Bacillus Anthracis

The bacteria Bacillus anthracis, the etiologic agent of Anthrax, is a large, gram positive, sporulating rod. Approximately 2-6 µm in length, this bacterium can be cultivated in ordinary nutrient medium under aerobic or anaerobic conditions. More commonly recognized by the name Anthrax, this bacterial pathogen is primarily a disease of domesticated and wild animals, particularly herbivorous animals, such as cattle, sheep, horses, mules, and goats. Humans become infected incidentally when brought into contact with diseased animals, which includes their flesh, bones, hides, hair and excrement. Recent bio-terrorism events in history dictate the necessity for a complete understanding of Anthrax and its infectious abilities. Unfortunately, the road to such discovery is long and arduous.

The virulence of Anthrax depends on two factors: the bacterial capsule and the toxin complex. All virulent strains of B. anthracis form a single antigenic type of capsule consisting of a poly-D-glutamate polypeptide. The unusual poly-D-glutamyl acid capsule is itself nontoxic, but functions to protect the organism against the bactericidal components of serum and phagocytes and against phagocytic engulfment. Capsule production depends on a 60-m

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Upon endocytic uptake, the protective antigen undergoes an acid-triggered conformational rearrangement that mediates the transfer of the lethal factor from the lumen of a late endocytic compartment to the cytoplasm. In addition, they showed that cleavage of map kinase kinase 3 — a target of LeTx proteolysis — still occurs in resistant cells.

Since the lethal factor is not as well understood, it has been the focus of many recent works.

Much of the research completed on B. The protective antigen binds to a ubiquitous receptor on the plasma membrane and is processed proteolytically by membrane peptidases, including furin, to a 63kDa form that is able to oligomerize and bind the lethal factor.

The Anthrax toxins are composed of three proteins: the protective antigen, the lethal factor and the edema factor. Once bound, a 20-kd fragment is proteolysed, thus exposing an additional binding site. Macrophage cells sample the environment within us, identify bacteria and viruses, and produce signals that can activate the immune system. The group also showed that Kif1C, a kinesin-like motor protein, is responsible for the differences in susceptibility to Anthrax and protects macrophages from LeTx. Additionally, cytokine production and consequent pathologies showed partial dependence on macrophage ROIs. It has beneficial effects on menopausal symptoms and blood clotting. anthracis germination in a murine inhalation infection model. Also, cultured blood monocyte-derived macrophages from a patient with Chronic Granulomatous Disease, a disorder in which the phagocyte's oxidative burst is disabled, were totally resistant to toxin, in contrast to control monocytes.

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