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Related Experiment Videos

Shigella Stays on the Move.

Noelia Lopez-Montero1, Jost Enninga1

  • 1Institut Pasteur, Dynamics of Host-Pathogen Interactions Unit, Paris, France.

Cell Host & Microbe
|October 13, 2017
PubMed
Summary

Guanylate-binding proteins (GBPs) trap cytosolic Shigella bacteria, preventing spread. However, the bacterial E3 ubiquitin ligase IpaH9.8 can overcome this host defense mechanism.

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Area of Science:

  • Immunology
  • Microbiology
  • Cell Biology

Background:

  • Guanylate-binding proteins (GBPs) are crucial for cellular defense against intracellular pathogens.
  • Shigella is an intracellular bacterium that causes severe diarrheal disease.

Purpose of the Study:

  • To investigate the role of Guanylate-binding proteins (GBPs) in controlling cytosolic Shigella infection.
  • To elucidate the mechanisms by which Shigella evades GBP-mediated host defenses.

Main Methods:

  • Cellular infection models using Shigella.
  • Immunofluorescence microscopy to visualize GBP recruitment and bacterial localization.
  • Genetic manipulation of bacterial and host factors.

Main Results:

  • Cytosolic Shigella are effectively entrapped within a coat of Guanylate-binding proteins (GBPs).
  • This GBP coat restricts bacterial cell-to-cell spread, limiting infection dissemination.
  • The bacterial E3 ubiquitin ligase IpaH9.8 antagonizes the GBP-mediated defense, promoting bacterial escape and spread.

Conclusions:

  • Guanylate-binding proteins (GBPs) represent a key host defense mechanism against cytosolic Shigella.
  • Shigella employs the E3 ubiquitin ligase IpaH9.8 to counteract GBP-mediated immunity, highlighting a critical host-pathogen conflict.

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