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

Dawid S. Zyla, Thomas Wiegand, Paul Bachmann, Rafal Zdanowicz, Christoph Giese, Beat H. Meier, Gabriel Waksman, Manuela K. Hospenthal () and Rudi Glockshuber
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Dawid S. Zyla: ETH Zürich
Thomas Wiegand: ETH Zürich
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
Rudi Glockshuber: ETH Zürich

Nature Communications, 2024, vol. 15, issue 1, 1-14

Abstract: 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.

Date: 2024
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DOI: 10.1038/s41467-024-47212-9

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