ArticleJournal of bacteriology2000
Influence of deletions within domain II of exotoxin A on its extracellular secretion from Pseudomonas aeruginosa.
Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 43 citations in OpenAlex.
- Discovery of mono-ADP ribosylating toxins with high structural homology to Pseudomonas exotoxin A.Communications biology · 2025Article
- Isolation and characterizations of a novel recombinant scFv antibody against exotoxin A of Pseudomonas aeruginosa.BMC infectious diseases · 2021Article
- Bacterial secretins: Mechanisms of assembly and membrane targeting.Protein science : a publication of the Protein Society · 2020Review
- Solving the Puzzle: Connecting a HeterologousFrontiers in cellular and infection microbiology · 2020Article
- Architecture, Function, and Substrates of the Type II Secretion System.EcoSal Plus · 2019Review
- Bacteria-Host Crosstalk: Sensing of the Quorum in the Context of Pseudomonas aeruginosa Infections.Journal of innate immunity · 2019Review
- Conformational determinants necessary for secretion of Paecilomyces thermophila β-1,4-xylosidase that lacks a signal peptide.AMB Express · 2018Article
- The Apoptogenic Toxin AIP56 Is Secreted by the Type II Secretion System of Photobacterium damselae subsp. piscicida.Toxins · 2017Article
- Downsizing a pullulanase to a small molecule with improved soluble expression and secretion efficiency in Escherichia coli.Microbial cell factories · 2016Article
- Pseudomonas Exotoxin A: optimized by evolution for effective killing.Frontiers in microbiology · 2015Review
- Structure of a translocation signal domain mediating conjugative transfer by type IV secretion systems.Molecular microbiology · 2013Article
- Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS.PLoS pathogens · 2013Article
- Type IV pilin proteins: versatile molecular modules.Microbiology and molecular biology reviews : MMBR · 2012Review
- On the path to uncover the bacterial type II secretion system.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- A guide to taming a toxin--recombinant immunotoxins constructed from Pseudomonas exotoxin A for the treatment of cancer.The FEBS journal · 2011Review
- Deciphering the Xcp Pseudomonas aeruginosa type II secretion machinery through multiple interactions with substrates.The Journal of biological chemistry · 2011Article
- Type VI secretion system in Pseudomonas aeruginosa: secretion and multimerization of VgrG proteins.The Journal of biological chemistry · 2011Article
- Protein Secretion Systems in Pseudomonas aeruginosa: An Essay on Diversity, Evolution, and Function.Frontiers in microbiology · 2011Article
- Structure of the cholera toxin secretion channel in its closed state.Nature structural & molecular biology · 2010Article
- Secretion signal and protein targeting in bacteria: a biological puzzle.Journal of bacteriology · 2010Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pseudomonas aeruginosa is a gram-negative bacterium that secretes many proteins into the extracellular medium via the Xcp machinery. This pathway, conserved in gram-negative bacteria, is called the type II pathway. The exoproteins contain information in their amino acid sequence to allow targeting to their secretion machinery. This information may be present within a conformational motif. The nature of this signal has been examined for P. aeruginosa exotoxin A (PE). Previous studies failed to identify a common minimal motif required for Xcp-dependent recognition and secretion of PE. One study identified a motif at the N terminus of the protein, whereas another one found additional information at the C terminus. In this study, we assess the role of the central PE domain II composed of six alpha-helices (A to F). The secretion behavior of PE derivatives, individually deleted for each helix, was analyzed. Helix E deletion has a drastic effect on secretion of PE, which accumulates within the periplasm. The conformational rearrangement induced in this variant is predicted from the three-dimensional PE structure, and the molecular modification is confirmed by gel filtration experiments. Helix E is in the core of the molecule and creates close contact with other domains (I and III). Deletion of the surface-exposed helix F has no effect on secretion, indicating that no secretion information is contained in this helix. Finally, we concluded that disruption of a structured domain II yields an extended form of the molecule and prevents formation of the conformational secretion motif.
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