ArticleNature microbiology2019
T3S injectisome needle complex structures in four distinct states reveal the basis of membrane coupling and assembly.
Article in Nature microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 72 citations in OpenAlex.
- How Salmonella Works Under Osmotic and Desiccation Stresses.Comprehensive reviews in food science and food safety · 2026Review
- Calcium controls type III secretion switch through an SctV-SctW interplay.Frontiers in microbiology · 2026Article
- Dynamic interaction of the Yersinia pseudotuberculosis type three secretion system proteins LcrV and LcrG.Protein science : a publication of the Protein Society · 2026Article
- Continuous exchange of an inner-membrane ring component is required for assembly and function of the type III secretion system.Nature communications · 2025Article
- Structural insights into the secretin complex of a type IVb pilus system.Nature communications · 2025Article
- Targeting Type III Secretion System usingIndian journal of microbiology · 2025Review
- Cryo-Electron Microscopy of BfpB Reveals a Type IVb Secretin Multimer Adapted to Accommodate the Exceptionally Wide Bundle-Forming Pilus.Pathogens (Basel, Switzerland) · 2025Article
- Structural insights into peptidoglycan glycosidase EtgA binding to the inner rod protein EscI of the type III secretion system via a designed EscI-EtgA fusion protein.Protein science : a publication of the Protein Society · 2024Article
- Expression, Purification, and Cryo-EM Structural Analysis of an Outer Membrane Secretin Channel.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Insights into dynamics and gating properties of T2SS secretins.Science advances · 2023Article
- A Tale aboutMicroorganisms · 2023Review
- Virulence-associated type III secretion systems in Gram-negative bacteria.Microbiology (Reading, England) · 2023Review
- Integrative structural analysis of the type III secretion system needle complex from Shigella flexneri.Protein science : a publication of the Protein Society · 2023Article
- Recruitment of heterologous substrates by bacterial secretion systems for transkingdom translocation.Frontiers in cellular and infection microbiology · 2023Review
- Assembly and architecture of the type III secretion sorting platform.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Cryo-EM of the injectisome and type III secretion systems.Current opinion in structural biology · 2022Review
- Type III secretion by Yersinia pseudotuberculosis is reliant upon an authentic N-terminal YscX secretor domain.Molecular microbiology · 2022Article
- Recognition of discrete export signals in early flagellar subunits during bacterial type III secretion.eLife · 2022Article
- Recognition of a translocation motif in the regulator HpaA fromFrontiers in plant science · 2022Article
- CryoEM structure of the outer membrane secretin channel pIV from the f1 filamentous bacteriophage.Nature communications · 2021Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
The bacterial injectisome is a syringe-shaped macromolecular nanomachine utilized by many pathogenic Gram-negative bacteria, including the causative agents of plague, typhoid fever, whooping cough, sexually transmitted infections and major nosocomial infections. Bacterial proteins destined for self-assembly and host-cell targeting are translocated by the injectisome in a process known as type III secretion (T3S). The core structure is the ~4 MDa needle complex (NC), built on a foundation of three highly oligomerized ring-forming proteins that create a hollow scaffold spanning the bacterial inner membrane (IM) (24-mer ring-forming proteins PrgH and PrgK in the Salmonella enterica serovar Typhimurium Salmonella pathogenicity island 1 (SPI-1) type III secretion system (T3SS)) and outer membrane (OM) (15-mer InvG, a member of the broadly conserved secretin pore family). An internalized helical needle projects from the NC and bacterium, ultimately forming a continuous passage to the host, for delivery of virulence effectors. Here, we have captured snapshots of the entire prototypical SPI-1 NC in four distinct needle assembly states, including near-atomic resolution, and local reconstructions in the absence and presence of the needle. These structures reveal the precise localization and molecular interactions of the internalized SpaPQR 'export apparatus' complex, which is intimately encapsulated and stabilized within the IM rings in the manner of a nanodisc, and to which the PrgJ rod directly binds and functions as an initiator and anchor of needle polymerization. We also describe the molecular details of the extensive and continuous coupling interface between the OM secretin and IM rings, which is remarkably facilitated by a localized 16-mer stoichiometry in the periplasmic-most coupling domain of the otherwise 15-mer InvG oligomer.
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