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N-fragment of edema factor as a candidate antigen for immunization against anthrax.
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The nontoxic N-terminal fragment of Bacillus anthracis edema factor (EF) was evaluated as a candidate antigen in an anthrax vaccine using a replication-incompetent adenoviral vector. An E1/E3 deleted adenovirus (Ad/EFn) encoding the N-terminal region 1-254 amino acids of the edema factor (EFn) was
The lethal and edema factors of anthrax toxin bind only to oligomeric forms of the protective antigen.
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The three proteins that comprise anthrax toxin, edema factor (EF), lethal factor (LF), and protective antigen (PA), assemble at the mammalian cell surface into toxic complexes. After binding to its receptor, PA is proteolytically activated, yielding a carboxyl-terminal 63-kDa fragment (PA(63)) that
Binding of N-terminal fragments of anthrax edema factor (EF(N)) and lethal factor (LF(N)) to the protective antigen pore.
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Anthrax toxin consists of three different molecules: the binding component protective antigen (PA, 83 kDa), and the enzymatic components lethal factor (LF, 90 kDa) and edema factor (EF, 89 kDa). The 63 kDa C-terminal part of PA, PA(63), forms heptameric channels that insert in endosomal membranes at
In situ gastrointestinal protection against anthrax edema toxin by single-chain antibody fragment producing lactobacilli.
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BACKGROUND
Anthrax is caused by the bacterium Bacillus anthracis and is regarded as one of the most prominent bioterrorism threats. Anthrax toxicity is induced by the tripartite toxin complex, composed of the receptor-binding anthrax protective antigen and the two enzymatic subunits, lethal factor
Emergence of anthrax edema toxin as a master manipulator of macrophage and B cell functions.
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Anthrax edema toxin (ET), a powerful adenylyl cyclase, is an important virulence factor of Bacillus anthracis. Until recently, only a modest amount of research was performed to understand the role this toxin plays in the organism's immune evasion strategy. A new wave of studies have begun to
cAMP imaging of cells treated with pertussis toxin, cholera toxin, and anthrax edema toxin.
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The enzymatic activity of the three most studied bacterial toxins that increase the cytosolic cAMP level: pertussis toxin (PT), cholera toxin (CT), and anthrax edema toxin (ET), was imaged by fluorescence videomicroscopy. Three different cell lines were transfected with a fluorescence resonance
Anthrax toxin complexes: heptameric protective antigen can bind lethal factor and edema factor simultaneously.
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The 83 kDa protective antigen (PA(83)) component of anthrax toxin, after proteolytic activation, self-associates to form ring-shaped heptamers ([PA(63)](7)) that bind and aid delivery of the Edema Factor (EF) and Lethal Factor (LF) components to the cytosol. Here we show using fluorescence (Förster)
The major neutralizing antibody responses to recombinant anthrax lethal and edema factors are directed to non-cross-reactive epitopes.
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Anthrax lethal and edema toxins (LeTx and EdTx, respectively) form by binding of lethal factor (LF) or edema factor (EF) to the pore-forming moiety protective antigen (PA). Immunity to LF and EF protects animals from anthrax spore challenge and neutralizes anthrax toxins. The goal of the present
Inhibition of platelet aggregation by anthrax edema toxin.
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Edema toxin is a key virulence determinant in anthrax pathogenesis that causes augmentation of cAMP inside host cells. This exotoxin has been implicated in facilitating bacterial invasion by impairing host defenses. Here, we report for the first time that edema toxin plays an important role in
Suppression of dendritic cell activation by anthrax lethal toxin and edema toxin depends on multiple factors including cell source, stimulus used, and function tested.
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Bacillus anthracis produces lethal toxin (LT) and edema toxin (ET), and they suppress the function of LPS-stimulated dendritic cells (DCs). Because DCs respond differently to various microbial stimuli, we compared toxin effects in bone marrow DCs stimulated with either LPS or Legionella pneumophila
Transcriptional stimulation of anthrax toxin receptors by anthrax edema toxin and Bacillus anthracis Sterne spore.
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We used quantitative real-time RT-PCR to not only investigate the mRNA levels of anthrax toxin receptor 1 (ANTXR1) and 2 (ANTXR2) in the murine J774A.1 macrophage cells and different tissues of mice, but also evaluate the effect of anthrax edema toxin and Bacillus anthracis Sterne spores on the
In vivo dynamics of active edema and lethal factors during anthrax.
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Lethal and edema toxins are critical virulence factors of Bacillus anthracis. However, little is known about their in vivo dynamics of production during anthrax. In this study, we unraveled for the first time the in vivo kinetics of production of the toxin components EF (edema factor) and LF (lethal
Ratio of lethal and edema factors in rabbit systemic anthrax.
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Bacillus anthracis secretes two binary toxins: lethal toxin (PA + LF) and edema toxin (PA + EF) that play a major role in the pathogenesis of anthrax. Their activities can synergize or interfere among each other, depending on the cell type. It is therefore fundamental to know their concentration
Atomic Structures of Anthrax Prechannel Bound with Full-Length Lethal and Edema Factors
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Pathogenesis of anthrax disease involves two cytotoxic enzymes-edema factor (EF) and lethal factor (LF)-which are individually recruited by the protective antigen heptamer (PA7) or octamer (PA8) prechannel and subsequently translocated across channels formed on the endosomal
[Efficient expression of anthrax edema factor in Escherichia coli and its single-step purification].
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To develop a new method for efficient expression and rapid preparation of biologically active anthrax edema factor (EF).
EF was fused with GST and expressed in the host E. coli BL21-CodonPlus (DE3)-RIL by IPTG induction. The crud protein was extracted by permeabilization, and then EF was purified by
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