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1996
Anthrax is a disease known since antiquity1 and one of the first bacterial infections whose etiology was definitively established. The disease is caused by the Gram-positive, aerobic, spore-forming Bacillus anthracis, first isolated in 1877 by Robert Koch.2 The study of anthrax led to the establishment of Koch’s postulates, a set of criteria for ...
Carlo Petosa, Robert C. Liddington
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Anthrax is a disease known since antiquity1 and one of the first bacterial infections whose etiology was definitively established. The disease is caused by the Gram-positive, aerobic, spore-forming Bacillus anthracis, first isolated in 1877 by Robert Koch.2 The study of anthrax led to the establishment of Koch’s postulates, a set of criteria for ...
Carlo Petosa, Robert C. Liddington
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The roles of anthrax toxin in pathogenesis
Current Opinion in Microbiology, 2004Anthrax lethal toxin is a multi-functional virulence factor that has evolved to target multiple host functions to allow for optimal establishment of Bacillus anthracis infection. The toxin appears to play a role in all stages of infection, from germination to the induction of vascular collapse leading to host death.
Mahtab, Moayeri, Stephen H, Leppla
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Anthrax toxin receptor proteins
Biochemical Pharmacology, 2003Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. Here we discuss what is known about the anthrax toxin receptor (ATR), the cellular receptor for anthrax toxin, and how this information is being used to develop treatments for anthrax as well as to understand aspects of cancer. ATR was identified recently as
Kenneth A, Bradley, John A T, Young
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Stoichiometry of Anthrax Toxin Complexes
Biochemistry, 2001After being proteolytically activated, the protective antigen (PA) moiety of anthrax toxin self-associates to form symmetric, ring-shaped heptamers. Heptameric PA competitively binds the enzymatic moieties of the toxin, edema factor and lethal factor, and translocates them across the endosomal membrane by a pH-dependent process. We used two independent
Jeremy, Mogridge +2 more
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2004
Bacillus anthracis, the etiological agent of anthrax, secretes three polypeptides that assemble into toxic complexes on the cell surfaces of the host it infects. One of these polypeptides, protective antigen (PA), binds to the integrin-like domains of ubiquitously expressed membrane proteins of mammalian cells.
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Bacillus anthracis, the etiological agent of anthrax, secretes three polypeptides that assemble into toxic complexes on the cell surfaces of the host it infects. One of these polypeptides, protective antigen (PA), binds to the integrin-like domains of ubiquitously expressed membrane proteins of mammalian cells.
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Structure and Function of Anthrax Toxin
2002Anthrax toxin is a binary A-B toxin comprised of protective antigen (PA) and two enzymatic moieties, edema factor (EF) and lethal factor (LF). In the presence of a host cell-surface receptor, PA can mediate the delivery of EF and LF from the extracellular milieu into the host cell cytosol to effect toxicity.
D B, Lacy, R J, Collier
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Comptes rendus des seances de la Societe de biologie et de ses filiales, 1998
Bacillus anthracis, a Gram positive bacterium, is the causative agent of anthrax. This organism is capsulogen and toxinogenic. It secretes two toxins which are composed of three proteins: the protective antigen (PA), the lethal factor (LF) and the edema factor (EF). The lethal toxin (PA + LF) provokes a subite death in animals, the edema toxin (PA + EF)
F, Brossier, C, Guidi-Rontani, M, Mock
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Bacillus anthracis, a Gram positive bacterium, is the causative agent of anthrax. This organism is capsulogen and toxinogenic. It secretes two toxins which are composed of three proteins: the protective antigen (PA), the lethal factor (LF) and the edema factor (EF). The lethal toxin (PA + LF) provokes a subite death in animals, the edema toxin (PA + EF)
F, Brossier, C, Guidi-Rontani, M, Mock
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Designing a polyvalent inhibitor of anthrax toxin
Nature Biotechnology, 2001Screening peptide libraries is a proven strategy for identifying inhibitors of protein-ligand interactions. Compounds identified in these screens often bind to their targets with low affinities. When the target protein is present at a high density on the surface of cells or other biological surfaces, it is sometimes possible to increase the biological ...
M, Mourez +7 more
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Evidence for adjuvanticity of anthrax edema toxin
Vaccine, 2006Bacillus anthracis edema factor (EF) is an adenylate cyclase that increases intracellular cAMP concentrations. Since EF is present as a contaminant in the licensed protective antigen(PA)-based vaccines, we investigated its effect on anti-PA humoral immune response in BALB/c mice.
Anne, Quesnel-Hellmann +3 more
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Three steps to targeting anthrax toxin
Trends in Molecular Medicine, 2002Anthrax toxin is responsible for the severe symptoms and death associated with inhalational anthrax (Fig. 1Fig. 1). Inhaled Bacillus anthracis spores are phagocytosed by macrophages, transported to the lymph nodes where germination occurs up to 60days later, and the new vegetative bacteria produce the toxin.
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