Identification of the cellular receptor for anthrax toxin

Kenneth A. Bradley, Jeremy Mogridge, Michael Mourez, R. John Collier and John A. T. Young
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Kenneth A. Bradley: McArdle Laboratory for Cancer Research, University of Wisconsin—Madison
Jeremy Mogridge: Harvard Medical School
Michael Mourez: Harvard Medical School
R. John Collier: Harvard Medical School
John A. T. Young: McArdle Laboratory for Cancer Research, University of Wisconsin—Madison

Nature, 2001, vol. 414, issue 6860, 225-229

Abstract: Abstract The tripartite toxin secreted by Bacillus anthracis, the causative agent of anthrax, helps the bacterium evade the immune system and can kill the host during a systemic infection. Two components of the toxin enzymatically modify substrates within the cytosol of mammalian cells: oedema factor (OF) is an adenylate cyclase that impairs host defences through a variety of mechanisms including inhibiting phagocytosis1,2; lethal factor (LF) is a zinc-dependent protease that cleaves mitogen-activated protein kinase kinase and causes lysis of macrophages3,4,5. Protective antigen (PA), the third component, binds to a cellular receptor and mediates delivery of the enzymatic components to the cytosol. Here we describe the cloning of the human PA receptor using a genetic complementation approach. The receptor, termed ATR (anthrax toxin receptor), is a type I membrane protein with an extracellular von Willebrand factor A domain that binds directly to PA. In addition, a soluble version of this domain can protect cells from the action of the toxin.

Date: 2001
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DOI: 10.1038/n35101999

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