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Molecular Organization of Soluble Type III Secretion System Sorting Platform Complexes.

Ivonne Bernal1, Jonathan Börnicke1, Johannes Heidemann2

  • 1Center for Structural Systems Biology, Helmholtz Centre for Infection Research, Department of Structural Infection Biology, Notkestraße 85, 22607 Hamburg, Germany; Max Planck Institute for Infection Biology, Structural Systems Biology Group, Charitéplatz 1, 10117 Berlin, Germany.

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|July 10, 2019
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Summary

Researchers elucidated the structure of the Salmonella Typhimurium type III secretion system (T3SS) sorting platform. This study reveals the protein complex

Keywords:
Host–pathogen interactionSalmonella entericanative mass spectrometryprotein complexsmall-angle X‐ray scattering (SAXS)

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Area of Science:

  • Microbiology
  • Structural Biology
  • Molecular Biology

Background:

  • Gram-negative bacteria utilize the type III secretion system (T3SS) for host pathogen interactions.
  • The T3SS sorting platform, a cytosolic complex, regulates effector protein secretion.
  • The exact structure and subunit stoichiometry of the T3SS sorting platform remain largely uncharacterized.

Purpose of the Study:

  • To determine the stoichiometry and 3D organization of the Salmonella Typhimurium T3SS sorting platform.
  • To characterize the interactions between key sorting platform components: InvC, OrgB, SpaO, and SpaOC.
  • To propose a model for the T3SS sorting platform's core building block.

Main Methods:

  • Reconstitution of soluble protein complexes of T3SS sorting platform components.
  • Native mass spectrometry to determine subunit stoichiometry.
  • Small-angle X-ray scattering (SAXS) to gain insights into complex organization.
  • Domain-domain interaction analysis.

Main Results:

  • SpaOC was identified as essential for SpaO solubility.
  • The stoichiometry of the SpaO/SpaOC/OrgB/InvC complex was determined for the first time.
  • The soluble complex adopts an extended L-shaped conformation in solution.
  • This L-shaped complex resembles structures observed in situ, suggesting it's a core building block.

Conclusions:

  • The reconstituted SpaO/SpaOC/OrgB/InvC complex represents a fundamental unit of the T3SS sorting platform.
  • The L-shaped conformation provides a structural basis for understanding T3SS assembly and function.
  • This work offers critical insights into the molecular architecture of a key bacterial virulence machinery.