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A Visual Assay to Monitor T6SS-mediated Bacterial Competition
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TssA forms a gp6-like ring attached to the type VI secretion sheath.

Sara Planamente1, Osman Salih2, Eleni Manoli1

  • 1MRC Centre for Molecular Bacteriology and Infection (CMBI), Department of Life Sciences, Imperial College London, London, UK.

The EMBO Journal
|June 12, 2016
PubMed
Summary

The type VI secretion system (T6SS) TssA1 protein forms ring structures that resemble phage baseplates. This finding suggests a shared evolutionary origin between bacterial T6SS and phage tail baseplate structures.

Keywords:
T6SSTssAbacteriophage baseplategp6type VI secretion system

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Area of Science:

  • Bacteriology
  • Microbiology
  • Structural Biology

Background:

  • The type VI secretion system (T6SS) is a complex bacterial machine for toxin delivery.
  • T6SS shares structural similarities with bacteriophage tails.

Purpose of the Study:

  • To investigate the structure and function of TssA1, a component of the T6SS.
  • To compare the T6SS baseplate with bacteriophage baseplates.

Main Methods:

  • Structural analysis of TssA1 dodecameric ring formation.
  • In vivo functional assays of TssA1.
  • Comparative sequence and structural analysis with phage baseplate components.

Main Results:

  • TssA1 forms dodecameric rings that fit the TssBC sheath and accommodate the Hcp tube.
  • TssA1 binds the T6SS sheath and influences its in vivo behavior.
  • Sequence and structural similarities were found between TssA1 and phage gp6, TssK1 and gp8, TssF and gp6N-terminus, and TssG and gp53.

Conclusions:

  • TssA1 is proposed as a T6SS baseplate component.
  • A comparative model for the T6SS baseplate and phage baseplate is proposed.
  • This suggests a potential evolutionary link between T6SS and phage tail machinery.