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TitleArchaic chaperone-usher pili self-secrete into superelastic zigzag springs.
Journal, issue, pagesNature, Vol. 609, Issue 7926, Page 335-340, Year 2022
Publish dateJul 19, 2022
AuthorsNatalia Pakharukova / Henri Malmi / Minna Tuittila / Tobias Dahlberg / Debnath Ghosal / Yi-Wei Chang / Si Lhyam Myint / Sari Paavilainen / Stefan David Knight / Urpo Lamminmäki / Bernt Eric Uhlin / Magnus Andersson / Grant Jensen / Anton V Zavialov /
PubMed AbstractAdhesive 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 ...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.
External linksNature / PubMed:35853476 / PubMed Central
MethodsEM (helical sym.)
Resolution3.45 Å
Structure data

14777

7zl4

EMDB-14777, PDB-7zl4:
Cryo-EM structure of archaic chaperone-usher Csu pilus of Acinetobacter baumannii
Method: EM (helical sym.) / Resolution: 3.45 Å

Source
  • acinetobacter baumannii (bacteria)
KeywordsCELL ADHESION / chaperone-usher pathway / bacterial adhesion / biofilm formation / Acinetobacter baumannii / Csu pili

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