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Related Experiment Video

Updated: Jun 16, 2026

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance
10:41

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance

Published on: January 3, 2012

Interplay between toxin transport and flotillin localization.

Sascha Pust1, Anne Berit Dyve, Maria L Torgersen

  • 1Centre for Cancer Biomedicine, University of Oslo, Oslo, Norway.

Plos One
|January 29, 2010
PubMed
Summary

Flotillin proteins regulate the retrograde transport of Shiga toxin (Stx) and ricin. Depleting flotillins increases toxin toxicity but does not affect uptake, suggesting a role in intracellular trafficking.

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Area of Science:

  • Cell biology
  • Molecular toxicology
  • Membrane trafficking

Background:

  • Flotillins are proteins found in lipid domains of the plasma membrane and intracellular compartments.
  • Their role in toxin transport, specifically Shiga toxin (Stx) and ricin, is not fully understood.

Purpose of the Study:

  • To investigate the role of flotillin-1 and flotillin-2 in the uptake and transport of Stx and ricin.
  • To determine if toxin binding and uptake are associated with flotillin relocalization.
  • To elucidate the impact of flotillins on toxin-induced cellular toxicity.

Main Methods:

  • Studied toxin-induced flotillin redistribution, potentially regulated by p38.
  • Utilized gene silencing (knockdown) to deplete flotillin-1 or flotillin-2.
  • Assessed toxin endocytic uptake, Golgi-dependent sulfation, and mannosylation.
  • Evaluated toxin toxicity and the effect of Brefeldin A (BFA).

Main Results:

  • Toxin exposure induced flotillin redistribution in a p38-dependent manner.
  • Flotillin depletion did not alter Stx or ricin endocytic uptake.
  • Golgi-dependent sulfation of both toxins was reduced in flotillin knockdown cells.
  • Ricin mannosylation increased, and toxicity of both toxins doubled in flotillin-depleted cells.
  • Brefeldin A still inhibited toxicity in flotillin knockdown cells, indicating Golgi-dependent retrograde transport.

Conclusions:

  • Flotillin proteins are not essential for the initial endocytic uptake of Stx and ricin.
  • Flotillins play a crucial role in regulating and facilitating the retrograde transport of Stx and ricin from the Golgi to the ER.
  • Flotillin depletion enhances toxin toxicity by impairing retrograde transport, while maintaining Golgi dependence.