Serum protease cleavage of Bacillus anthracis protective antigen.

@article{Ezzell1992SerumPC,
  title={Serum protease cleavage of Bacillus anthracis protective antigen.},
  author={John W. Ezzell and T G Abshire},
  journal={Journal of general microbiology},
  year={1992},
  volume={138 3},
  pages={
          543-9
        }
}
The protective antigen component of anthrax lethal toxin, produced in vitro, has a molecular mass of 83 kDa. Cell-culture studies by others have demonstrated that upon binding of the 83 kDa protective antigen to cell-surface receptors, the protein is cleaved by an unidentified cell-associated protease activity. The resultant 63 kDa protein then binds lethal factor to form lethal toxin, which has been proposed to be internalized by endocytosis. We found that, in the blood of infected animals… CONTINUE READING

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