Anthrax Research Today is a free monthly online journal that collates and summarizes the latest research about Anthrax, including details on bacillus anthracis, contagiousness, exposure, effects.

Anthrax Toxin: Receptor Binding, Internalization, Pore Formation, and Translocation.

Young JA, Collier RJ

1Infectious Disease Laboratory, The Salk Institute for Biological Studies, La Jolla, California 92037; email: jyoung@salk.edu , 2Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115; email: jcollier@hms.harvard.edu.

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.

Published 26 June 2007 in Annu Rev Biochem, 76: 243-265.
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