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Open AccessJournal ArticleDOI

Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells.

Stephen H. Leppla
- 01 May 1982 - 
- Vol. 79, Iss: 10, pp 3162-3166
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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.

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Dissertation

Mechanisms of action of the Pseudomonas aeruginosa type III secreted toxins

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Journal ArticleDOI

Pathogenic Bacilli as an Emerging Biothreat?

TL;DR: It is important to improve the knowledge of the phylogeny within the B. cereus sensu lato group to better understand the origin of emerging strains of Bacillus cereus and more efficiently monitor the emergence of new strains to better control the risk of infection and limit potentially malicious uses.
Dissertation

Biotechnological and clinical potential of AIP56 toxin

TL;DR: The present project was aimed at producing AIP56 chimeric proteins that could be directed to cells other than macrophages through replacing the Aip56 receptor-binding domain by protein ligands, whose receptors are over-expressed in cancer cells, and thus, promoting specific targeting, internalization, and intoxication towards determined cancer cells.
Book ChapterDOI

The endothelial cytoskeleton: Multifunctional role of the endothelial actomyosin cytoskeleton

TL;DR: Garcia et al. as discussed by the authors showed that the mammalian cytoskeleton plays an essential role in providing the mechanical support necessary to maintain cell shape, cell motility and movement and in signaling transducing functions.
References
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Journal Article

Protein Measurement with the Folin Phenol Reagent

TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
Journal ArticleDOI

Restoration of Several Morphological Characteristics of Normal Fibroblasts in Sarcoma Cells Treated with Adenosine-3':5'-Cyclic Monophosphate and Its Derivatives

TL;DR: The data suggest that cyclic AMP may be an important factor in the determination of morphology of normal fibroblasts and this function may be lost or altered during transformation.
Journal ArticleDOI

Activation of adenylate cyclase by choleragen.

J Moss, +1 more
TL;DR: An attempt is made to evaluate the mechanism of action of NAD Glycohydrolase and ADP-Ribosyltransferase on GTP-Binding Protein and GTPase Activity in response to the presence of Gangliosides and Their Oligosaccharides in Choleragen.
Journal ArticleDOI

A Permeability Factor (Toxin) found in Cholera Stools and Culture Filtrates and its Neutralization by Convalescent Cholera Sera.

TL;DR: A Permeability Factor (Toxin) found in Cholera Stools and Culture Filtrates and its Neutralization by Convalescent CholERA Sera is found to be neutralized by convalescent cholera patients.
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