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Related Experiment Videos

Fiber assembly by the chaperone-usher pathway.

Frederic G Sauer1, Han Remaut, Scott J Hultgren

  • 1Section of Microbial Pathogenesis, Yale University School of Medicine, Boyer Center for Molecular Medicine, 295 Congress Ave., New Haven, CT 06536, USA.

Biochimica Et Biophysica Acta
|November 18, 2004
PubMed
Summary

Bacterial pathogens use the chaperone-usher pathway to build virulence fibers. Chaperone release fuels fiber assembly, driven by outer-membrane usher proteins.

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Bacterial extracellular fibers are crucial for pathogen virulence.
  • The chaperone-usher pathway is a key mechanism for assembling these fibers.

Purpose of the Study:

  • To elucidate the mechanism of fiber subunit incorporation in the chaperone-usher pathway.
  • To understand the role of periplasmic chaperones in driving fiber assembly.

Main Methods:

  • Structural analysis of chaperone-subunit interactions.
  • Biochemical assays to measure chaperone dissociation and fiber assembly rates.

Main Results:

  • Periplasmic chaperones facilitate initial subunit folding.
  • Chaperones trap subunits in activated folding transition states.

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  • Chaperone dissociation releases energy that drives subunit incorporation into growing fibers.

    • Conclusions:

    • The chaperone-usher pathway utilizes a unique energy release mechanism for fiber assembly.
    • Outer-membrane ushers form a pore essential for fiber elongation.
    • Understanding this pathway offers potential targets for anti-virulence strategies.