ArticleBiophysical journal2011
Induced conformational changes in the activation of the Pseudomonas aeruginosa type III toxin, ExoU.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 18 citations in OpenAlex.
- Patatin-domain-containing (phospho)lipases under control: Mammalian co-regulators and pathogenic activation mechanisms.FEBS open bio · 2026Review
- Site-directed spin label EPR studies of the structure and membrane interactions of the bacterial phospholipase ExoU.Applied magnetic resonance · 2024Article
- Engineering white blood cell membrane-camouflaged nanocarriers for inflammation-related therapeutics.Bioactive materials · 2023Review
- Perspectives on theToxins · 2021Review
- A pipeline to evaluate inhibitors of the Pseudomonas aeruginosa exotoxin U.The Biochemical journal · 2021Article
- Conformational Changes and Membrane Interaction of the Bacterial Phospholipase, ExoU: Characterization by Site-Directed Spin Labeling.Cell biochemistry and biophysics · 2019Article
- Identification of a ubiquitin-binding interface using Rosetta and DEER.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Phosphatidylinositol 4,5-Bisphosphate-Dependent Oligomerization of the Pseudomonas aeruginosa Cytotoxin ExoU.Infection and immunity · 2018Article
- Article
- Cooperative Substrate-Cofactor Interactions and Membrane Localization of the Bacterial Phospholipase AThe Journal of biological chemistry · 2017Article
- Association between Pseudomonas aeruginosa type III secretion, antibiotic resistance, and clinical outcome: a review.Critical care (London, England) · 2014Review
- Identification of the major ubiquitin-binding domain of the Pseudomonas aeruginosa ExoU A2 phospholipase.The Journal of biological chemistry · 2013Article
- Structure of the type III secretion effector protein ExoU in complex with its chaperone SpcU.PloS one · 2012Article
- Structural basis of cytotoxicity mediated by the type III secretion toxin ExoU from Pseudomonas aeruginosa.PLoS pathogens · 2012Article
- Ubiquitin and ubiquitin-modified proteins activate the Pseudomonas aeruginosa T3SS cytotoxin, ExoU.Molecular microbiology · 2011Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
ExoU is a 74-kDa, water-soluble toxin injected directly into mammalian cells through the type III secretion system of the opportunistic pathogen, Pseudomonas aeruginosa. Previous studies have shown that ExoU is a Ca(2+)-independent phospholipase that requires a eukaryotic protein cofactor. One protein capable of activating ExoU and serving as a required cofactor was identified by biochemical and proteomic methods as superoxide dismutase (SOD1). In these studies, we carried out site-directed spin-labeling electron paramagnetic resonance spectroscopy to examine the effects of SOD1 and substrate liposomes on the structure and dynamics of ExoU. Local conformational changes within the catalytic site were observed in the presence of substrate liposomes, and were enhanced by the addition of SOD1 in a concentration-dependent manner. Conformational changes in the C-terminal domain of ExoU were observed upon addition of cofactor, even in the absence of liposomes. Double electron-electron resonance experiments indicated that ExoU samples multiple conformations in the resting state. In contrast, addition of SOD1 induced ExoU to adopt a single, well-defined conformation. These studies provide, to our knowledge, the first direct evidence for cofactor- and membrane-induced conformational changes in the mechanism of activation of ExoU.
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