Mechanical architecture and folding of E. coli type 1 pilus domains

Alvaro Alonso-Caballero, Jörg Schönfelder, Simon Poly, Fabiano Corsetti, David Sancho, Emilio Artacho and Raul Perez-Jimenez ()
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Alvaro Alonso-Caballero: CIC nanoGUNE
Jörg Schönfelder: CIC nanoGUNE
Simon Poly: CIC nanoGUNE
Fabiano Corsetti: CIC nanoGUNE
David Sancho: Donostia International Physics Center
Emilio Artacho: CIC nanoGUNE
Raul Perez-Jimenez: CIC nanoGUNE

Nature Communications, 2018, vol. 9, issue 1, 1-11

Abstract: Abstract Uropathogenic Escherichia coli attach to tissues using pili type 1. Each pilus is composed by thousands of coiled FimA domains followed by the domains of the tip fibrillum, FimF-FimG-FimH. The domains are linked by non-covalent β-strands that must resist mechanical forces during attachment. Here, we use single-molecule force spectroscopy to measure the mechanical contribution of each domain to the stability of the pilus and monitor the oxidative folding mechanism of a single Fim domain assisted by periplasmic FimC and the oxidoreductase DsbA. We demonstrate that pilus domains bear high mechanical stability following a hierarchy by which domains close to the tip are weaker than those close to or at the pilus rod. During folding, this remarkable stability is achieved by the intervention of DsbA that not only forms strategic disulfide bonds but also serves as a chaperone assisting the folding of the domains.

Date: 2018
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-05107-6

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DOI: 10.1038/s41467-018-05107-6

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