ArticleCell2015
Atomic structure of T6SS reveals interlaced array essential to function.
Article in Cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.
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Who cites it
105 citing papers in PubMed.
- Structure and potential role of T6SS effector PdpC in Francisella tularensis intracellular lifestyle.Communications biology · 2026Article
- T6SS1 suppresses pro-inflammatory cytokine transcription to drive immune evasion and systemic infection inInfection and immunity · 2026Article
- Article
- T6SS-mediated competition bymSystems · 2025Article
- Outer membrane tube formation bymBio · 2025Article
- Atomic Structure and Phospholipid Binding Properties of thebioRxiv : the preprint server for biology · 2025Article
- Article
- Structural dynamics of contractile injection systems.Biophysical journal · 2025Article
- Identification of theFrontiers in cellular and infection microbiology · 2025Article
- Atomic structures of a bacteriocin targeting Gram-positive bacteria.Nature communications · 2024Article
- Atomic structures of a bacteriocin targeting Gram-positive bacteria.Research square · 2024Article
- Breaking the cellular defense: the role of autophagy evasion inFrontiers in cellular and infection microbiology · 2024Article
- Pathogenicity and virulence ofVirulence · 2023Review
- Structure ofViruses · 2023Article
- A subcellular biochemical model for T6SS dynamics reveals winning competitive strategies.PNAS nexus · 2023Article
- Killing in the name of: T6SS structure and effector diversity.Microbiology (Reading, England) · 2023Review
- Intracellular Phage Tail-Like Nanostructures Affect Susceptibility of Streptomyces lividans to Osmotic Stress.mSphere · 2023Article
- In Situ Structures of the Ultra-Long Extended and Contracted Tail of Myoviridae Phage P1.Viruses · 2023Article
- High-resolution reconstruction of a Jumbo-bacteriophage infecting capsulated bacteria using hyperbranched tail fibers.Nature communications · 2022Article
- Atomic Structure of IglD Demonstrates Its Role as a Component of the Baseplate Complex of themBio · 2022Article
45 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors.
Funding
Abstract
Type VI secretion systems (T6SSs) are newly identified contractile nanomachines that translocate effector proteins across bacterial membranes. The Francisella pathogenicity island, required for bacterial phagosome escape, intracellular replication, and virulence, was presumed to encode a T6SS-like apparatus. Here, we experimentally confirm the identity of this T6SS and, by cryo electron microscopy (cryoEM), show the structure of its post-contraction sheath at 3.7 Å resolution. We demonstrate the assembly of this T6SS by IglA/IglB and secretion of its putative effector proteins in response to environmental stimuli. The sheath has a quaternary structure with handedness opposite that of contracted sheath of T4 phage tail and is organized in an interlaced two-dimensional array by means of β sheet augmentation. By structure-based mutagenesis, we show that this interlacing is essential to secretion, phagosomal escape, and intracellular replication. Our atomic model of the T6SS will facilitate design of drugs targeting this highly prevalent secretion apparatus.
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