ArticleJournal of bacteriology2007
IcsA surface presentation in Shigella flexneri requires the periplasmic chaperones DegP, Skp, and SurA.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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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.
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Who cites it
64 citing papers in PubMed.
- Mutations affecting the β-sheet at the extracellular opening of the intimin β-barrel domain lead to reduced protein levels and inefficient passenger secretion.Bioscience reports · 2026Article
- Insights into the complex formation of a trimeric autotransporter adhesin with a peptidoglycan-binding periplasmic protein.Cell surface (Amsterdam, Netherlands) · 2025Article
- The serine protease HtrA regulates Group B Streptococcus virulence and affects the host response to infection.PLoS pathogens · 2025Article
- Intricate Structure-Function Relationships: The Case of the HtrA Family Proteins from Gram-Negative Bacteria.International journal of molecular sciences · 2024Review
- Dual client binding sites in the ATP-independent chaperone SurA.Nature communications · 2024Article
- (p)ppGpp is required for virulence ofInfection and immunity · 2024Article
- Identification and characterization of a novel lytic peptidoglycan transglycosylase (MltC) in Shigella dysenteriae.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Article
- Toward aInternational journal of molecular sciences · 2023Review
- SurA-like and Skp-like Proteins as Important Virulence Determinants of the Gram Negative Bacterial Pathogens.International journal of molecular sciences · 2022Review
- Cysteine-Dependent Conformational Heterogeneity of Shigella flexneri Autotransporter IcsA and Implications of Its Function.Microbiology spectrum · 2022Article
- The periplasmic chaperone Skp prevents misfolding of the secretory lipase A fromFrontiers in molecular biosciences · 2022Article
- Shigella flexneri Diguanylate Cyclases Regulate Virulence.Journal of bacteriology · 2021Article
- Competing stress-dependent oligomerization pathways regulate self-assembly of the periplasmic protease-chaperone DegP.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Folding Control in the Path of Type 5 Secretion.Toxins · 2021Review
- Identifying virulence determinants of multidrug-resistant Klebsiella pneumoniae in Galleria mellonella.Pathogens and disease · 2021Article
- A novel FRET peptide assay reveals efficient Helicobacter pylori HtrA inhibition through zinc and copper binding.Scientific reports · 2020Article
- Differential gene expression profile ofFuture science OA · 2020Article
- Proteomic profiling ofBioImpacts : BI · 2020Article
- Serine Protease Autotransporters of theMicroorganisms · 2019Review
- Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
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3 authors.
Funding
Abstract
A Shigella flexneri degP mutant, which was defective for plaque formation in Henle cell monolayers, had a reduced amount of IcsA detectable on the bacterial surface with antibody. However, the mutant secreted IcsA to the outer membrane at wild-type levels. This suggests that IcsA adopts an altered conformation in the outer membrane of the degP mutant with reduced exposure on the cell surface. IcsA is, therefore, unlikely to be accessible to actin-nucleating proteins within the eukaryotic cell cytoplasm, which is required for bacterial movement within the host cell and cell-to-cell spread. The degP mutant was somewhat more sensitive to detergents, antibiotics, and the antimicrobial peptide magainin, indicating that the degP phenotype was not limited to IcsA surface presentation. The plaque defect of the degP mutant, which is independent of DegP protease activity, was suppressed by overexpression of the periplasmic chaperone Skp but not by SurA. S. flexneri skp and surA mutants failed to form plaques in Henle cell monolayers and were defective in cell surface presentation and polar localization of IcsA. Therefore, the three periplasmic folding factors DegP, Skp, and SurA were all required for IcsA localization and plaque formation by S. flexneri.
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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.