved in conflict between related bacterial strains. They are typically composed of a secreted multidomain toxin, a protective immunity protein, and multiple cassettes encoding alternative toxic domains. The C-terminal domains of polymorphic toxins carry the toxic activity, whereas the N-terminal domains are related to the trafficking mode. In silico analysis of PTS identified over 150 distinct toxin domains, including putative nuclease, deaminase, or peptidase domains. Immunity genes found immediately downstream of the toxin genes encode small proteins that protect bacteria against their own toxins or against toxins secreted by neighboring cells. PTS encompass well-known colicins and pyocins, contact-dependent growth inhibition systems which include CdiA and Rhs toxins and some effectors of type VI secretion systems. We have recently characterized the MafB toxins, a new family of PTS deployed by pathogenic Neisseria spp. Many other putative PTS have been identified by in silico predictions but have yet to be characterized experimentally. However, the high number of these systems suggests that PTS have a fundamental role in bacterial biology that is likely to extend beyond interbacterial competition.
Indexed as
Identifiers
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.