8EHT

Cryo-EM reconstruction of the CS20 bacterial adhesion pili

Summary for 8EHT

• Entry DOI: 10.2210/pdb8eht/pdb
• EMDB information: 28152
• Descriptor: CS20 fimbria major subunit protein (1 entity in total)
• Functional Keywords: enterotoxigenic, adhesion pili, superelastic, cell adhesion
• Biological source: Escherichia coli
• Total number of polymer chains: 7
• Total formula weight: 122046.39

Authors

Doran, M.H.,Bullitt, E. (deposition date: 2022-09-14, release date: 2023-03-22, Last modification date: 2024-10-23)

Primary citation

Doran, M.H.,Baker, J.L.,Dahlberg, T.,Andersson, M.,Bullitt, E.
Three structural solutions for bacterial adhesion pilus stability and superelasticity.
Structure, 31:529-540.e7, 2023

PubMed Abstract: Bacterial adhesion pili are key virulence factors that mediate host-pathogen interactions in diverse epithelial environments. Deploying a multimodal approach, we probed the structural basis underpinning the biophysical properties of pili originating from enterotoxigenic (ETEC) and uropathogenic bacteria. Using cryo-electron microscopy we solved the structures of three vaccine target pili from ETEC bacteria, CFA/I, CS17, and CS20. Pairing these and previous pilus structures with force spectroscopy and steered molecular dynamics simulations, we find a strong correlation between subunit-subunit interaction energies and the force required for pilus unwinding, irrespective of genetic similarity. Pili integrate three structural solutions for stabilizing their assemblies: layer-to-layer interactions, N-terminal interactions to distant subunits, and extended loop interactions from adjacent subunits. Tuning of these structural solutions alters the biophysical properties of pili and promotes the superelastic behavior that is essential for sustained bacterial attachment.

PubMed: 37001523
DOI: 10.1016/j.str.2023.03.005

Experimental method

ELECTRON MICROSCOPY (3.4 Å)