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Archaic chaperone-usher pili self-secrete into superelastic zigzag springs
Joint Biotechnology Laboratory, MediCity, Faculty of Medicine, University of Turku, Turku, Finland.ORCID iD: 0000-0002-8363-6105
Joint Biotechnology Laboratory, MediCity, Faculty of Medicine, University of Turku, Turku, Finland.ORCID iD: 0000-0001-9872-8523
Joint Biotechnology Laboratory, MediCity, Faculty of Medicine, University of Turku, Turku, Finland.
Umeå University, Faculty of Science and Technology, Department of Physics. Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR). (The Biophysics and Biophotonics group)
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2022 (English)In: Nature, ISSN 0028-0836, E-ISSN 1476-4687, Vol. 609, no 7926, p. 335-340Article in journal (Refereed) Published
Abstract [en]

Adhesive pili assembled via the chaperone-usher pathway (CUP) are hair-like appendages that mediate host tissue colonization and biofilm formation of Gram-negative bacteria 1-3. Archaic CUP pili, the most diverse and widespread CUP adhesins, are promising vaccine and drug targets due to their prevalence in the most troublesome multidrug-resistant (MDR) pathogens 1,4,5. However, their architecture and assembly-secretion process remain unknown. Here, we present the 3.4 Å resolution cryo-electron microscopy structure of the prototypical archaic Csu pilus that mediates biofilm formation of Acinetobacter baumannii, a notorious MDR nosocomial pathogen. In contrast to the thick helical tubes of the classical type 1 and P pili, archaic pili assemble into a conceptually novel 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 now for the first time 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 MDR bacterial infections.

Place, publisher, year, edition, pages
Nature Publishing Group, 2022. Vol. 609, no 7926, p. 335-340
National Category
Microbiology in the medical area Other Physics Topics Structural Biology
Research subject
Microbiology
Identifiers
URN: urn:nbn:se:umu:diva-198528DOI: 10.1038/s41586-022-05095-0ISI: 000844487100001PubMedID: 35853476Scopus ID: 2-s2.0-85136986109OAI: oai:DiVA.org:umu-198528DiVA, id: diva2:1686020
Funder
Swedish Research Council, 2019-04016The Kempe Foundations, JCK-1724Swedish Research Council, 2019-01720Swedish Research Council, 2016-04451Available from: 2022-08-08 Created: 2022-08-08 Last updated: 2023-03-24Bibliographically approved

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Dahlberg, TobiasMyint, Si LhyamUhlin, Bernt EricAndersson, Magnus

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Pakharukova, NataliaMalmi, HenriDahlberg, TobiasChang, Yi-WeiMyint, Si LhyamKnight, Stefan DavidUhlin, Bernt EricAndersson, MagnusJensen, GrantZavialov, Anton V.
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Department of PhysicsUmeå Centre for Microbial Research (UCMR)Molecular Infection Medicine Sweden (MIMS)Department of Molecular Biology (Faculty of Medicine)
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Nature
Microbiology in the medical areaOther Physics TopicsStructural Biology

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