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Bacterial CdiA effector proteins deliver toxic CdiA-CT into target cells. Precise cleavage activates the CdiA-CT entry domain for translocation, revealing a critical structural switch for bacterial toxin delivery.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Gram-negative bacteria utilize CdiA effector proteins to inhibit competing bacteria.
  • CdiA delivers its toxic CdiA-CT domain into the periplasm of target cells via proteolytic cleavage.

Purpose of the Study:

  • To investigate the role of CdiA-CT processing in its translocation into the cytoplasm.
  • To elucidate the mechanism by which the CdiA-CT entry domain gains membrane translocation competence.

Main Methods:

  • Analysis of CdiA-CT processing and translocation using biochemical and biophysical techniques.
  • Investigating the impact of precise versus imprecise proteolytic cleavage on CdiA-CT function.

Main Results:

  • Proteolytic cleavage is essential not only for CdiA-CT release but also for activating its N-terminal entry domain for membrane translocation.
  • Precise cleavage after the conserved VENN peptide sequence is critical for activating the entry domain's translocation capability.
  • Imprecisely processed CdiA-CT fragments fail to transition to a translocation-competent state and cannot enter the cytoplasm.

Conclusions:

  • CdiA-CT processing induces a conformational change, switching the entry domain into a membrane-translocation competent state.
  • Accurate proteolytic processing is a key regulatory step controlling the delivery of CdiA toxins into bacterial cytoplasm.