ArticleNature communications2020
Intramolecular chaperone-mediated secretion of an Rhs effector toxin by a type VI secretion system.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 53 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
53 citing papers in PubMed, 77 citations in OpenAlex.
- A type VI secretion ADP-ribosyltransferase Rhs toxin selectively modifies charged tRNAThr(GGU) anticodon loops to block ACC codon decoding.Nucleic acids research · 2026Article
- Specific and broad-spectrum antibacterial effectors of type VI secretion system drive competition ofMicrobiology spectrum · 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
- Global identification of Chromobacterium violaceum T6SS effectors reveals an Rhs antibacterial toxin featuring FIX and ADP-ribosyltransferase domains.The Journal of biological chemistry · 2026Article
- AnMicrobiology spectrum · 2026Article
- The type VI secretion system and associated effector proteins.Nature reviews. Microbiology · 2026Review
- Reprogrammed SimCells for antimicrobial therapy.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Ancestral neuronal receptors are bacterial accessory toxins.Nature communications · 2026Article
- Structural insights into the antibacterial function of the Pseudomonas putida effector Tke5.The EMBO journal · 2026Article
- Article
- The type 6 secretion system immunity protein RhsFI has been repurposed for small RNA regulation in pathogenic Escherichia coli.Nucleic acids research · 2025Article
- Not just passengers: effectors contribute to the assembly of the type VI secretion system as structural building blocks.Journal of bacteriology · 2025Review
- Article
- 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
- Specialized killing across the domains of life by the type VI secretion systems of Pseudomonas aeruginosa.The Biochemical journal · 2025Review
- Fulminant necrotizing fasciitis secondary toFrontiers in medicine · 2025Article
- Article
- A widespread accessory protein family diversifies the effector repertoire of the type VI secretion system spike.Nature communications · 2024Article
- Structure of a Rhs effector clade domain provides mechanistic insights into type VI secretion system toxin delivery.Nature communications · 2024Article
- T6SS in plant pathogens: unique mechanisms in complex hosts.Infection and immunity · 2024Review
Corrections and comments
- Erratum issued
Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
Abstract
Bacterial Rhs proteins containing toxic domains are often secreted by type VI secretion systems (T6SSs) through unclear mechanisms. Here, we show that the T6SS Rhs-family effector TseI of Aeromonas dhakensis is subject to self-cleavage at both the N- and the C-terminus, releasing the middle Rhs core and two VgrG-interacting domains (which we name VIRN and VIRC). VIRC is an endonuclease, and the immunity protein TsiI protects against VIRC toxicity through direct interaction. Proteolytic release of VIRC and VIRN is mediated, respectively, by an internal aspartic protease activity and by two conserved glutamic residues in the Rhs core. Mutations abolishing self-cleavage do not block secretion, but reduce TseI toxicity. Deletion of VIRN or the Rhs core abolishes secretion. TseI homologs from Pseudomonas syringae, P. aeruginosa, and Vibrio parahaemolyticus are also self-cleaved. VIRN and VIRC interact with protein VgrG1, while the Rhs core interacts with protein TecI. We propose that VIRN and the Rhs core act as T6SS intramolecular chaperones to facilitate toxin secretion and function.
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.