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:Â
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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Anthrax toxin: Pathologic effects on the cardiovascular system
Honey B. Golden,Linley E. Watson,Hind Lal,Suresh K Verma,Donald M. Foster,Shu Ru Kuo,Avadhesh C Sharma,Arthur E. Frankel,David E. Dostal +8 more
TL;DR: The current understanding of anthrax toxins on cellular function in the context of cardiovascular function is described and potential therapeutic strategies are discussed.
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Domain flexibility modulates the heterogeneous assembly mechanism of anthrax toxin protective antigen.
TL;DR: Molecular determinants that influence the stoichiometry of PA in toxin complexes are described and it is proposed that there are different orientations of D4 relative to the main body of PA that favor the formation of either the heptamer or the octamer.
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Proteome analysis of mouse macrophages treated with anthrax lethal toxin
Harish Chandra,Pradeep K. Gupta,Kirti Sharma,Abid R. Mattoo,Satyendra K. Garg,W. N. Gade,Ravi Sirdeshmukh,Kapil Maithal,Yogendra Singh +8 more
TL;DR: Analysis of up- and down-regulated proteins revealed that primarily the stress response and energy generation proteins play an important role in the LT-mediated macrophage cell death.
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A high-throughput screening approach to anthrax lethal factor inhibition.
TL;DR: The identification of new scaffolds that inhibit LF and the Botulinum Neurotoxin Type A in the low micromolar range, while sparing the human metallo-proteases MMP-2 and M MP-9 could be further exploited for the development of potent and selective anti-toxin agents.
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Bordetella pertussis adenylate cyclase. Identification of multiple forms of the enzyme by antibodies.
TL;DR: Polyclonal antibodies raised against the 47-kDa catalyst specifically recognize both forms of the enzyme in purified state as well as in bacterial extracts on immunoblots, and prevents the penetration of the invasive B. pertussis adenylate cyclase into human lymphocytes.
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