National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM122510
United States
Citation
Journal: Elife / Year: 2018 Title: Functional role of the type 1 pilus rod structure in mediating host-pathogen interactions. Authors: Caitlin N Spaulding / Henry Louis Schreiber / Weili Zheng / Karen W Dodson / Jennie E Hazen / Matt S Conover / Fengbin Wang / Pontus Svenmarker / Areli Luna-Rico / Olivera Francetic / Magnus ...Authors: Caitlin N Spaulding / Henry Louis Schreiber / Weili Zheng / Karen W Dodson / Jennie E Hazen / Matt S Conover / Fengbin Wang / Pontus Svenmarker / Areli Luna-Rico / Olivera Francetic / Magnus Andersson / Scott Hultgren / Edward H Egelman / Abstract: Uropathogenic (UPEC), which cause urinary tract infections (UTI), utilize type 1 pili, a chaperone usher pathway (CUP) pilus, to cause UTI and colonize the gut. The pilus rod, comprised of repeating ...Uropathogenic (UPEC), which cause urinary tract infections (UTI), utilize type 1 pili, a chaperone usher pathway (CUP) pilus, to cause UTI and colonize the gut. The pilus rod, comprised of repeating FimA subunits, provides a structural scaffold for displaying the tip adhesin, FimH. We solved the 4.2 Å resolution structure of the type 1 pilus rod using cryo-electron microscopy. Residues forming the interactive surfaces that determine the mechanical properties of the rod were maintained by selection based on a global alignment of sequences. We identified mutations that did not alter pilus production in vitro but reduced the force required to unwind the rod. UPEC expressing these mutant pili were significantly attenuated in bladder infection and intestinal colonization in mice. This study elucidates an unappreciated functional role for the molecular spring-like property of type 1 pilus rods in host-pathogen interactions and carries important implications for other pilus-mediated diseases.
Helical symmetry: (Circular symmetry: 1 / Dyad axis: no / N subunits divisor: 1 / Num. of operations: 10 / Rise per n subunits: 7.7 Å / Rotation per n subunits: 115 °)
Details
THE HELICAL SYMMETRY PARAMETER SHOULD BE APPLIED TO A SINGLE CHAIN OF THE MODEL, INSTEAD OF WHOLE MODEL IN COORDINATES FILE, TO ACHIEVE THE ENTIRE ASSEMBLY.
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Components
#1: Protein
Type-1fimbrialprotein, Achain / Type-1A pilin
Mass: 15835.243 Da / Num. of mol.: 11 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P04128
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Experimental details
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Experiment
Experiment
Method: ELECTRON MICROSCOPY
EM experiment
Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction
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Sample preparation
Component
Name: Type 1 pilus / Type: COMPLEX / Entity ID: all / Source: NATURAL
Molecular weight
Experimental value: NO
Source (natural)
Organism: Escherichia coli K-12 (bacteria)
Buffer solution
pH: 7.4
Specimen
Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen support
Details: unspecified
Vitrification
Cryogen name: ETHANE / Humidity: 95 %
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Electron microscopy imaging
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
Microscopy
Model: FEI TITAN KRIOS
Electron gun
Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lens
Mode: BRIGHT FIELD
Image recording
Electron dose: 20 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON II (4k x 4k)
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