Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells.
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TLDR
It is shown here that EF is an adenylate cyclase [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1] produced by Bacillus anthracis in an inactive form and nearly equals that of the most active known cyclase.Abstract:
Anthrax toxin is composed of three proteins: protective antigen (PA), lethal factor (LF), and edema factor (EF). These proteins individually cause no known physiological effects in animals but in pairs produce two toxic actions. Injection of PA with LF causes death of rats in 60 min, whereas PA with EF causes edema in the skin of rabbits and guinea pigs. The mechanisms of action of these proteins have not been determined. It is shown here that EF is an adenylate cyclase [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1] produced by Bacillus anthracis in an inactive form. Activation occurs upon contact with a heat-stable eukaryotic cell material. The specific activity of the resulting adenylate cyclase nearly equals that of the most active known cyclase. In Chinese hamster ovary cells exposed to PA and EF, cAMP concentrations increase without a lag to values about 200-fold above normal, remain high in the continued presence of toxin, and decrease rapidly after its removal. The increase in cAMP is completely blocked by excess LF. It is suggested that PA interacts with cells to form a receptor system by which EF and perhaps LF gain access to the cytoplasm.read more
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Journal ArticleDOI
Chemical Dissection of Protein Translocation through the Anthrax Toxin Pore
TL;DR: Edema Factor, the enzymatic moiety of anthrax edema toxin, is transported to the cytosol by a similar mechanism, where it inactivates selected target proteins.
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Tumor Targeting and Drug Delivery by Anthrax Toxin.
TL;DR: The anthrax toxin system has proved to be a versatile system for drug delivery of several enzymatic moieties into cells and has recently been further modified by introducing ubiquitin as a cytosolic cleavage site into lethal factor fusion proteins.
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The cytotoxic activity of Bacillus anthracis lethal factor is inhibited by leukotriene A4 hydrolase and metallopeptidase inhibitors.
TL;DR: Results support the proposal that anthrax lethal factor might display in the cytosol of intoxicated cells a peptidase activity similar to that of LTA4 hydrolase, a bifunctional enzyme also endowed with a metallopeptid enzyme activity.
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An alternative approach to combination vaccines: intradermal administration of isolated components for control of anthrax, botulism, plague and staphylococcal toxic shock
Garry L. Morefield,Ralph Tammariello,Bret K. Purcell,Patricia L. Worsham,Jennifer Chapman,Leonard A. Smith,Jason B. Alarcon,John A. Mikszta,Robert G. Ulrich +8 more
TL;DR: The vaccination method described may be scalable to include a greater number of antigens, while avoiding the physical and chemical incompatibilities encountered by combining multiple vaccines together in one product.
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Binding of 3'-anthraniloyl-2'-deoxy-ATP to calmodulin-activated adenylate cyclase from Bordetella pertussis and Bacillus anthracis.
Robert Sarfati,Vinod K. Kansal,Hélène Munier,Philippe Glaser,Anne-Marie Gilles,Elisabeth Labruyère,Michèle Mock,Antoine Danchin,Octavian Bârzu +8 more
TL;DR: The results substantiate the role of CaM in favoring substrate binding to CaM-activated enzymes as shown by its displacement with ATP or 3'-dATP.
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