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The assembly platform FimD is required to obtain the most stable quaternary structure of type 1 pili

Author

Listed:
  • Dawid S. Zyla

    (ETH Zürich
    La Jolla Institute for Immunology)

  • Thomas Wiegand

    (ETH Zürich
    RWTH Aachen University
    Max Planck Institute for Chemical Energy Conversion)

  • Paul Bachmann

    (ETH Zürich)

  • Rafal Zdanowicz

    (ETH Zürich)

  • Christoph Giese

    (ETH Zürich)

  • Beat H. Meier

    (ETH Zürich)

  • Gabriel Waksman

    (University College London and Birkbeck)

  • Manuela K. Hospenthal

    (ETH Zürich
    University College London and Birkbeck)

  • Rudi Glockshuber

    (ETH Zürich)

Abstract

Type 1 pili are important virulence factors of uropathogenic Escherichia coli that mediate bacterial attachment to epithelial cells in the urinary tract. The pilus rod is comprised of thousands of copies of the main structural subunit FimA and is assembled in vivo by the assembly platform FimD. Although type 1 pilus rods can self-assemble from FimA in vitro, this reaction is slower and produces structures with lower kinetic stability against denaturants compared to in vivo-assembled rods. Our study reveals that FimD-catalysed in vitro-assembled type 1 pilus rods attain a similar stability as pilus rods assembled in vivo. Employing structural, biophysical and biochemical analyses, we show that in vitro assembly reactions lacking FimD produce pilus rods with structural defects, reducing their stability against dissociation. Overall, our results indicate that FimD is not only required for the catalysis of pilus assembly, but also to control the assembly of the most stable quaternary structure.

Suggested Citation

  • Dawid S. Zyla & Thomas Wiegand & Paul Bachmann & Rafal Zdanowicz & Christoph Giese & Beat H. Meier & Gabriel Waksman & Manuela K. Hospenthal & Rudi Glockshuber, 2024. "The assembly platform FimD is required to obtain the most stable quaternary structure of type 1 pili," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-47212-9
    DOI: 10.1038/s41467-024-47212-9
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    References listed on IDEAS

    as
    1. Christoph Giese & Chasper Puorger & Oleksandr Ignatov & Zuzana Bečárová & Marco E. Weber & Martin A. Schärer & Guido Capitani & Rudi Glockshuber, 2023. "Stochastic chain termination in bacterial pilus assembly," Nature Communications, Nature, vol. 14(1), pages 1-21, December.
    2. Natalia Pakharukova & Henri Malmi & Minna Tuittila & Tobias Dahlberg & Debnath Ghosal & Yi-Wei Chang & Si Lhyam Myint & Sari Paavilainen & Stefan David Knight & Urpo Lamminmäki & Bernt Eric Uhlin & Ma, 2022. "Archaic chaperone–usher pili self-secrete into superelastic zigzag springs," Nature, Nature, vol. 609(7926), pages 335-340, September.
    3. Maximilian M. Sauer & Roman P. Jakob & Jonathan Eras & Sefer Baday & Deniz Eriş & Giulio Navarra & Simon Bernèche & Beat Ernst & Timm Maier & Rudi Glockshuber, 2016. "Catch-bond mechanism of the bacterial adhesin FimH," Nature Communications, Nature, vol. 7(1), pages 1-13, April.
    4. Michael Vetsch & Chasper Puorger & Thomas Spirig & Ulla Grauschopf & Eilika U. Weber-Ban & Rudi Glockshuber, 2004. "Pilus chaperones represent a new type of protein-folding catalyst," Nature, Nature, vol. 431(7006), pages 329-333, September.
    5. Sebastian Geibel & Erik Procko & Scott J. Hultgren & David Baker & Gabriel Waksman, 2013. "Structural and energetic basis of folded-protein transport by the FimD usher," Nature, Nature, vol. 496(7444), pages 243-246, April.
    6. Gilles Phan & Han Remaut & Tao Wang & William J. Allen & Katharina F. Pirker & Andrey Lebedev & Nadine S. Henderson & Sebastian Geibel & Ender Volkan & Jun Yan & Micha B. A. Kunze & Jerome S. Pinkner , 2011. "Crystal structure of the FimD usher bound to its cognate FimC–FimH substrate," Nature, Nature, vol. 474(7349), pages 49-53, June.
    7. Minge Du & Zuanning Yuan & Glenn T. Werneburg & Nadine S. Henderson & Hemil Chauhan & Amanda Kovach & Gongpu Zhao & Jessica Johl & Huilin Li & David G. Thanassi, 2021. "Processive dynamics of the usher assembly platform during uropathogenic Escherichia coli P pilus biogenesis," Nature Communications, Nature, vol. 12(1), pages 1-9, December.
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