ArticleJournal of bacteriology2002
Spa32 regulates a switch in substrate specificity of the type III secreton of Shigella flexneri from needle components to Ipa proteins.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 97 citations in OpenAlex.
- Review
- Molecular characterization and in-depth genomic analysis to unravel the pathogenic features of an environmental isolate Enterobacter sp. S-33.International microbiology : the official journal of the Spanish Society for Microbiology · 2024Article
- Genetic code expansion enables visualization ofeLife · 2021Article
- TheMicroorganisms · 2021Review
- The T3SS ofMicroorganisms · 2020Review
- Inactivation of theMicroorganisms · 2020Article
- Genome-wide Analysis of Four Enterobacter cloacae complex type strains: Insights into Virulence and Niche Adaptation.Scientific reports · 2020Article
- Multiple proteins arising from a single gene: The role of the Spa33 variants in Shigella T3SS regulation.MicrobiologyOpen · 2019Article
- The Injectisome, a Complex Nanomachine for Protein Injection into Mammalian Cells.EcoSal Plus · 2019Review
- The inner-rod component of Shigella flexneri type 3 secretion system, MxiI, is involved in the transmission of the secretion activation signal by its interaction with MxiC.MicrobiologyOpen · 2018Article
- Article
- Behind the lines-actions of bacterial type III effector proteins in plant cells.FEMS microbiology reviews · 2016Review
- The Structure and Function of Type III Secretion Systems.Microbiology spectrum · 2016Review
- The Structure of a Type 3 Secretion System (T3SS) Ruler Protein Suggests a Molecular Mechanism for Needle Length Sensing.The Journal of biological chemistry · 2016Article
- Type Three Secretion System in Attaching and Effacing Pathogens.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
- Bacterial iron-sulfur cluster sensors in mammalian pathogens.Metallomics : integrated biometal science · 2015Review
- Shigella type III secretion protein MxiI is recognized by Naip2 to induce Nlrc4 inflammasome activation independently of Pkcδ.PLoS pathogens · 2014Article
- Type III chaperones & Co in bacterial plant pathogens: a set of specialized bodyguards mediating effector delivery.Frontiers in plant science · 2013Review
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Type III secretion systems (TTSS) are essential virulence determinants of many gram-negative bacteria and serve, upon physical contact with target cells, to translocate bacterial proteins directly across eukaryotic cell membranes. The Shigella TTSS is encoded by the mxi/spa loci located on its virulence plasmid. By electron microscopy secretons are visualized as tripartite with an external needle, a transmembrane domain, and a cytoplasmic bulb. In the present study, we generated a Shigella spa32 mutant and studied its phenotype. The spa32 gene shows low sequence homology to Salmonella TTSS1 invJ/spaN and to flagellar fliK. The spa32 mutant, like the wild-type strain, secreted the Ipas and IpgD, which are normally secreted via the TTSS, at low levels into the growth medium. However, unlike the wild-type strain, the spa32 mutant could neither be induced to secrete the Ipas and IpgD instantaneously upon addition of Congo red nor penetrate HeLa cells in vitro. Additionally, the Spa32 protein is secreted in large amounts by the TTSS during exponential growth but not upon Congo red induction. Interestingly, electron microscopy analysis of the spa32 mutant revealed that the needle of its secretons were up to 10 times longer than those of the wild type. In addition, in the absence of induction, the spa32 mutant secreted normal levels of MxiI but a large excess of MxiH. Taken together, our data indicate that the spa32 mutant presents a novel phenotype and that the primary defect of the mutant may be its inability to regulate or control secretion of MxiH.
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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.