ArticleNature microbiology2018
Mechanism of loading and translocation of type VI secretion system effector Tse6.
Article in Nature microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
What it found
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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.
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Who cites it
66 citing papers in PubMed, 117 citations in OpenAlex.
- Functional diversity of accessory factors of the type VI secretion system.Journal of bacteriology · 2026Review
- Targeted delivery of diverse biomolecules with engineered bacterial nanosyringes.Nature biotechnology · 2026Article
- Molecular basis of type VI secretion system effector loading.Nature microbiology · 2026Article
- An ART-fold Rhs toxin from Pluralibacter gergoviae defines Tne5, a novel family of NAD(P) glycohydrolases effectors.The Journal of biological chemistry · 2026Article
- A T4SS effector directly disarms competing antibacterial T6SSs by hijacking their conserved spike component.Science China. Life sciences · 2026Article
- "Molecular insights into the bactericidal toxin Tle1 of Pseudomonas aeruginosa: Interaction with VgrG, its adaptor, and its immunity protein".The Journal of biological chemistry · 2026Article
- The type VI secretion system and associated effector proteins.Nature reviews. Microbiology · 2026Review
- Systematic identification of Salmonella T6SS effectors uncovers diverse new families and lipid-targeting activities.PLoS biology · 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
- TseCurrent research in microbial sciences · 2026Article
- Article
- Occurrence of type VI secretion system effector genes in longitudinal isolates ofMicrobial genomics · 2025Article
- Molecular mechanism of bacteriophage contraction structure of an S-layer-penetrating bacteriophage.Life science alliance · 2025Article
- Insights into mechanisms and significance of domain swapping from emerging examples in the Mog1p/PsbP-like fold.Biochemical and biophysical research communications · 2025Review
- Not just passengers: effectors contribute to the assembly of the type VI secretion system as structural building blocks.Journal of bacteriology · 2025Review
- Article
- Specialized killing across the domains of life by the type VI secretion systems of Pseudomonas aeruginosa.The Biochemical journal · 2025Review
- Identifying a type of toxic effectors exported by the type VII secretion system to enhance competitive fitness inFrontiers in cellular and infection microbiology · 2025Article
- Thioredoxin 1 moonlights as a chaperone for an interbacterial ADP-ribosyltransferase toxin.Nature communications · 2024Article
6 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
6 authors at 3 institutions in 3 countries.
Funding
Abstract
The type VI secretion system (T6SS) primarily functions to mediate antagonistic interactions between contacting bacterial cells, but also mediates interactions with eukaryotic hosts. This molecular machine secretes antibacterial effector proteins by undergoing cycles of extension and contraction; however, how effectors are loaded into the T6SS and subsequently delivered to target bacteria remains poorly understood. Here, using electron cryomicroscopy, we analysed the structures of the Pseudomonas aeruginosa effector Tse6 loaded onto the T6SS spike protein VgrG1 in solution and embedded in lipid nanodiscs. In the absence of membranes, Tse6 stability requires the chaperone EagT6, two dimers of which interact with the hydrophobic transmembrane domains of Tse6. EagT6 is not directly involved in Tse6 delivery but is crucial for its loading onto VgrG1. VgrG1-loaded Tse6 spontaneously enters membranes and its toxin domain translocates across a lipid bilayer, indicating that effector delivery by the T6SS does not require puncturing of the target cell inner membrane by VgrG1. Eag chaperone family members from diverse Proteobacteria are often encoded adjacent to putative toxins with predicted transmembrane domains and we therefore anticipate that our findings will be generalizable to numerous T6SS-exported membrane-associated effectors.
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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.