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Structural basis for effector recognition by an antibacterial type IV secretion system.

Gabriel U Oka1, Diorge P Souza1, William Cenens1

  • 1Department of Biochemistry, Institute of Chemistry, University of São Paulo, São Paulo 05508-000, SP, Brazil.

Proceedings of the National Academy of Sciences of the United States of America
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Summary

Bacterial type IV secretion system (T4SS) effectors, X-Tfes, use their XVIPCD domain to interact with VirD4. This interaction, crucial for effector translocation, is mediated by the N-terminal region of XVIPCD and influenced by pH.

Keywords:
Xanthomonasbacterial competitionprotein NMRtype IV coupling proteintype IV secretion system

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Area of Science:

  • Bacteriology
  • Molecular Biology
  • Structural Biology

Background:

  • Soil, water, and plant bacteria use type IV secretion systems (T4SS) to translocate effector proteins (X-Tfes) into target cells, causing cell death.
  • X-Tfes possess a carboxyl-terminal domain (XVIPCD) essential for interaction with the T4SS coupling protein VirD4 and for translocation.
  • The structural basis of the XVIPCD-VirD4 interaction remains uncharacterized.

Purpose of the Study:

  • To elucidate the structural basis of the interaction between the XVIPCD and the VirD4 coupling protein.
  • To determine the functional regions within the XVIPCD domain responsible for VirD4 interaction and effector translocation.

Main Methods:

  • Solution Nuclear Magnetic Resonance (NMR) spectroscopy to determine the structure of the XVIPCD.
  • Mapping the interaction surface between XVIPCD and the VirD4 central all-alpha domain (VirD4AAD).
  • Isothermal titration calorimetry and in vivo competition assays to assess functional interactions.

Main Results:

  • The XVIPCD directly interacts with the VirD4AAD.
  • The N-terminal region of XVIPCD, containing conserved motifs, mediates VirD4AAD binding.
  • Both N- and carboxyl-terminal regions of XVIPCD are necessary for efficient X-Tfe translocation.
  • The N-terminal region's stability decreases at pH 7.0 and below, potentially aiding translocation.

Conclusions:

  • The XVIPCD-VirD4 interaction is structurally defined by the XVIPCD's N-terminal region binding to VirD4AAD.
  • Distinct regions of XVIPCD have specialized roles in VirD4 interaction and translocation.
  • pH-dependent conformational changes in XVIPCD may facilitate effector translocation into the periplasm.