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
Citations
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Journal ArticleDOI
IgG-Engineered Protective Antigen for Cytosolic Delivery of Proteins into Cancer Cells.
Zeyu Lu,Nicholas L. Truex,Mariane B. Melo,Yiran Cheng,Na Li,Darrell J. Irvine,Bradley L. Pentelute +6 more
TL;DR: In this paper, the authors developed novel immunotoxins by dovetailing full-length immunoglobulin G (IgG) antibodies and nontoxic anthrax proteins, in which the C terminus of the IgG heavy chain is connected to the side chain of anthrax toxin.
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Anthrax lethal factor
TL;DR: This chapter describes the structural chemistry and the biological aspects of anthrax lethal factor, a metalloprotease distantly related to thermolysin, but one with a highly restricted substrate specificity.
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Toxin-neutralizing antibodies elicited by naturally acquired cutaneous anthrax are elevated following severe disease and appear to target conformational epitopes
Eric K. Dumas,Eric K. Dumas,Hayati Demiraslan,Rebecca J. Ingram,Rebecca M Sparks,Emily E. Muns,Adriana Zamora,Jason L. Larabee,Lori Garman,Lori Garman,Jimmy D. Ballard,Geert-Jan Boons,Geert-Jan Boons,Judith A. James,Judith A. James,Uner Kayabas,Mehmet Doganay,A. Darise Farris,A. Darise Farris +18 more
TL;DR: Comparison of serum binding to overlapping decapeptides covering the entire length of PA, LF and EF proteins in 26 cases compared to 8 regional controls revealed that anthrax toxin-neutralizing antibody responses elicited following natural cutaneous anthrax infection are directed to conformational epitopes.
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Epitope-focused peptide immunogens in human use adjuvants protect rabbits from experimental inhalation anthrax.
TL;DR: An LND-specific epitope-focused vaccine may complement PA-based vaccines and may represent a complementary stand-alone vaccine for anthrax.
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Proteomic Studies of Bacillus anthracis Reveal In Vitro CO2-Modulation and Expression During Infection of Extracellular Proteases
Theodor Chitlaru,Orit Gat,Galia Zaide,Haim Grosfeld,Izhak Inbar,Sharon Ehrlich,M Leitner,Ofer Cohen,Avigdor Shafferman +8 more
TL;DR: Data show that distinct CO2/bicarbonate responsive chromosome-and plasmid-encoded regulatory factors modulate the secretion of potential novel virulence factors, most of which are associated with extracellular proteolytic activities.
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