ArticleProteins2012
Identification of the bile salt binding site on IpaD from Shigella flexneri and the influence of ligand binding on IpaD structure.
Article in Proteins, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
39 citing papers in PubMed.
- Functional assays to evaluate antibody-mediated responses againstFrontiers in cellular and infection microbiology · 2023Review
- Shigella flexneri Diguanylate Cyclases Regulate Virulence.Journal of bacteriology · 2021Article
- Cryo-EM structure of the needle filament tip complex of theProceedings of the National Academy of Sciences of the United States of America · 2021Article
- An antibody targeting type III secretion system induces broad protection against Salmonella and Shigella infections.PLoS neglected tropical diseases · 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
- Preformulation Characterization and the Effect of Ionic Excipients on the Stability of a Novel DB Fusion Protein.Journal of pharmaceutical sciences · 2021Article
- Antibodies Inhibiting the Type III Secretion System of Gram-Negative Pathogenic Bacteria.Antibodies (Basel, Switzerland) · 2020Review
- Novel Noncompetitive Type Three Secretion System ATPase Inhibitors Shut DownBiochemistry · 2020Article
- The type III secretion system needle, tip, and translocon.Protein science : a publication of the Protein Society · 2019Review
- A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion.PLoS biology · 2019Article
- Review
- Article
- Visualization of the type III secretion mediatedeLife · 2018Article
- Enterobacteria and host resistance to infection.Mammalian genome : official journal of the International Mammalian Genome Society · 2018Review
- Protein-Injection Machines in Bacteria.Cell · 2018Review
- Deoxycholate-Enhanced Shigella Virulence Is Regulated by a Rare π-Helix in the Type Three Secretion System Tip Protein IpaD.Biochemistry · 2017Article
- 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
- Analysis of Shigella flexneri Resistance, Biofilm Formation, and Transcriptional Profile in Response to Bile Salts.Infection and immunity · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
Type III secretion (TTS) is an essential virulence factor for Shigella flexneri, the causative agent of shigellosis. The Shigella TTS apparatus (TTSA) is an elegant nanomachine that is composed of a basal body, an external needle to deliver effectors into human cells, and a needle tip complex that controls secretion activation. IpaD is at the tip of the nascent TTSA needle where it controls the first step of TTS activation. The bile salt deoxycholate (DOC) binds to IpaD to induce recruitment of the translocator protein IpaB into the maturing tip complex. We recently used spectroscopic analyses to show that IpaD undergoes a structural rearrangement that accompanies binding to DOC. Here, we report a crystal structure of IpaD with DOC bound and test the importance of the residues that make up the DOC binding pocket on IpaD function. IpaD binds DOC at the interface between helices α3 and α7, with concomitant movement in the orientation of helix α7 relative to its position in unbound IpaD. When the IpaD residues involved in DOC binding are mutated, some are found to lead to altered invasion and secretion phenotypes. These findings suggest that adoption of a DOC bound structural state for IpaD primes the Shigella TTSA for contact with host cells. The data presented here and in the studies leading up to this work provide the foundation for developing a model of the first step in Shigella TTS activation.
Indexed as
Identifiers
What OpenQuestion holds
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.