ArticleNature microbiology2021
Identification of Tse8 as a Type VI secretion system toxin from Pseudomonas aeruginosa that targets the bacterial transamidosome to inhibit protein synthesis in prey cells.
Article in Nature microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
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Who cites it
33 citing papers in PubMed, 57 citations in OpenAlex.
- Functional characterization of a pore-forming effector TseMt from the H4 type VI secretion system ofmLife · 2026Article
- The type VI secretion system and associated effector proteins.Nature reviews. Microbiology · 2026Review
- Structural and functional insights into Pseudomonas aeruginosa's secretion systems 1-6: regulation, role in microbial keratitis and drug targets.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2026Review
- Occurrence of type VI secretion system effector genes in longitudinal isolates ofMicrobial genomics · 2025Article
- Coordination of virulence factors and lifestyle transition in Pseudomonas aeruginosa through single-cell analysis.Communications biology · 2025Article
- Two cysteines control Tse1 secretion by H1-T6SS in Pseudomonas aeruginosa.Protein science : a publication of the Protein Society · 2025Article
- Type VI secretion system activity at lethal antibiotic concentrations leads to overestimation of weapon potency.Microbiology (Reading, England) · 2025Article
- The Pseudomonas aeruginosa Type VI secretion system toxin Tse8 evolved from a novel N-carbamoylputrescine amidohydrolase.The Biochemical journal · 2025Article
- The Pseudomonas aeruginosa Tse4 toxin assembles ion-selective and voltage-sensitive ion channels to couple membrane depolarisation with K+ efflux.PLoS pathogens · 2025Article
- A new class of type VI secretion system effectors can carry two toxic domains and are recognized through the WHIX motif for export.PLoS biology · 2025Article
- A universal and wide-range cytosine base editor via domain-inlaid and fidelity-optimized CRISPR-FrCas9.Nature communications · 2025Article
- Distribution of the four type VI secretion systems in Pseudomonas aeruginosa and classification of their core and accessory effectors.Nature communications · 2025Article
- Systematic discovery of antibacterial and antifungal bacterial toxins.Nature microbiology · 2024Article
- Bactericidal effectors of themBio · 2024Article
- Review
- The type VI secretion system of the emerging pathogenmSphere · 2023Article
- Killing in the name of: T6SS structure and effector diversity.Microbiology (Reading, England) · 2023Review
- Effectiveness of Pseudomonas aeruginosa type VI secretion system relies on toxin potency and type IV pili-dependent interaction.PLoS pathogens · 2023Article
- Recent advances in therapeutic targets identification and development of treatment strategies towards Pseudomonas aeruginosa infections.BMC microbiology · 2023Review
- Article
Corrections and comments
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Authors and funding
11 authors at 6 institutions in 5 countries.
Funding
Abstract
The Type VI secretion system (T6SS) is a bacterial nanomachine that delivers toxic effectors to kill competitors or subvert some of their key functions. Here, we use transposon directed insertion-site sequencing to identify T6SS toxins associated with the H1-T6SS, one of the three T6SS machines found in Pseudomonas aeruginosa. This approach identified several putative toxin-immunity pairs, including Tse8-Tsi8. Full characterization of this protein pair demonstrated that Tse8 is delivered by the VgrG1a spike complex into prey cells where it targets the transamidosome, a multiprotein complex involved in protein synthesis in bacteria that lack either one, or both, of the asparagine and glutamine transfer RNA synthases. Biochemical characterization of the interactions between Tse8 and the transamidosome components GatA, GatB and GatC suggests that the presence of Tse8 alters the fine-tuned stoichiometry of the transamidosome complex, and in vivo assays demonstrate that Tse8 limits the ability of prey cells to synthesize proteins. These data expand the range of cellular components targeted by the T6SS by identifying a T6SS toxin affecting protein synthesis and validate the use of a transposon directed insertion site sequencing-based global genomics approach to expand the repertoire of T6SS toxins in T6SS-encoding bacteria.
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