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Related Experiment Videos

Customized secretion chaperones in pathogenic bacteria

P Wattiau1, S Woestyn, G R Cornelis

  • 1Microbial Pathogenesis Unit, International Institute of Cellular and Molecular Pathology, Brussels, Belgium.

Molecular Microbiology
|April 1, 1996
PubMed
Summary
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Pathogenic bacteria use a specialized Yop secretion (Ysc) system to export anti-host Yop proteins without a signal peptide. Specific Yop chaperone (Syc) proteins assist this crucial virulence mechanism.

Area of Science:

  • Microbiology
  • Bacteriology
  • Molecular Biology

Background:

  • Pathogenic Yersinia species secrete virulence factors known as Yops.
  • Yop secretion utilizes a type III secretion system (Ysc), distinct from classical signal peptide pathways.
  • The Ysc system is related to flagellar assembly apparatus.

Purpose of the Study:

  • To investigate the mechanism of Yop secretion in pathogenic Yersinia.
  • To characterize the role of cytoplasmic proteins (Syc) in Yop secretion.
  • To define the Yop secretion signal and chaperone requirements.

Main Methods:

  • Analysis of the Yop secretion pathway.
  • Identification and characterization of Yop secretion (Ysc) machinery.
  • Investigation of specific Yop chaperone (Syc) proteins and their interaction with Yops.

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Main Results:

  • Yop secretion occurs via the Ysc apparatus, a type III secretion system.
  • Secretion of several Yops requires specific cytoplasmic chaperones (Syc).
  • Syc proteins bind cognate Yops and lack ATPase activity, differing from typical chaperones.

Conclusions:

  • The Ysc system is a key virulence factor for pathogenic Yersinia.
  • Syc chaperones play a critical role in Yop secretion, facilitating the process.
  • The Yop secretion mechanism and associated chaperones have counterparts in other pathogenic bacteria.