ArticleInfection and immunity2010
Domains of the Shigella flexneri type III secretion system IpaB protein involved in secretion regulation.
Article in Infection and immunity, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 40 citations in OpenAlex.
- Development of a visual Adhesion/Invasion Inhibition Assay to assess the functionality ofFrontiers in immunology · 2024Article
- Functional assays to evaluate antibody-mediated responses againstFrontiers in cellular and infection microbiology · 2023Review
- Characterization of Functional B-Cell Epitopes at the Amino Terminus ofApplied and environmental microbiology · 2022Article
- Efficient production of immunologically active Shigella invasion plasmid antigens IpaB and IpaH using a cell-free expression system.Applied microbiology and biotechnology · 2022Article
- 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
- TheMicroorganisms · 2021Review
- 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 type III secretion system needle, tip, and translocon.Protein science : a publication of the Protein Society · 2019Review
- In silico design of a novel chimeric shigella IpaB fused to C terminal of clostridium perfringens enterotoxin as a vaccine candidate.Bioengineered · 2018Article
- Steps for Shigella Gatekeeper Protein MxiC Function in Hierarchical Type III Secretion Regulation.The Journal of biological chemistry · 2017Article
- Genetic Dissection of the Signaling Cascade that Controls Activation of the Shigella Type III Secretion System from the Needle Tip.Scientific reports · 2016Article
- Characterization of the Shigella and Salmonella Type III Secretion System Tip-Translocon Protein-Protein Interaction by Paramagnetic Relaxation Enhancement.Chembiochem : a European journal of chemical biology · 2016Article
- The Many Faces of IpaB.Frontiers in cellular and infection microbiology · 2016Review
- MxiA, MxiC and IpaD Regulate Substrate Selection and Secretion Mode in the T3SS of Shigella flexneri.PloS one · 2016Article
- Reassessment of MxiH subunit orientation and fold within native Shigella T3SS needles using surface labelling and solid-state NMR.Journal of structural biology · 2015Article
- Co-administration of rIpaB domain of Shigella with rGroEL of S. Typhi enhances the immune responses and protective efficacy against Shigella infection.Cellular & molecular immunology · 2015Article
- Type III secretion systems: the bacterial flagellum and the injectisome.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- Engineered nanoparticles mimicking cell membranes for toxin neutralization.Advanced drug delivery reviews · 2015Review
- Three-dimensional electron microscopy reconstruction and cysteine-mediated crosslinking provide a model of the type III secretion system needle tip complex.Molecular microbiology · 2015Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Type III secretion systems (T3SSs) are key determinants of virulence in many Gram-negative bacterial pathogens. Upon cell contact, they inject effector proteins directly into eukaryotic cells through a needle protruding from the bacterial surface. Host cell sensing occurs through a distal needle "tip complex," but how this occurs is not understood. The tip complex of quiescent needles is composed of IpaD, which is topped by IpaB. Physical contact with host cells initiates secretion and leads to assembly of a pore, formed by IpaB and IpaC, in the host cell membrane, through which other virulence effector proteins may be translocated. IpaB is required for regulation of secretion and may be the host cell sensor. It binds needles via its extreme C-terminal coiled coil, thereby likely positioning a large domain containing its hydrophobic regions at the distal tips of needles. In this study, we used short deletion mutants within this domain to search for regions of IpaB involved in secretion regulation. This identified two regions, amino acids 227 to 236 and 297 to 306, the presence of which are required for maintenance of IpaB at the needle tip, secretion regulation, and normal pore formation but not invasion. We therefore propose that removal of either of these regions leads to an inability to block secretion prior to reception of the activation signal and/or a defect in host cell sensing.
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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.