ArticleBiochemistry2013
N-terminus of IpaB provides a potential anchor to the Shigella type III secretion system tip complex protein IpaD.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 34 citations in OpenAlex.
- Multifunctional antibody responses from a primateScience translational medicine · 2026Article
- Protective and pathogenic antibody responses from a primate Shigella outbreak inform vaccine design.bioRxiv : the preprint server for biology · 2025Article
- The sequence of events of enteropathogeniciScience · 2024Article
- Toward aInternational journal of molecular sciences · 2023Review
- Transmembrane substrates of type three secretion system injectisomes.Microbiology (Reading, England) · 2023Review
- Characterization of Functional B-Cell Epitopes at the Amino Terminus ofApplied and environmental microbiology · 2022Article
- Phosphomimetic Tyrosine Mutations in Spa47 Inhibit Type Three Secretion ATPase Activity andPathogens (Basel, Switzerland) · 2022Article
- 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
- The T3SS ofMicroorganisms · 2020Review
- Interfacial amino acids support Spa47 oligomerization and shigella type three secretion system activation.Proteins · 2019Article
- The type III secretion system needle, tip, and translocon.Protein science : a publication of the Protein Society · 2019Review
- Shutting Down Shigella Secretion: Characterizing Small Molecule Type Three Secretion System ATPase Inhibitors.Biochemistry · 2018Article
- Using disruptive insertional mutagenesis to identify the in situ structure-function landscape of the Shigella translocator protein IpaB.Protein science : a publication of the Protein Society · 2018Article
- MxiN Differentially Regulates Monomeric and Oligomeric Species of the Shigella Type Three Secretion System ATPase Spa47.Biochemistry · 2018Article
- In silico design of a novel chimeric shigella IpaB fused to C terminal of clostridium perfringens enterotoxin as a vaccine candidate.Bioengineered · 2018Article
- 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
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
The type III secretion system (T3SS) is an essential virulence factor for Shigella flexneri , providing a conduit through which host-altering effectors are injected directly into a host cell to promote uptake. The type III secretion apparatus (T3SA) is composed of a basal body, external needle, and regulatory tip complex. The nascent needle is a polymer of MxiH capped by a pentamer of invasion plasmid antigen D (IpaD). Exposure to bile salts (e.g., deoxycholate) causes a conformational change in IpaD and promotes recruitment of IpaB to the needle tip. It has been proposed that IpaB senses contact with host cell membranes, recruiting IpaC and inducing full secretion of T3SS effectors. Although the steps of T3SA maturation and their external triggers have been identified, details of specific protein interactions and mechanisms have remained difficult to study because of the hydrophobic nature of the IpaB and IpaC translocator proteins. Here, we explored the ability for a series of soluble N-terminal IpaB peptides to interact with IpaD. We found that DOC is required for the interaction and that a region of IpaB between residues 11-27 is required for maximum binding, which was confirmed in vivo. Furthermore, intramolecular FRET measurements indicated that movement of the IpaD distal domain away from the protein core accompanied the binding of IpaB11-226. Together, these new findings provide important new insight into the interactions and potential mechanisms that define the maturation of the Shigella T3SA needle tip complex and provide a foundation for further studies probing T3SS activation.
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