ArticlePLoS genetics2015
The Type VI Secretion TssEFGK-VgrG Phage-Like Baseplate Is Recruited to the TssJLM Membrane Complex via Multiple Contacts and Serves As Assembly Platform for Tail Tube/Sheath Polymerization.
Article in PLoS genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 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
114 citing papers in PubMed, 185 citations in OpenAlex.
- From gut colonization to recurrence:Gut microbes · 2026Review
- Regulation of Type VI Secretion Systems of Burkholderia during transition to intracellular lifestyle.EMBO reports · 2026Article
- Functional diversity of accessory factors of the type VI secretion system.Journal of bacteriology · 2026Review
- Repression of the Type VI Secretion System (T6SS) During Biofilm Formation Provides a Fitness Advantage forMicroorganisms · 2026Article
- Secretion systems shaping host-pathogen interactions in Burkholderia species.Applied microbiology and biotechnology · 2026Review
- The type VI secretion system and associated effector proteins.Nature reviews. Microbiology · 2026Review
- TseCurrent research in microbial sciences · 2026Article
- The SPI-20 and SPI-21 T6SS gene clusters fromFrontiers in microbiology · 2026Article
- The SPI-6 T6SS gene cluster fromFrontiers in microbiology · 2026Article
- TssW-PpkA-Fha axis controls the positioning and initiation of the type VI secretion system inmBio · 2025Article
- Deciphering theJournal of bacteriology · 2025Review
- Review
- The Competitive Edge: T6SS-Mediated Interference Competition byMicroorganisms · 2025Review
- Not just passengers: effectors contribute to the assembly of the type VI secretion system as structural building blocks.Journal of bacteriology · 2025Review
- Article
- Identification and functional characterization of a fructose-inducible phosphotransferase system inApplied and environmental microbiology · 2025Article
- Delivery determinants of anmBio · 2025Article
- Article
- The Tol Pal system integrates maintenance of the three layered cell envelope.npj antimicrobials and resistance · 2024Review
- Advanced glycation end-product crosslinking activates a type VI secretion system phospholipase effector protein.Nature communications · 2024Article
54 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
5 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 widespread weapon dedicated to the delivery of toxin proteins into eukaryotic and prokaryotic cells. The 13 T6SS subunits assemble a cytoplasmic contractile structure anchored to the cell envelope by a membrane-spanning complex. This structure is evolutionarily, structurally and functionally related to the tail of contractile bacteriophages. In bacteriophages, the tail assembles onto a protein complex, referred to as the baseplate, that not only serves as a platform during assembly of the tube and sheath, but also triggers the contraction of the sheath. Although progress has been made in understanding T6SS assembly and function, the composition of the T6SS baseplate remains mostly unknown. Here, we report that six T6SS proteins-TssA, TssE, TssF, TssG, TssK and VgrG-are required for proper assembly of the T6SS tail tube, and a complex between VgrG, TssE,-F and-G could be isolated. In addition, we demonstrate that TssF and TssG share limited sequence homologies with known phage components, and we report the interaction network between these subunits and other baseplate and tail components. In agreement with the baseplate being the assembly platform for the tail, fluorescence microscopy analyses of functional GFP-TssF and TssK-GFP fusion proteins show that these proteins assemble stable and static clusters on which the sheath polymerizes. Finally, we show that recruitment of the baseplate to the apparatus requires initial positioning of the membrane complex and contacts between TssG and the inner membrane TssM protein.
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.