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Archaic chaperone–usher pili self-secrete into superelastic zigzag springs
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Archaic chaperone–usher pili self-secrete into superelastic zigzag springs
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Journal Article
Archaic chaperone–usher pili self-secrete into superelastic zigzag springs
2022
Overview
Adhesive pili assembled through the chaperone–usher pathway are hair-like appendages that mediate host tissue colonization and biofilm formation of Gram-negative bacteria
1
–
3
. 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
1
,
4
,
5
. 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.
The Csu pili of the multidrug-resistant nosocomial pathogen
Acinetobacter baumannii
assemble into an ultrathin zigzag architecture secured by a clinch mechanism that provides the pilus with high mechanical stability and superelasticity.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 82/80
/ 82/83
/ Acinetobacter baumannii - cytology
/ Acinetobacter baumannii - ultrastructure
/ Adhesins
/ Biofilms
/ Fimbriae Proteins - chemistry
/ Fimbriae Proteins - metabolism
/ Fimbriae Proteins - ultrastructure
/ Fimbriae, Bacterial - chemistry
/ Fimbriae, Bacterial - metabolism
/ Fimbriae, Bacterial - ultrastructure
/ Humanities and Social Sciences
/ Molecular Chaperones - chemistry
/ Molecular Chaperones - metabolism
/ Molecular Chaperones - ultrastructure
/ Pili
/ Science
/ Tubes
/ Vaccines
