ArticleProtein science : a publication of the Protein Society2013
Oligomeric states of the Shigella translocator protein IpaB provide structural insights into formation of the type III secretion translocon.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed.
- Computational structural dynamics and immunoinformatic analysis of EIEC IpaHMolecular diversity · 2026Article
- Development of a NovelVaccines · 2026Article
- The bacterial type three secretion system induces mechanoporation of vacuolar membranes.PLoS biology · 2025Article
- Pathogenicity and virulence ofVirulence · 2023Review
- A NovelmSphere · 2023Article
- Article
- Review
- Phosphomimetic Tyrosine Mutations in Spa47 Inhibit Type Three Secretion ATPase Activity andPathogens (Basel, Switzerland) · 2022Article
- Efficient production of immunologically active Shigella invasion plasmid antigens IpaB and IpaH using a cell-free expression system.Applied microbiology and biotechnology · 2022Article
- TheMicroorganisms · 2021Review
- Structural Insights ofFrontiers in cellular and infection microbiology · 2021Article
- Type three secretion system in Salmonella Typhimurium: the key to infection.Genes & genomics · 2020Review
- Development of a Broadly Protective, Self-Adjuvanting Subunit Vaccine to Prevent Infections byFrontiers in immunology · 2020Article
- The cytoplasmic domain of MxiG interacts with MxiK and directs assembly of the sorting platform in theThe Journal of biological chemistry · 2019Article
- In-silico design and production of a novel antigenic chimeric Shigella IpaB fused to C-terminal of Clostridium perfringens enterotoxin.Molecular biology reports · 2019Article
- The cytoplasmic portion of the T3SS inner membrane ring components sort into distinct families based on biophysical properties.Biochimica et biophysica acta. Proteins and proteomics · 2019Article
- Bacterial type III secretion systems: a complex device for the delivery of bacterial effector proteins into eukaryotic host cells.FEMS microbiology letters · 2018Review
- 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
- Characterization and Protective Efficacy of Type III Secretion Proteins as a Broadly Protective Subunit Vaccine against Salmonella enterica Serotypes.Infection and immunity · 2018Article
- Deoxycholate-Enhanced Shigella Virulence Is Regulated by a Rare π-Helix in the Type Three Secretion System Tip Protein IpaD.Biochemistry · 2017Article
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8 authors.
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Abstract
The Shigella flexneri Type III secretion system (T3SS) senses contact with human intestinal cells and injects effector proteins that promote pathogen entry as the first step in causing life threatening bacillary dysentery (shigellosis). The Shigella Type III secretion apparatus (T3SA) consists of an anchoring basal body, an exposed needle, and a temporally assembled tip complex. Exposure to environmental small molecules recruits IpaB, the first hydrophobic translocator protein, to the maturing tip complex. IpaB then senses contact with a host cell membrane, forming the translocon pore through which effectors are delivered to the host cytoplasm. Within the bacterium, IpaB exists as a heterodimer with its chaperone IpgC; however, IpaB's structural state following secretion is unknown due to difficulties isolating stable protein. We have overcome this by coexpressing the IpaB/IpgC heterodimer and isolating IpaB by incubating the complex in mild detergents. Interestingly, preparation of IpaB with n-octyl-oligo-oxyethylene (OPOE) results in the assembly of discrete oligomers while purification in N,N-dimethyldodecylamine N-oxide (LDAO) maintains IpaB as a monomer. In this study, we demonstrate that IpaB tetramers penetrate phospholipid membranes to allow a size-dependent release of small molecules, suggesting the formation of discrete pores. Monomeric IpaB also interacts with liposomes but fails to disrupt them. From these and additional findings, we propose that IpaB can exist as a tetramer having inherent flexibility, which allows it to cooperatively interact with and insert into host cell membranes. This event may then lay the foundation for formation of the Shigella T3SS translocon pore.
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