ArticlePLoS pathogens2011
Crystal structure of PrgI-SipD: insight into a secretion competent state of the type three secretion system needle tip and its interaction with host ligands.
Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.
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Who cites it
41 citing papers in PubMed, 1 synthesis or guideline pooled it, 68 citations in OpenAlex.
- Recent progress in molecular mechanisms of Salmonella effectors involved in gut epithelium invasion.Molecular biology reports · 2025Pooled it
- Neutralizing human monoclonal antibodies that target the PcrV component of the type III secretion system ofeLife · 2026Article
- Infection biology ofEcoSal Plus · 2024Review
- Evaluation of the Anticancer and Biological Activities of Istaroxime via Ex Vivo Analyses, Molecular Docking and Conceptual Density Functional Theory Computations.Molecules (Basel, Switzerland) · 2023Article
- Synthesis, Characterization, and Docking Study of Novel Thioureidophosphonate-Incorporated Silver Nanocomposites as Potent Antibacterial Agents.Pharmaceutics · 2023Article
- Cryo-EM of the injectisome and type III secretion systems.Current opinion in structural biology · 2022Review
- Genome analysis and virulence gene expression profile of a multi drug resistant Salmonella enterica serovar Typhimurium ms202.Gut pathogens · 2022Article
- Cryo-EM structure of the needle filament tip complex of theProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Type 3 secretion system 1 of Salmonella typhimurium and its inhibitors: a novel strategy to combat salmonellosis.Environmental science and pollution research international · 2021Review
- An antibody targeting type III secretion system induces broad protection against Salmonella and Shigella infections.PLoS neglected tropical diseases · 2021Article
- Type three secretion system in Salmonella Typhimurium: the key to infection.Genes & genomics · 2020Review
- Review
- The type III secretion system needle, tip, and translocon.Protein science : a publication of the Protein Society · 2019Review
- Association of Salmonella virulence factor alleles with intestinal and invasive serovars.BMC genomics · 2019Article
- The Injectisome, a Complex Nanomachine for Protein Injection into Mammalian Cells.EcoSal Plus · 2019Review
- Review
- Bacterial type III secretion systems: a complex device for the delivery of bacterial effector proteins into eukaryotic host cells.FEMS microbiology letters · 2018Review
- Single-domain antibodies pinpoint potential targets withinThe Journal of biological chemistry · 2017Article
- Characterization of Small-Molecule Scaffolds That Bind to the Shigella Type III Secretion System Protein IpaD.ChemMedChem · 2017Article
- Acylation of the Type 3 Secretion System Translocon Using a Dedicated Acyl Carrier Protein.PLoS genetics · 2017Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many infectious gram-negative bacteria, including Salmonella typhimurium, require a Type Three Secretion System (T3SS) to translocate virulence factors into host cells. The T3SS consists of a membrane protein complex and an extracellular needle together that form a continuous channel. Regulated secretion of virulence factors requires the presence of SipD at the T3SS needle tip in S. typhimurium. Here we report three-dimensional structures of individual SipD, SipD in fusion with the needle subunit PrgI, and of SipD:PrgI in complex with the bile salt, deoxycholate. Assembly of the complex involves major conformational changes in both SipD and PrgI. This rearrangement is mediated via a π bulge in the central SipD helix and is stabilized by conserved amino acids that may allow for specificity in the assembly and composition of the tip proteins. Five copies each of the needle subunit PrgI and SipD form the T3SS needle tip complex. Using surface plasmon resonance spectroscopy and crystal structure analysis we found that the T3SS needle tip complex binds deoxycholate with micromolar affinity via a cleft formed at the SipD:PrgI interface. In the structure-based three-dimensional model of the T3SS needle tip, the bound deoxycholate faces the host membrane. Recently, binding of SipD with bile salts present in the gut was shown to impede bacterial infection. Binding of bile salts to the SipD:PrgI interface in this particular arrangement may thus inhibit the T3SS function. The structures presented in this study provide insight into the open state of the T3SS needle tip. Our findings present the atomic details of the T3SS arrangement occurring at the pathogen-host interface.
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