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A receptor-based switch that regulates anthrax toxin pore formation.

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Summary

Anthrax toxin entry is controlled by the ANTXR2 receptor acting as a molecular switch. This study reveals a novel intermediate in toxin activation, showing ANTXR2 remains bound after pore formation.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Cellular receptors function as molecular switches controlling microbial toxin entry.
  • The precise mechanisms of these receptor-based switches are not fully understood.
  • Anthrax toxin entry involves the protective antigen (PA) subunit interacting with cellular receptors.

Purpose of the Study:

  • To elucidate the mechanism of the anthrax toxin receptor ANTXR2.
  • To understand how ANTXR2 binding to protective antigen (PA) domains 2 and 4 regulates toxin entry.
  • To investigate the role of receptor-binding in the prepore-to-pore conversion of PA.

Main Methods:

  • Utilized transfer cross-saturation (TCS) NMR to monitor PA-receptor contacts.
  • Analyzed changes during the prepore-to-pore conversion of the heptameric PA structure.
  • Investigated receptor interactions with PA domains 2 and 4.

Main Results:

  • Receptor binding to PA restricts necessary structural changes for pore formation.
  • A novel intermediate was identified where ANTXR2 contact with PA domain 2 weakens before pore conversion.
  • ANTXR2 remains bound to PA domain 4 even after pore formation.

Conclusions:

  • ANTXR2 acts as a molecular switch controlling anthrax toxin cellular entry.
  • The identified intermediate provides new insights into the toxin activation pathway.
  • Persistent ANTXR2 binding to the PA pore may influence its structure and function.