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A Salmonella type three secretion effector/chaperone complex adopts a hexameric ring-like structure.

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Bacterial pathogens use type three secretion systems (T3SS) to inject effectors. Researchers found that the Salmonella SopB/SigE effector complex forms a ring structure, potentially aiding T3SS recognition and effector delivery.

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Bacterial pathogens utilize type three secretion systems (T3SS) to translocate effector proteins into host cells.
  • T3SS components are conserved across diverse pathogens, but a common effector recognition motif remains elusive.

Purpose of the Study:

  • To biochemically and structurally characterize the Salmonella SopB/SigE chaperone/effector complex.
  • To investigate the role of effector oligomerization in T3SS recognition.

Main Methods:

  • Small-angle X-ray scattering (SAXS) was employed for biochemical and structural analysis.
  • The study focused on the Salmonella SopB/SigE complex.

Main Results:

  • The SopB/SigE complex forms dynamic, homohexameric ring structures with an internal tunnel.
  • The chaperone (SigE) positions the disordered N-terminal end of the effector (SopB) for T3SS processing.
  • The ring structure's dimensions are compatible with the injectisome's ATPase rings, suggesting a role in recognition.

Conclusions:

  • This is the first evidence of effector oligomerization in solution, mimicking the secretion machinery's organization.
  • Oligomeric structure may be a conserved strategy for specific and efficient T3SS recognition, despite a lack of sequence or structural identity among effectors.