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A Visual Assay to Monitor T6SS-mediated Bacterial Competition
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Type VI secretion requires a dynamic contractile phage tail-like structure.

M Basler1, M Pilhofer, G P Henderson

  • 1Department of Microbiology and Immunobiology, Harvard Medical School, 200 Longwood Avenue, Boston, Massachusetts 02115, USA.

Nature
|February 28, 2012
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Summary

Type VI secretion systems in Vibrio cholerae utilize dynamic tubular structures, similar to phage tails, for protein secretion. These structures contract to propel proteins into target cells, acting as bacterial nanomachines.

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Area of Science:

  • Microbiology
  • Bacterial Pathogenesis
  • Molecular Biology

Background:

  • Type VI secretion systems (T1SS) are complex protein machines found in bacteria.
  • These systems are involved in virulence and share evolutionary links with bacteriophage tails.

Purpose of the Study:

  • To investigate the mechanism of protein secretion by the Type VI secretion system in Vibrio cholerae.
  • To elucidate the role of the intracellular tubular structure in T1SS function.

Main Methods:

  • Time-lapse fluorescence light microscopy to observe dynamic sheath behavior.
  • Whole-cell electron cryotomography for high-resolution structural analysis.

Main Results:

  • The T1SS sheath undergoes cyclical assembly, contraction, disassembly, and re-assembly.
  • Sheaths exist in extended or contracted states, connected to the inner membrane via a basal structure.
  • Sheath contraction is identified as the energy source for protein translocation.

Conclusions:

  • The T1SS sheath functions as a contractile nanomachine, analogous to phage tails.
  • This contraction mechanism drives the translocation of effector proteins into adjacent cells.
  • The findings provide a mechanistic understanding of bacterial protein secretion via T1SS.