Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells.
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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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Dissertation
Structural and stability studies on domain IV of anthrax toxin protective antigen (PA); its role in anthrax pathogenesis
TL;DR: Thesis (Ph.D.) as mentioned in this paper, Wichita State University, College of Liberal Arts and Sciences, Dept. of Chemistry (CLAS), WSU, Wichita, KS.
Book ChapterDOI
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TL;DR: The use of anthrax as a model system dates back to the late 19th century and Koch’s initial investigations into the transmission of infectious diseases enabled him to formulate the first set of rules on infectious diseases.
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Design and use of a novel substrate for simple, rapid, and specific early detection of anthrax infection
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