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Lukas F Milles1, Eduard M Unterauer2, Thomas Nicolaus2

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Staphylococcal B domains exhibit remarkable protein mechanostability, exceeding 2 nN. Calcium ions are critical for this strength, allowing tunable force responses and making them promising for protein design.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Microbiology

Background:

  • Staphylococcal pathogens utilize Ig-like B domains to withstand mechanical stress during host adhesion.
  • Understanding the mechanical properties of these B domains is crucial for comprehending bacterial resilience.

Purpose of the Study:

  • To investigate the mechanical stability and force-bearing capacity of Staphylococcal B domains.
  • To elucidate the role of calcium ions in the extraordinary mechanostability of B domains.

Main Methods:

  • Atomic force microscopy-based single-molecule force spectroscopy was employed to probe B domain unfolding.
  • Systematic mutations in calcium coordination sites were introduced to assess their impact on mechanical strength.

Main Results:

  • Individual B domains demonstrated unprecedented mechanostability, with unfolding forces exceeding 2 nN.
  • Removal of calcium ions via chelation reduced unfolding forces by a factor of four.
  • Mutational analysis revealed that calcium ions are essential for extreme mechanical strength and allow for tunable force responses.

Conclusions:

  • Staphylococcal B domains possess exceptional mechanical strength, significantly higher than previously reported proteins.
  • Calcium ions are indispensable for the high mechanostability of B domains.
  • The calcium-tunable force response and rapid refolding properties make B domains attractive targets for protein engineering.