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Engineering a pH responsive pore forming protein.

Matic Kisovec1, Saša Rezelj1, Primož Knap1

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Researchers engineered Listeriolysin O (LLO) to create a pH-dependent toxin. This engineered LLO can perforate membranes in a controlled manner, offering potential for nanobiotechnology applications.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Nanobiotechnology

Background:

  • Listeriolysin O (LLO) is a pore-forming toxin that interacts with cholesterol-rich cell membranes.
  • LLO possesses a pH-sensitive domain influencing its stability and activity.
  • Engineering LLO for pH-governed responsiveness is a key area for biotechnological control.

Purpose of the Study:

  • To engineer a variant of Listeriolysin O (LLO) with controllable, pH-dependent hemolytic activity.
  • To investigate the structural and molecular mechanisms underlying pH-dependent pore formation in LLO.
  • To explore the potential of engineered LLO in nanobiotechnological applications.

Main Methods:

  • Detailed structural analysis of LLO.
  • Molecular dynamics simulations to predict allosteric effects on the pH sensor.
  • Site-directed mutagenesis (Tyr406Ala) to create LLO variants.
  • Functional assays to assess hemolytic activity and membrane perforation at different pH levels.

Main Results:

  • A single mutation (Tyr406Ala) was found to allosterically affect the pH sensor of LLO.
  • The Tyr406Ala mutant exhibits pH-dependent membrane insertion and pore formation.
  • The engineered LLO variant can be activated by acidic pH on artificial and cellular membranes.
  • Oligomerization and membrane binding are similar to wild-type LLO, but insertion is pH-controlled.

Conclusions:

  • The Tyr406Ala mutation successfully engineered pH-regulated membrane perforation by LLO.
  • This pH-dependent LLO variant shows significant potential for controlled substance release and pH sensing.
  • The findings open avenues for novel nanobiotechnological tools utilizing engineered toxins.