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Archaic chaperone-usher pili self-secrete into superelastic zigzag springs

Pakharukova, Natalia and Malmi, Henri and Tuittila, Minna and Dahlberg, Tobias and Ghosal, Debnath and Chang, Yi-Wei and Myint, Si Lhyam and Paavilainen, Sari and Knight, Stefan David and Lamminmäki, Urpo and Uhlin, Bernt Eric and Andersson, Magnus and Jensen, Grant and Zavialov, Anton V. (2022) Archaic chaperone-usher pili self-secrete into superelastic zigzag springs. Nature, 609 . pp. 335-340. ISSN 0028-0836. doi:10.1038/s41586-022-05095-0.

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Adhesive pili assembled through the chaperone–usher pathway are hair-like appendages that mediate host tissue colonization and biofilm formation of Gram-negative bacteria. Archaic chaperone–usher pathway pili, the most diverse and widespread chaperone–usher pathway adhesins, are promising vaccine and drug targets owing to their prevalence in the most troublesome multidrug-resistant pathogens. However, their architecture and assembly–secretion process remain unknown. Here, we present the cryo-electron microscopy structure of the prototypical archaic Csu pilus that mediates biofilm formation of Acinetobacter baumannii—a notorious multidrug-resistant nosocomial pathogen. In contrast to the thick helical tubes of the classical type 1 and P pili, archaic pili assemble into an ultrathin zigzag architecture secured by an elegant clinch mechanism. The molecular clinch provides the pilus with high mechanical stability as well as superelasticity, a property observed for the first time, to our knowledge, in biomolecules, while enabling a more economical and faster pilus production. Furthermore, we demonstrate that clinch formation at the cell surface drives pilus secretion through the outer membrane. These findings suggest that clinch-formation inhibitors might represent a new strategy to fight multidrug-resistant bacterial infections.

Item Type:Article
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URLURL TypeDescription ItemFree ReadCube access
Pakharukova, Natalia0000-0002-8363-6105
Malmi, Henri0000-0001-9872-8523
Ghosal, Debnath0000-0002-2227-0330
Chang, Yi-Wei0000-0003-2391-473X
Knight, Stefan David0000-0002-7180-8758
Uhlin, Bernt Eric0000-0002-2991-8072
Andersson, Magnus0000-0002-9835-3263
Jensen, Grant0000-0003-1556-4864
Zavialov, Anton V.0000-0001-6191-5931
Additional Information:We thank the staff of the Cryo-EM Swedish National Facility at SciLifeLab, Stockholm and the Beckman Institute Resource Center for Transmission Electron Microscopy at Caltech, Pasadena for their assistance during data collection; and C. Sachse, J. Huiskonen and S. Huber for their suggestions on helical reconstruction. This work was supported by grants from the Academy of Finland (321762) and S. Juselius Foundation (2019) to A.V.Z.; the National Institutes of Health (RO1 AI127401) to G.J.; the Swedish Research Council (SRC) (2019-04016) to M.A.; SRC (2019-01720) and The Kempe Foundations (JCK-1724) to B.E.U.; and SRC (2016-04451) to S.D.K. Open access funding provided by University of Turku (UTU) including Turku University Central Hospital.
Funding AgencyGrant Number
Academy of Finland321762
S. Juselius FoundationUNSPECIFIED
NIHRO1 AI127401
Swedish Research Council2019-04016
Swedish Research Council2019-01720
Kempe FoundationJCK-1724
Swedish Research Council2016-04451
University of TurkuUNSPECIFIED
Turku University Central HospitalUNSPECIFIED
Record Number:CaltechAUTHORS:20220901-478558800.783
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:116664
Deposited By: Melissa Ray
Deposited On:01 Sep 2022 22:25
Last Modified:10 Oct 2022 19:22

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