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Bacterial macroscopic rope-like fibers with cytopathic and adhesive properties

Juan Xicohtencatl-Cortes1, Zeus Saldaña, Wanyin Deng

  • 1Laboratorio de Bacteriología Intestinal, Hospital Infantil de México Federico Gómez, Dr. Márquez 162, Col. Doctores, Delegación Cuauhtémoc, México D.F. 06720, México.

The Journal of Biological Chemistry
|August 7, 2010
PubMed

Insights

Deadly E. coli form macroscopic, amyloid-like ropes from EspC/EspP proteins. These structures enhance bacterial survival, adhesion, and biofilm formation, contributing to pathogen virulence.

Area of Science:

  • Microbiology
  • Structural Biology
  • Pathogenesis

Background:

  • Enterohemorrhagic and enteropathogenic Escherichia coli are deadly human pathogens.
  • Autotransporter proteins like EspC and EspP are associated with virulence.

Purpose of the Study:

  • To investigate the oligomerization of EspC and EspP proteins.
  • To characterize the novel macroscopic structures formed by these proteins.

Main Methods:

  • Ultrastructural, biochemical, and genetic analyses were employed.
  • Protein aggregation, stability, and dye-binding properties were assessed.
  • Bacterial cultures and recombinant protein assembly were studied.

Main Results:

  • EspC and EspP proteins oligomerize into macroscopic, rope-like structures (>1 cm).
  • These ropes exhibit amyloid-like properties (aggregation, insolubility, dye binding, stability).
  • Ropes enhance bacterial adherence, biofilm formation, epithelial cell damage, and protection from antimicrobials.

Conclusions:

  • The formation of amyloid-like ropes by EspC/EspP is specific to pathogenic E. coli strains.
  • These structures likely play a significant role in bacterial survival and pathogenesis.
  • Self-assembly of EspP monomers suggests a direct role in rope formation.

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