ArticleScientific reports2018
The bacterial Type III toxin-antitoxin system, ToxIN, is a dynamic protein-RNA complex with stability-dependent antiviral abortive infection activity.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 48 citations in OpenAlex.
- Bioengineering Interventions to Enhance the Capacity of the Gut Microbiota in Controlling Food Allergies.Life (Basel, Switzerland) · 2026Review
- Steering the course: targeting and exploiting surface receptors in phage therapy.Journal of bacteriology · 2026Review
- Revisiting lactococcal abortive infection-like antiphage systems: diversity, structures, and mechanisms.FEMS microbiology reviews · 2026Review
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- Antibiotic resistance and virulence of bacteria in spices: a systematic review.One health outlook · 2025Review
- Deciphering the RNA-based regulation mechanism of the phage-encoded AbiF system in Clostridioides difficile.PLoS genetics · 2025Article
- Construction of antibiotic-free riboflavin producer inSynthetic and systems biotechnology · 2025Article
- Characterization of a small non-coding RNA S612 inEngineering microbiology · 2025Article
- Isolation and characterization of a phage collection against Pseudomonas putida.Environmental microbiology · 2024Article
- Toxin:antitoxin ratio sensing autoregulation of theScience advances · 2024Article
- Replication cycle timing determines phage sensitivity to a cytidine deaminase toxin/antitoxin bacterial defense system.PLoS pathogens · 2023Article
- Bacterial Toxin-Antitoxin Systems' Cross-Interactions-Implications for Practical Use in Medicine and Biotechnology.Toxins · 2023Review
- The Battle between Bacteria and Bacteriophages: A Conundrum to Their Immune System.Antibiotics (Basel, Switzerland) · 2023Review
- Time to lysis determines phage sensitivity to a cytidine deaminase toxin/antitoxin bacterial defense system.bioRxiv : the preprint server for biology · 2023Article
- Bacterial toxin-antitoxin systems: Novel insights on toxin activation across populations and experimental shortcomings.Current research in microbial sciences · 2023Review
- Article
- Phage defence by deaminase-mediated depletion of deoxynucleotides in bacteria.Nature microbiology · 2022Article
- The Vibrio cholerae Seventh Pandemic Islands act in tandem to defend against a circulating phage.PLoS genetics · 2022Article
- Identification, functional characterization, assembly and structure of ToxIN type III toxin-antitoxin complex from E. coli.Nucleic acids research · 2022Article
- Identification and characterization of VapBC toxin-antitoxin system inRNA (New York, N.Y.) · 2021Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Bacteria have evolved numerous defense systems to protect themselves from viral (bacteriophage) infection. The ToxIN system of Pectobacterium atrosepticum is a Type III toxin-antitoxin complex and "altruistic suicide" anti-phage system, which kills phage-infected cells through the release of a ribonuclease toxin, ToxN. ToxN is counteracted by a co-transcribed antitoxic RNA pseudoknot, ToxI, which self-assembles with ToxN into an inactive 3 ToxI:3 ToxN complex in vitro. However it is not known whether this complex is predominant in vivo, or how the complex is disassembled following infection to trigger a lethal, "altruistic" response. In this study, we characterise ToxI turnover and folding, and explore the link between complex stability and anti-phage activity, with a view to understanding events that lead to ToxN-mediated suicide following phage infection. We present evidence that ToxN constantly cleaves fresh ToxI in vivo rather than staying associated with pre-processed antitoxin, and that the ToxI antitoxin can partially fold spontaneously using conserved nucleotides. We also show that reducing the stability of the ToxIN complex can increase the strength of the antiviral response in a phage-dependent manner. Based on this information, we propose a revised model for ToxN inhibition, complex assembly and activation by infecting bacteriophage.
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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.