ArticleNature2015
Biogenesis and structure of a type VI secretion membrane core complex.
Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 169 papers.
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Who cites it
169 citing papers in PubMed, 272 citations in OpenAlex.
- 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
- Genomic characterization of the type VI secretion system in extraintestinal pathogenicMicrobiology spectrum · 2026Article
- Klebsiella pneumoniae inhibits vasodilation through capsule and T6SS-dependent pathways.Nature microbiology · 2026Article
- Review
- Phenotypic heterogeneity optimizes trade-offs during adaptive deployment of the type VI secretion system.PLoS biology · 2026Article
- Neisseria subflava Type 6 Secretion System competition with bacterial and fungal species.Applied microbiology and biotechnology · 2026Article
- The type VI secretion system and associated effector proteins.Nature reviews. Microbiology · 2026Review
- Functional divergence and regulatory network of the type VI secretion system inJournal of bacteriology · 2026Review
- OmpA_C-Like Domain of PorE Is Essential for PorE Function in the Type IX Secretion System (T9SS) of Porphyromonas gingivalis and Some T9SS Cargo Proteins Are Secreted in a PorE-Independent Manner.Microbiology and immunology · 2026Article
- The SPI-6 T6SS gene cluster fromFrontiers in microbiology · 2026Article
- The SPI-20 and SPI-21 T6SS gene clusters fromFrontiers in microbiology · 2026Article
- T3SS1 accessory protein geneFrontiers in cellular and infection microbiology · 2026Article
- Plasmids serve as vehicles and reservoirs of type VI secretion systems.ISME communications · 2026Article
- TssW-PpkA-Fha axis controls the positioning and initiation of the type VI secretion system inmBio · 2025Article
- T6SS4 is heterogeneously expressed in Yersinia pseudotuberculosis and is a target for transcriptional and post-transcriptional regulation.PLoS pathogens · 2025Article
- Function and firing of theeLife · 2025Article
- Engineering the T6SS of Pseudomonas for targeted delivery of antibacterial and antifungal effectors.Journal of biological engineering · 2025Article
- Not just passengers: effectors contribute to the assembly of the type VI secretion system as structural building blocks.Journal of bacteriology · 2025Review
- Carvacrol and Streptomycin in Combination Weaken Streptomycin Resistance inPlants (Basel, Switzerland) · 2025Article
109 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
14 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteria share their ecological niches with other microbes. The bacterial type VI secretion system is one of the key players in microbial competition, as well as being an important virulence determinant during bacterial infections. It assembles a nano-crossbow-like structure in the cytoplasm of the attacker cell that propels an arrow made of a haemolysin co-regulated protein (Hcp) tube and a valine-glycine repeat protein G (VgrG) spike and punctures the prey's cell wall. The nano-crossbow is stably anchored to the cell envelope of the attacker by a membrane core complex. Here we show that this complex is assembled by the sequential addition of three type VI subunits (Tss)-TssJ, TssM and TssL-and present a structure of the fully assembled complex at 11.6 Å resolution, determined by negative-stain electron microscopy. With overall C5 symmetry, this 1.7-megadalton complex comprises a large base in the cytoplasm. It extends in the periplasm via ten arches to form a double-ring structure containing the carboxy-terminal domain of TssM (TssMct) and TssJ that is anchored in the outer membrane. The crystal structure of the TssMct-TssJ complex coupled to whole-cell accessibility studies suggest that large conformational changes induce transient pore formation in the outer membrane, allowing passage of the attacking Hcp tube/VgrG spike.
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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.