ArticlePloS one2013
Dissection of the TssB-TssC interface during type VI secretion sheath complex formation.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.
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.
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
16 citing papers in PubMed, 1 synthesis or guideline pooled it, 25 citations in OpenAlex.
- Drug-resistantClinical microbiology reviews · 2025Pooled it
- From gut colonization to recurrence:Gut microbes · 2026Review
- Phenotypic heterogeneity optimizes trade-offs during adaptive deployment of the type VI secretion system.PLoS biology · 2026Article
- Article
- The type-VI secretion system of the beneficial symbiontMicrobiology (Reading, England) · 2023Review
- An Overview of Anti-Eukaryotic T6SS Effectors.Frontiers in cellular and infection microbiology · 2020Review
- Role of Recipient Susceptibility Factors During Contact-Dependent Interbacterial Competition.Frontiers in microbiology · 2020Review
- Structure and Activity of the Type VI Secretion System.Microbiology spectrum · 2019Review
- Type VI Secretion System in PathogenicFrontiers in microbiology · 2019Review
- Atomic Structure of Type VI Contractile Sheath from Pseudomonas aeruginosa.Structure (London, England : 1993) · 2018Article
- A single point mutation in a TssB/VipA homolog disrupts sheath formation in the type VI secretion system of Proteus mirabilis.PloS one · 2017Article
- Structure and specificity of the Type VI secretion system ClpV-TssC interaction in enteroaggregative Escherichia coli.Scientific reports · 2016Article
- Coevolution of the ATPase ClpV, the sheath proteins TssB and TssC, and the accessory protein TagJ/HsiE1 distinguishes type VI secretion classes.The Journal of biological chemistry · 2014Article
- The VgrG proteins are "à la carte" delivery systems for bacterial type VI effectors.The Journal of biological chemistry · 2014Article
- Article
- A disordered region in the EvpP protein from the type VI secretion system of Edwardsiella tarda is essential for EvpC binding.PloS one · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Type VI secretion system (T6SS) is a versatile machine that delivers toxins into either eukaryotic or bacterial cells. At a molecular level, the T6SS is composed of a membrane complex that anchors a long cytoplasmic tubular structure to the cell envelope. This structure is thought to resemble the tail of contractile bacteriophages. It is composed of the Hcp protein that assembles into hexameric rings stacked onto each other to form a tube similar to the phage tail tube. This tube is proposed to be wrapped by a structure called the sheath, composed of two proteins, TssB and TssC. It has been shown using fluorescence microscopy that the TssB and TssC proteins assemble into a tubular structure that cycles between long and short conformations suggesting that, similarly to the bacteriophage sheath, the T6SS sheath undergoes elongation and contraction events. The TssB and TssC proteins have been shown to interact and a specific α-helix of TssB is required for this interaction. Here, we confirm that the TssB and TssC proteins interact in enteroaggregative E. coli. We further show that this interaction requires the N-terminal region of TssC and the conserved α-helix of TssB. Using site-directed mutagenesis coupled to phenotypic analyses, we demonstrate that an hydrophobic motif located in the N-terminal region of this helix is required for interaction with TssC, sheath assembly and T6SS function.
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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.