Anthrax toxicity

Smith H, Stoner HB. Anthrax toxic complex. Fed Proc 1967 26(5) 1554-1557. 

The recruitment of zinc for a structural role, or to activate an enzyme, has been observed. The zinc ion induces the dimerization of human growth hormone (hGH), with two Zn ions associated per dimer of hGH. This is confirmed by replacement of possible zinc binding residues resulting in weakened binding of the zinc ion. Formation of a zinc-hGH dimeric complex may be important for storage of hGH in secretory granules.975 In a toxic role, anthrax lethal factor is one of the three components of the secreted toxin and is a zinc-dependent protease that cleaves a protein kinase and causes lysis of macrophages.976... 

Suggested Alternatives for Differential Diagnosis Acute respiratory distress syndrome, congestive heart failure, pulmonary edema, AIDS, pneumonia, cardiogenic shock, septic shock, phosgene toxicity, phosphine toxicity, salicylate toxicity with pulmonary edema, influenza, plague, tularemia, and anthrax. 

Suggested Alternatives for Differential Diagnosis Anthrax, brucellosis, dengue, ehrlichiosis, infectious mononucleosis, Kawasaki disease, leptospirosis, malaria, meningitis, men-ingococcemia, relapsing fever, Rocky Mountain spotted fever, syphilis, toxic shock syndrome, toxoplasmosis, tularemia, typhoid fever, rubella, measles. 

In June of 2003, the U.S. Army unearthed 113 bacteria-containing vials, including live strains of brucellosis and non-virulent anthrax, during excavation of its Fort Detrick site to eliminate toxic chemicals and hazardous waste. (Credit The Council for Responsible Genetics)... 

Classical bacterial exotoxins, such as diphtheria toxin, cholera toxin, clostridial neurotoxins, and the anthrax toxins are enzymes that modify their substrates within the cytosol of mammalian cells. To reach the cytosol, these toxins must first bind to different cell-surface receptors and become subsequently internalized by the cells. To this end, many bacterial exotoxins contain two functionally different domains. The binding (B-) domain binds to a cellular receptor and mediates uptake of the enzymatically active (A-) domain into the cytosol, where the A-domain modifies its specific substrate (see Figure 1). Thus, three important properties characterize the mode of action for any AB-type toxin selectivity, specificity, and potency. Because of their selectivity toward certain cell types and their specificity for cellular substrate molecules, most of the individual exotoxins are associated with a distinct disease. Because of their enzymatic nature, placement of very few A-domain molecules in the cytosol will normally cause a cytopathic effect. Therefore, bacterial AB-type exotoxins which include the potent neurotoxins from Clostridium tetani and C. botulinum are the most toxic substances known today. However, the individual AB-type toxins can greatly vary in terms of subunit composition and enzyme activity (see Table 2). 

Industrial processes, such as mUling and mining, construction work, and the burning of wood or fossil fuel, generate particulates that can be directly toxic or can serve as vectors for the transfer of bound material, such as sulfuric acid, metals, and hydrocarbons, into the lungs. Natural products such as pollen, anthrax spores, and animal dander can elicit toxic reactions on inhalation or skin contact. The inhalation of asbestos, silica, or coal dust can cause pneumoconiosis, which may develop into serious lung disease. The size of the particle, ventilatory rate, and depth of breathing will determine the extent of pulmonary deposition. 

Some bacteria produce effects similar to those of cholera toxin in different ways. For example, among a variety of toxic proteins produced by Bacillus anthracis, the causative agent of anthrax, is an adenylate cyclase that is able to enter the host s cells.s Similarly, B. pertussis, in addition to... 

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