ArticlePLoS pathogens2013
A refined model of the prototypical Salmonella SPI-1 T3SS basal body reveals the molecular basis for its assembly.
Article in PLoS pathogens, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Continuous exchange of an inner-membrane ring component is required for assembly and function of the type III secretion system.Nature communications · 2025Article
- Assembly and architecture of the type III secretion sorting platform.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Research Progress on Small Molecular Inhibitors of the Type 3 Secretion System.Molecules (Basel, Switzerland) · 2022Review
- Asiatic Acid Attenuates Inflammation Induced byInternational journal of molecular sciences · 2022Article
- Cryo-EM of the injectisome and type III secretion systems.Current opinion in structural biology · 2022Review
- Native flagellar MS ring is formed by 34 subunits with 23-fold and 11-fold subsymmetries.Nature communications · 2021Article
- Substrate-engaged type III secretion system structures reveal gating mechanism for unfolded protein translocation.Nature communications · 2021Article
- TheMicroorganisms · 2021Review
- Molecular Targets and Strategies for Inhibition of the Bacterial Type III Secretion System (T3SS); Inhibitors Directly Binding to T3SS Components.Biomolecules · 2021Review
- The Role of the Membrane-Associated Domain of the Export Apparatus Protein, EscV (SctV), in the Activity of the Type III Secretion System.Frontiers in microbiology · 2021Article
- The Structures of SctK and SctD from Pseudomonas aeruginosa Reveal the Interface of the Type III Secretion System Basal Body and Sorting Platform.Journal of molecular biology · 2020Article
- Type three secretion system in Salmonella Typhimurium: the key to infection.Genes & genomics · 2020Review
- The cytoplasmic domain of MxiG interacts with MxiK and directs assembly of the sorting platform in theThe Journal of biological chemistry · 2019Article
- T3S injectisome needle complex structures in four distinct states reveal the basis of membrane coupling and assembly.Nature microbiology · 2019Article
- PhoP-Mediated Repression of the SPI1 Type 3 Secretion System in Salmonella enterica Serovar Typhimurium.Journal of bacteriology · 2019Article
- The Injectisome, a Complex Nanomachine for Protein Injection into Mammalian Cells.EcoSal Plus · 2019Review
- TheeLife · 2019Article
- A Hybrid Secretion System Facilitates Bacterial Sporulation: A Structural Perspective.Microbiology spectrum · 2019Review
- Visualization of the type III secretion mediatedeLife · 2018Article
- Cryo-EM analysis of the T3S injectisome reveals the structure of the needle and open secretin.Nature communications · 2018Article
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11 authors.
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Abstract
The T3SS injectisome is a syringe-shaped macromolecular assembly found in pathogenic Gram-negative bacteria that allows for the direct delivery of virulence effectors into host cells. It is composed of a "basal body", a lock-nut structure spanning both bacterial membranes, and a "needle" that protrudes away from the bacterial surface. A hollow channel spans throughout the apparatus, permitting the translocation of effector proteins from the bacterial cytosol to the host plasma membrane. The basal body is composed largely of three membrane-embedded proteins that form oligomerized concentric rings. Here, we report the crystal structures of three domains of the prototypical Salmonella SPI-1 basal body, and use a new approach incorporating symmetric flexible backbone docking and EM data to produce a model for their oligomeric assembly. The obtained models, validated by biochemical and in vivo assays, reveal the molecular details of the interactions driving basal body assembly, and notably demonstrate a conserved oligomerization mechanism.
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