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      Anthrax toxin: receptor binding, internalization, pore formation, and translocation.

      1 ,
      Annual review of biochemistry
      Annual Reviews

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          Abstract

          Anthrax toxin consists of three nontoxic proteins that self-assemble at the surface of receptor-bearing mammalian cells or in solution, yielding a series of toxic complexes. Two of the proteins, called Lethal Factor (LF) and Edema Factor (EF), are enzymes that act on cytosolic substrates. The third, termed Protective Antigen (PA), is a multifunctional protein that binds to receptors, orchestrates the assembly and internalization of the complexes, and delivers them to the endosome. There, the PA moiety forms a pore in the endosomal membrane and promotes translocation of LF and EF to the cytosol. Recent advances in understanding the entry process include insights into how PA recognizes its two known receptors and its ligands, LF and EF; how the PA:receptor interaction influences the pH-dependence of pore formation; and how the pore functions in promoting translocation of LF and EF across the endosomal membrane.

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          Author and article information

          Journal
          Annu Rev Biochem
          Annual review of biochemistry
          Annual Reviews
          0066-4154
          0066-4154
          2007
          : 76
          Affiliations
          [1 ] Infectious Disease Laboratory, The Salk Institute for Biological Studies, La Jolla, California 92037, USA. jyoung@salk.edu
          Article
          10.1146/annurev.biochem.75.103004.142728
          17335404
          50370f86-40a0-49ea-b23c-f54a6a078c60
          History

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