Abstract
Bacillus anthracis is the etiological agent of anthrax, a disease often fatal in humans and many animals species. Fully virulent strains of this pathogen harbor two plasmids, pXO1 and pXO2, coding for the production of two toxins and D-glutamic acid polymer capsule, respectively. The two toxins, edema and lethal toxin, are secreted by B. anthracis and are composed of three distinct proteins, protective antigen (PA; 85 kDa), lethal factor (LF; 83 kDa) and edema factor (EF; 89 kDa). PA combined with LF forms the lethal toxin (Beali et al., 1962; Smith & Stoner, 1967), whereas edema toxin consists of PA and EF. Both toxins are organized according to the A-B type model (Gill, 1978). PA represents a common B component, with receptor-binding activity, and mediates entry of either LF or EF into target cells (Leppla, 1984). EF has been shown to be a calmodulin-dependent adenylate cyclase (Leppla, 1982). By sequence comparison, it has been suggested that LF is a metalloprotease (Klimpel et al., 1994).
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
