ArticleInfection and immunity2012
Role of CD11b/CD18 in the process of intoxication by the adenylate cyclase toxin of Bordetella pertussis.
Article in Infection and immunity, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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.
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Who cites it
17 citing papers in PubMed, 26 citations in OpenAlex.
- Article
- Phagocytosis via complement receptor 3 enables microbes to evade killing by neutrophils.Journal of leukocyte biology · 2023Article
- Involvement of Bacterial Extracellular Membrane Nanovesicles in Infectious Diseases and Their Application in Medicine.Pharmaceutics · 2022Review
- Bordetella pertussis Adenylate Cyclase Toxin Disrupts Functional Integrity of Bronchial Epithelial Layers.Infection and immunity · 2018Article
- Understanding the Mechanism of Translocation of Adenylate Cyclase Toxin across Biological Membranes.Toxins · 2017Review
- Phospholipase A activity of adenylate cyclase toxin mediates translocation of its adenylate cyclase domain.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Albumin, in the Presence of Calcium, Elicits a Massive Increase in Extracellular Bordetella Adenylate Cyclase Toxin.Infection and immunity · 2017Article
- Bordetella adenylate cyclase toxin interacts with filamentous haemagglutinin to inhibit biofilm formation in vitro.Molecular microbiology · 2017Article
- Rediscovering Pertussis.Frontiers in pediatrics · 2016Review
- Bacterial Toxins as Pathogen Weapons Against Phagocytes.Frontiers in microbiology · 2016Review
- Adenylate Cyclase Toxin promotes bacterial internalisation into non phagocytic cells.Scientific reports · 2015Article
- The Bordetella adenylate cyclase repeat-in-toxin (RTX) domain is immunodominant and elicits neutralizing antibodies.The Journal of biological chemistry · 2015Article
- Cyclic AMP-mediated suppression of neutrophil extracellular trap formation and apoptosis by the Bordetella pertussis adenylate cyclase toxin.Infection and immunity · 2014Article
- Bordetella pertussis adenylate cyclase toxin translocation across a tethered lipid bilayer.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Article
- Calpain-Mediated Processing of Adenylate Cyclase Toxin Generates a Cytosolic Soluble Catalytically Active N-Terminal Domain.PloS one · 2013Article
- Delivery of Bordetella pertussis adenylate cyclase toxin to target cells via outer membrane vesicles.FEBS letters · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The adenylate cyclase toxin (ACT) of Bordetella pertussis does not require a receptor to generate intracellular cyclic AMP (cAMP) in a broad range of cell types. To intoxicate cells, ACT binds to the cell surface, translocates its catalytic domain across the cell membrane, and converts intracellular ATP to cAMP. In cells that express the integrin CD11b/CD18 (CR3), ACT is more potent than in CR3-negative cells. We find, however, that the maximum levels of cAMP accumulation inside CR3-positive and -negative cells are comparable. To better understand how CR3 affects the generation of cAMP, we used Chinese hamster ovary and K562 cells transfected to express CR3 and examined the steps in intoxication in the presence and absence of the integrin. The binding of ACT to cells is greater in CR3-expressing cells at all concentrations of ACT, and translocation of the catalytic domain is enhanced by CR3 expression, with ∼80% of ACT molecules translocating their catalytic domain in CR3-positive cells but only 25% in CR3-negative cells. Once in the cytosol, the unregulated catalytic domain converts ATP to cAMP, and at ACT concentrations >1,000 ng/ml, the intracellular ATP concentration is <5% of that in untreated cells, regardless of CR3 expression. This depletion of ATP prevents further production of cAMP, despite the CR3-mediated enhancement of binding and translocation. In addition to characterizing the effects of CR3 on the actions of ACT, these data show that ATP consumption is yet another concentration-dependent activity of ACT that must be considered when studying how ACT affects target cells.
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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.