The assembly platform FimD is required to obtain the most stable quaternary structure of type 1 pili
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2024-04-08
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Journal Article
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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.
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15 (1)
Pages / Article No.
3032
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Nature
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03412 - Glockshuber, Rudolf (emeritus) / Glockshuber, Rudolf (emeritus)
09756 - Hospenthal, Manuela / Hospenthal, Manuela
02521 - Inst. f. Molekularbiologie u. Biophysik / Inst. Molecular Biology and Biophysics
02515 - Laboratorium für Physikalische Chemie / Laboratory of Physical Chemistry
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Funding
201234 - Structural and functional characterization of filamentous, supramolecular protein complexes in urinary tract infections (SNF)
176403 - Mechanism of assembly and receptor binding of adhesive pili from pathogenic bacteria (SNF)
156304 - Functional significance of the dynamics of receptor binding and the alternative folding possibilities of pilus subunits in urinary tract infections caused by pathogenic Escherichia coli strains (SNF)
188711 - NMR studies in the Solid State (SNF)
176403 - Mechanism of assembly and receptor binding of adhesive pili from pathogenic bacteria (SNF)
156304 - Functional significance of the dynamics of receptor binding and the alternative folding possibilities of pilus subunits in urinary tract infections caused by pathogenic Escherichia coli strains (SNF)
188711 - NMR studies in the Solid State (SNF)