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A Visual Assay to Monitor T6SS-mediated Bacterial Competition
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Composition of the type VII secretion system membrane complex.

Edith N G Houben1, Jovanka Bestebroer, Roy Ummels

  • 1Department of Medical Microbiology and Infection Control, VU University Medical Center, Amsterdam, The Netherlands. e.houben@vumc.nl

Molecular Microbiology
|August 29, 2012
PubMed
Summary

Pathogenic mycobacteria use type VII secretion (T7S) systems to export virulence factors. This study characterizes the ESX-5 T7S membrane complex, revealing its composition and structure.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Structural Biology

Background:

  • Pathogenic mycobacteria utilize type VII secretion (T7S) systems for virulence factor transport.
  • Mycobacterium tuberculosis possesses up to five T7S systems (ESX-1 to ESX-5).
  • The ESX-5 system's role in secreting EsxN, PPE, and PE_PGRS proteins highlights its significance in M. tuberculosis.

Purpose of the Study:

  • To elucidate the composition and structure of the T7S membrane complex.
  • To investigate the ESX-5 system in Mycobacterium marinum and Mycobacterium bovis BCG as a model.
  • To provide foundational insights into mycobacterial T7S machinery.

Main Methods:

  • Purification and analysis of the T7S membrane complex under native conditions.
  • Blue native-PAGE and immunoprecipitation assays.
  • Limited proteolysis to determine protein localization within the complex.

Main Results:

  • The ESX-5 membrane complex (~1500 kDa) comprises four conserved proteins: EccB(5), EccC(5), EccD(5), and EccE(5).
  • EccC(5) and EccE(5) are located at the complex periphery.
  • Expression of EccC(5) and EccD(5) is crucial for stable membrane complex formation.

Conclusions:

  • This study presents the first structural data on a T7S membrane complex.
  • The findings on the ESX-5 complex are likely generalizable to other mycobacterial T7S systems due to component conservation.
  • Understanding T7S complex structure is key to deciphering virulence factor secretion in pathogenic mycobacteria.