Journal
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES
Volume 364, Issue 1514, Pages 209-215Publisher
ROYAL SOC
DOI: 10.1098/rstb.2008.0126
Keywords
planar bilayer membranes; protein unfolding; lethal factor; voltage-driven transport
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Funding
- National Institutes of Health [GM29210]
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Anthrax toxin consists of three proteins (approx. 90 kDa each): lethal factor (LF); oedema factor (OF); and protective antigen (PA). The former two are enzymes that act when they reach the cytosol of a targeted cell. To enter the cytosol, however, which they do after being endocytosed into an acidic vesicle compartment, they require the third component, PA. PA (or rather its proteolytically generated fragment PA(63)) forms at low pH a heptameric beta-barrel channel, (PA(63))(7), through which LF and OF are transported-a phenomenon we have demonstrated in planar phospholipid bilayers. It might appear that (PA(63))(7) simply forms a large hole through which LF and OF diffuse. However, LF and OF are folded proteins, much too large to fit through the approximately 15 angstrom diameter (PA(63))(7) beta-barrel. This paper discusses how the (PA(63))(7) channel both participates in the unfolding of LF and OF and functions in their translocation as a proton-protein symporter.
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