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Updated: Jun 2, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
Crystallography and electron microscopy of chaperone/usher pilus systems
Sebastian Geibel1, Gabriel Waksman
1Institute of Structural Molecular Biology, Birkbeck and University College London, London, UK. s.geibel@mail.cryst.bbk.ac.uk
The chaperone-usher pathway assembles bacterial pili for host cell attachment. This review details the structural mechanisms of this essential bacterial organelle biogenesis.
Area of Science:
- Microbiology
- Structural Biology
- Biochemistry
Background:
- The chaperone-usher (CU) pathway is a conserved system in bacteria for assembling and translocating adhesive protein fibers called pili or fimbriae.
- Pili are crucial for pathogenic bacteria, mediating attachment to host cells via adhesins at their tips, initiating infections like those caused by uropathogenic E. coli (UPEC).
Purpose of the Study:
- To review the structural biology of the chaperone-usher pathway.
- To elucidate the mechanisms underlying the biogenesis of CU pili, a significant class of bacterial organelles.
Main Methods:
- This review synthesizes existing structural data on the chaperone-usher pathway.
- Focuses on the roles of periplasmic chaperones and the outer membrane usher in pilus assembly.
Main Results:
- The usher protein catalyzes the ordered assembly of pilus subunits.
- Chaperones are released, and the growing pilus is translocated stepwise to the bacterial surface.
Conclusions:
- Structural insights into the chaperone-usher pathway reveal the intricate mechanisms of pilus biogenesis.
- Understanding this pathway is key to comprehending bacterial adhesion and infection processes.
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