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Anthrax infection is initiated by the inhalation, ingestion, or cutaneous contact with Bacillus anthracis endospores. B. anthracis produces three polypeptides that comprise the anthrax toxin: protective antigen (PA), lethal factor (LF), and edema factor (EF) (1,2 for review). PA binds to two related proteins on the cell surface; these are termed tumor epithelial marker 8 (TEM8)/anthrax toxin receptor (ATR)3 and capillary morphogenesis protein 2 (CMG2),4 although it is still unclear which is physiologically relevant. Following PA binding to its receptor, PA is cleaved into two fragments by a furin-like protease. The bound fragment binds both LF and EF; the resulting complex is then endocytosed which allows the translocation of LF and EF into the cytoplasm. EF is a calmodulin and Ca++-dependent adenylate cyclase responsible for the edema seen in the disease. It is thought to benefit the B. anthracis bacteria by inhibiting cells of the host immune system.