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TitleEvolutionary fine-tuning of conformational ensembles in FimH during host-pathogen interactions.
Journal, issue, pagesSci Adv, Vol. 3, Issue 2, Page e1601944, Year 2017
Publish dateFeb 10, 2017
AuthorsVasilios Kalas / Jerome S Pinkner / Thomas J Hannan / Michael E Hibbing / Karen W Dodson / Alex S Holehouse / Hao Zhang / Niraj H Tolia / Michael L Gross / Rohit V Pappu / James Janetka / Scott J Hultgren /
PubMed AbstractPositive selection in the two-domain type 1 pilus adhesin FimH enhances fitness in urinary tract infection (UTI). We report a comprehensive atomic-level view of FimH in two-state conformational ...Positive selection in the two-domain type 1 pilus adhesin FimH enhances fitness in urinary tract infection (UTI). We report a comprehensive atomic-level view of FimH in two-state conformational ensembles in solution, composed of one low-affinity tense (T) and multiple high-affinity relaxed (R) conformations. Positively selected residues allosterically modulate the equilibrium between these two conformational states, each of which engages mannose through distinct binding orientations. A FimH variant that only adopts the R state is severely attenuated early in a mouse model of uncomplicated UTI but is proficient at colonizing catheterized bladders in vivo or bladder transitional-like epithelial cells in vitro. Thus, the bladder habitat has barrier(s) to R state-mediated colonization possibly conferred by the terminally differentiated bladder epithelium and/or decoy receptors in urine. Together, our studies reveal the conformational landscape in solution, binding mechanisms, and adhesive strength of an allosteric two-domain adhesin that evolved "moderate" affinity to optimize persistence in the bladder during UTI.
External linksSci Adv / PubMed:28246638 / PubMed Central
MethodsX-ray diffraction
Resolution1.962 - 2.596 Å
Structure data

PDB-5jqi:
Crystal structure of FimH A62S from E. coli UTI89 bound to FimG N-terminal extension
Method: X-RAY DIFFRACTION / Resolution: 1.962 Å

PDB-5jr4:
Crystal structure of FimH A27V/V163A from E. coli UTI89 bound to FimG N-terminal extension
Method: X-RAY DIFFRACTION / Resolution: 2.596 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-CA:
Unknown entry

Source
  • escherichia coli (strain uti89 / upec) (bacteria)
  • escherichia coli uti89 (bacteria)
KeywordsSUGAR BINDING PROTEIN / lectin / immunoglobulin fold / carbohydrate binding protein / donor strand exchange

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