ArticleMolecular microbiology2014
Genetically distinct pathways guide effector export through the type VI secretion system.
Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers.
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140 citing papers in PubMed, 211 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
- Elongation Factor Tu Acts as a Chaperone to Activate an Antibacterial RNase Toxin.Molecular microbiology · 2026Article
- Effector conformational plasticity enables lineage-specific secretion via Hcp heterohexamers in gut symbionts.Nature communications · 2026Article
- Biophysical characterization of Eag chaperones suggests the mechanism of effector transmembrane domain release.Nature communications · 2026Article
- The SPI-6 T6SS gene cluster fromFrontiers in microbiology · 2026Article
- The SPI-20 and SPI-21 T6SS gene clusters fromFrontiers in microbiology · 2026Article
- Interbacterial warfare in the human gut: insights from Bacteroidales' perspective.Gut microbes · 2025Review
- Distinct immunity protein families mediate compartment-specific neutralization of a bacterial toxin.Cell reports · 2025Article
- Occurrence of type VI secretion system effector genes in longitudinal isolates ofMicrobial genomics · 2025Article
- Pseudomonads coordinate innate defense against viruses and bacteria with a single regulatory system.Cell host & microbe · 2025Article
- Two cysteines control Tse1 secretion by H1-T6SS in Pseudomonas aeruginosa.Protein science : a publication of the Protein Society · 2025Article
- Deciphering theJournal of bacteriology · 2025Review
- Article
- The Pseudomonas aeruginosa Tse4 toxin assembles ion-selective and voltage-sensitive ion channels to couple membrane depolarisation with K+ efflux.PLoS pathogens · 2025Article
- Not just passengers: effectors contribute to the assembly of the type VI secretion system as structural building blocks.Journal of bacteriology · 2025Review
- Distribution of the four type VI secretion systems in Pseudomonas aeruginosa and classification of their core and accessory effectors.Nature communications · 2025Article
- Specialized killing across the domains of life by the type VI secretion systems of Pseudomonas aeruginosa.The Biochemical journal · 2025Review
- A widespread accessory protein family diversifies the effector repertoire of the type VI secretion system spike.Nature communications · 2024Article
- Contact-dependent growth inhibition (CDI) systems deploy a large family of polymorphic ionophoric toxins for inter-bacterial competition.PLoS genetics · 2024Article
80 more citing papers are in PubMed but not listed here.
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
Abstract
Bacterial secretion systems often employ molecular chaperones to recognize and facilitate export of their substrates. Recent work demonstrated that a secreted component of the type VI secretion system (T6SS), haemolysin co-regulated protein (Hcp), binds directly to effectors, enhancing their stability in the bacterial cytoplasm. Herein, we describe a quantitative cellular proteomics screen for T6S substrates that exploits this chaperone-like quality of Hcp. Application of this approach to the Hcp secretion island I-encoded T6SS (H1-T6SS) of Pseudomonas aeruginosa led to the identification of a novel effector protein, termed Tse4 (type VI secretion exported 4), subsequently shown to act as a potent intra-specific H1-T6SS-delivered antibacterial toxin. Interestingly, our screen failed to identify two predicted H1-T6SS effectors, Tse5 and Tse6, which differ from Hcp-stabilized substrates by the presence of toxin-associated PAAR-repeat motifs and genetic linkage to members of the valine-glycine repeat protein G (vgrG) genes. Genetic studies further distinguished these two groups of effectors: Hcp-stabilized effectors were found to display redundancy in interbacterial competition with respect to the requirement for the two H1-T6SS-exported VgrG proteins, whereas Tse5 and Tse6 delivery strictly required a cognate VgrG. Together, we propose that interaction with either VgrG or Hcp defines distinct pathways for T6S effector export.
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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.