ArticleJournal of bacteriology2009
Contribution of the periplasmic chaperone Skp to efficient presentation of the autotransporter IcsA on the surface of Shigella flexneri.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
What it found
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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
36 citing papers in PubMed.
- SurA-like and Skp-like Proteins as Important Virulence Determinants of the Gram Negative Bacterial Pathogens.International journal of molecular sciences · 2022Review
- The periplasmic chaperone Skp prevents misfolding of the secretory lipase A fromFrontiers in molecular biosciences · 2022Article
- Affinity of Skp to OmpC revealed by single-molecule detection.Scientific reports · 2020Article
- Serine Protease Autotransporters of theMicroorganisms · 2019Review
- Article
- The Shigella Virulence Factor IcsA Relieves N-WASP Autoinhibition by Displacing the Verprolin Homology/Cofilin/Acidic (VCA) Domain.The Journal of biological chemistry · 2017Article
- Bacterial Secretion Systems: An Overview.Microbiology spectrum · 2016Review
- Outer membrane protein biogenesis in Gram-negative bacteria.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- Article
- Article
- An alternative outer membrane secretion mechanism for an autotransporter protein lacking a C-terminal stable core.Molecular microbiology · 2013Article
- Role for Skp in LptD assembly in Escherichia coli.Journal of bacteriology · 2013Article
- Functional heterogeneity of the UpaH autotransporter protein from uropathogenic Escherichia coli.Journal of bacteriology · 2012Article
- Shigella flexneri effectors OspE1 and OspE2 mediate induced adherence to the colonic epithelium following bile salts exposure.Molecular microbiology · 2012Article
- VirK is a periplasmic protein required for efficient secretion of plasmid-encoded toxin from enteroaggregative Escherichia coli.Infection and immunity · 2012Article
- The Skp chaperone helps fold soluble proteins in vitro by inhibiting aggregation.Biochemistry · 2012Article
- Functional cell surface display and controlled secretion of diverse Agarolytic enzymes by Escherichia coli with a novel ligation-independent cloning vector based on the autotransporter YfaL.Applied and environmental microbiology · 2012Article
- Dissecting the Escherichia coli periplasmic chaperone network using differential proteomics.Proteomics · 2012Article
- Characterization of Esterase A, a Pseudomonas stutzeri A15 Autotransporter.Applied and environmental microbiology · 2012Article
- The Bam machine: a molecular cooper.Biochimica et biophysica acta · 2012Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
IcsA is an outer membrane protein in the autotransporter family that is required for Shigella flexneri pathogenesis. Following its secretion through the Sec translocon, IcsA is incorporated into the outer membrane in a process that depends on YaeT, a component of an outer membrane beta-barrel insertion machinery. We investigated the role of the periplasmic chaperone Skp in IcsA maturation. Skp is required for the presentation of the mature amino terminus (alpha-domain) of IcsA on the bacterial surface and contributes to cell-to-cell spread of S. flexneri in cell culture. A mutation in skp does not prevent the insertion of the beta-barrel into the outer membrane, suggesting that the primary role of Skp is the folding of the IcsA alpha-domain. In addition, the requirement for skp can be partially bypassed by disrupting icsP, an ortholog of Escherichia coli ompT, which encodes the protease that processes IcsA between the mature amino terminus and the beta-barrel outer membrane anchor. These findings are consistent with a model in which Skp plays a critical role in the chaperoning of the alpha-domain of IcsA during transit through the periplasm.
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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.