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Environmental pH modulates inerolysin activity via post-binding blockade.

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Summary
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Cholesterol-dependent cytolysins (CDCs) are bacterial toxins. Inerolysin (INY), a CDC from Lactobacillus iners, shows unique pH-dependent regulation, affecting pore formation at neutral pH.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Cholesterol-dependent cytolysins (CDCs) are bacterial pore-forming toxins.
  • Regulation of CDC activity is crucial for bacterial virulence.
  • Listeriolysin O (LLO) uses pH-dependent protein unfolding for regulation.

Purpose of the Study:

  • To investigate the pH-dependent mechanism of Inerolysin (INY), a CDC from Lactobacillus iners.
  • To elucidate how pH affects INY's pore-forming activity and membrane interactions.

Main Methods:

  • Assessing INY activity across a pH range.
  • Utilizing fluorescent membrane probe assays.
  • Analyzing membrane binding and oligomerization at different pH levels.

Main Results:

  • INY exhibits optimal activity at acidic pH, with reduced function at neutral pH.
  • INY retains membrane binding ability but loses pore formation at neutral pH.
  • Membrane insertion, but not oligomerization, is impaired at neutral pH.

Conclusions:

  • INY displays a distinct pH-dependence mechanism compared to other CDCs.
  • This regulation occurs at a late stage of pore formation, impacting membrane insertion.
  • A novel form of CDC pH-dependence has been identified.