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Related Experiment Videos

Structural polymorphism of bacterial adhesion pili

E Bullitt1, L Makowski

  • 1Department of Biophysics, Boston University School of Medicine, Massachusetts 02118-2394.

Nature
|January 12, 1995
PubMed
Summary

Uropathogenic P-pili, bacterial adhesion structures, resist urine flow due to their mechanical resilience. These pili can unravel to extend five times their original length without depolymerizing.

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biophysics

Background:

  • Bacterial adhesion pili are crucial for specific binding and attachment to host cells.
  • Uropathogenic P-pili exhibit remarkable mechanical resilience, enabling them to withstand urine flow and resist clearance.
  • P-pili are complex structures with defined dimensions and protein composition.

Purpose of the Study:

  • To investigate the structural properties and mechanical resilience of uropathogenic P-pili.
  • To understand the mechanism by which P-pili maintain bacterial attachment despite physiological forces.
  • To elucidate the structural basis for the unique unraveling capability of P-pili.

Main Methods:

  • Three-dimensional reconstruction of P-pili.
  • Analysis of protein composition and structural organization.
  • Investigation of mechanical properties and structural transitions.

Main Results:

  • P-pili are approximately 1 micron long, 68 Angstroms in diameter, and composed of ~1,000 PapA subunits.
  • The pilus structure is anchored by PapH and terminates in a fibrillus (PapK, PapE, PapF) presenting the PapG adhesin.
  • A structural transition allows P-pili to unravel into an extended, thinner structure five times their original length without depolymerization.

Conclusions:

  • P-pili possess a unique structural mechanism enabling significant extension, contributing to their adhesive function and resilience.
  • The conserved C-termini of structural proteins mediate binding to the PapD chaperone, essential for pilus assembly.
  • Understanding P-pili structure provides insights into bacterial pathogenesis and potential therapeutic targets.

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