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Inactive conformation enhances binding function in physiological conditions.

Olga Yakovenko1, Veronika Tchesnokova2, Evgeni V Sokurenko2

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Summary
This summary is machine-generated.

Wild-type FimH (bacterial adhesin) uses its inactive state for faster initial binding, while an engineered activated variant binds with higher affinity. This kinetic-selection model explains how mechanical forces enhance cell adhesion under flow.

Keywords:
adhesionconformational dynamicsligandmechanical forcereceptor

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Area of Science:

  • Biochemistry
  • Microbiology
  • Biophysics

Background:

  • Receptors often exhibit conformational flexibility, switching between inactive (open) and active (closed) states upon ligand binding.
  • The bacterial adhesin FimH is crucial for adhesion and displays such conformational changes.

Purpose of the Study:

  • To investigate the role of the inactive conformation in FimH-mediated binding.
  • To compare the binding dynamics of wild-type FimH with an engineered constitutively active variant.

Main Methods:

  • Comparative analysis of wild-type FimH and an engineered activated FimH variant.
  • Assessment of binding affinity, lifetime, mechanical strength, and bond association rates.
  • Evaluation of bacterial adhesion under static and flow conditions.

Main Results:

  • Activated FimH showed higher affinity and better static adhesion.
  • Wild-type FimH exhibited superior adhesion under flow conditions.
  • Wild-type FimH demonstrated a faster bond association rate, crucial for flow-mediated adhesion.

Conclusions:

  • Introduced the kinetic-selection model for ligand-associated conformational changes.
  • Mechanical force drives a non-equilibrium cycle, utilizing the fast binding of the inactive state and slow unbinding of the active state for enhanced effective affinity.