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Related Concept Videos

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Related Experiment Video

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Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
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Binding and cell intoxication studies of anthrax lethal toxin.

Momchilo Vuyisich1, Claire K Sanders, Steven W Graves

  • 1Los Alamos National Lab, MS M888, P.O. Box 1663, Los Alamos, NM 87545, USA. vuyisich@lanl.gov

Molecular Biology Reports
|January 6, 2012
PubMed
Summary
This summary is machine-generated.

Anthrax lethal toxin (LT) can assemble outside of cells and binds to mammalian cells with high affinity. This assembled LT may represent a new therapeutic target for anthrax infections.

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Area of Science:

  • Microbiology
  • Toxicology
  • Molecular Biology

Background:

  • Anthrax lethal toxin (LT) is a key virulence factor of Bacillus anthracis.
  • LT assembly is typically described as cell-dependent, but evidence suggests pre-assembled LT exists.
  • This study investigates the properties and implications of cell-free assembled LT.

Purpose of the Study:

  • To demonstrate facile, cell-free assembly and purification of anthrax lethal toxin (LT).
  • To characterize the binding affinity and cell interaction of fully assembled LT.
  • To explore potential novel therapeutic targets for anthrax.

Main Methods:

  • Cell-free assembly and purification of LT.
  • Binding affinity assays comparing assembled LT and protective antigen (PA).
  • Quantitative cell intoxication assays to determine LD(50).
  • Cell-binding studies with and without blocked PA-specific receptors.

Main Results:

  • Facile cell-free assembly and purification of LT were achieved.
  • Fully assembled LT exhibited ~100-fold higher receptor binding affinity than PA alone.
  • LT binds mammalian cells differently than PA, even when PA receptors are blocked.
  • LT demonstrates high affinity and efficacy in cell intoxication.

Conclusions:

  • Fully assembled LT can form in the bloodstream and efficiently intoxicate cells.
  • LT may bind cells via a novel receptor-independent mechanism or distinct receptors.
  • Bloodstream-borne LT presents a potential new therapeutic target for anthrax.