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Related Experiment Videos

Outer-membrane PapC molecular usher discriminately recognizes periplasmic chaperone-pilus subunit complexes

K W Dodson1, F Jacob-Dubuisson, R T Striker

  • 1Washington University Medical School, Department of Molecular Microbiology, St. Louis, MO 63110.

Proceedings of the National Academy of Sciences of the United States of America
|April 15, 1993
PubMed
Summary

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This study reveals how P pili assemble, showing that specific chaperone-subunit complexes target the molecular usher PapC. This differential targeting ensures the correct order of these virulence-associated pili structures.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • P pili are crucial virulence factors in uropathogenic bacteria.
  • Their assembly involves complex protein interactions requiring chaperones and outer membrane proteins.
  • PapC is identified as a key outer membrane protein, acting as a 'molecular usher'.

Purpose of the Study:

  • To investigate the mechanism of P pili assembly.
  • To determine how chaperone-PapD complexes interact with the outer membrane protein PapC.
  • To elucidate the role of differential targeting in ensuring correct pilus structure.

Main Methods:

  • Utilized in vitro binding assays to study protein-protein interactions.
  • Examined the binding affinities of PapD-subunit complexes to PapC.

Related Experiment Videos

  • Correlated binding affinity with the subunit's position in the P pilus tip fibrillum.

    • Main Results:

    • PapD-tip fibril protein complexes (PapG, PapF, PapE) bound to PapC.
    • Binding affinity correlated with the subunit's position within the pilus tip.
    • PapD-rod protein complexes (PapA, PapK) did not bind PapC.
    • Demonstrated differential targeting of chaperone-subunit complexes to PapC.

    Conclusions:

    • Differential targeting of PapD-subunit complexes to PapC is a key mechanism for ordered P pili assembly.
    • This process ensures the correct incorporation of subunits into the adhesive composite pili structure.
    • Highlights the role of molecular ushers in bacterial adhesion and pathogenesis.