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Unveiling molecular interactions that stabilize bacterial adhesion pili.

Tobias Dahlberg1, Joseph L Baker2, Esther Bullitt3

  • 1Department of Physics, Umeå University, Umeå, Sweden.

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Bacterial adhesion pili are superelastic filaments crucial for cell attachment. Their stability, enhanced by specific structural features like the N-terminal staple, is key to their function.

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Area of Science:

  • Microbiology
  • Biophysics
  • Structural Biology

Background:

  • Adhesion pili are bacterial surface appendages essential for host cell attachment.
  • P pili from uropathogenic bacteria are helical filaments assembled via the chaperone-usher pathway.
  • Understanding pili structure-function relationships is critical for combating bacterial infections.

Purpose of the Study:

  • To investigate the biophysical function and structural interactions stabilizing P pili.
  • To elucidate the role of subunit-subunit interactions and the N-terminal staple in pilus mechanics.
  • To compare stabilization mechanisms between P pili and type 1 pili.

Main Methods:

  • Utilizing optical tweezers to measure P pilus subunit-subunit interaction dynamics.
  • Employing steered molecular dynamics (sMD) simulations to determine atomic details of subunit interactions under tension.
  • Analyzing pilus compliance as a function of contour length.

Main Results:

  • Pilus compliance was found to be dependent on contour length.
  • sMD simulations revealed atomic details of subunit-subunit interactions under tensile stress.
  • The N-terminal staple region significantly stabilizes the P pilus helical structure through long-range interactions.

Conclusions:

  • P pilus stability is significantly influenced by its N-terminal staple region.
  • Layer-to-layer interactions may compensate for the absence of a staple in other pili types, like type 1 pili.
  • Bacterial pilus function is intrinsically linked to their unique structural and biophysical properties.