The shaft of the type 1 fimbriae regulates an external force to match the FimH catch bond

Biophys J. 2013 May 21;104(10):2137-48. doi: 10.1016/j.bpj.2013.03.059.

Abstract

Type 1 fimbriae mediate adhesion of uropathogenic Escherichia coli to host cells. It has been hypothesized that due to their ability to uncoil under exposure to force, fimbriae can reduce fluid shear stress on the adhesin-receptor interaction by which the bacterium adheres to the surface. In this work, we develop a model that describes how the force on the adhesin-receptor interaction of a type 1 fimbria varies as a bacterium is affected by a time-dependent fluid flow mimicking in vivo conditions. The model combines in vivo hydrodynamic conditions with previously assessed biomechanical properties of the fimbriae. Numerical methods are used to solve for the motion and adhesion force under the presence of time-dependent fluid profiles. It is found that a bacterium tethered with a type 1 pilus will experience significantly reduced shear stress for moderate to high flow velocities and that the maximum stress the adhesin will experience is limited to ∼120 pN, which is sufficient to activate the conformational change of the FimH adhesin into its stronger state but also lower than the force required for breaking it under rapid loading. Our model thus supports the assumption that the type 1 fimbria shaft and the FimH adhesin-receptor interaction are optimized to each other, and that they give piliated bacteria significant advantages in rapidly changing fluidic environments.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adhesins, Escherichia coli / chemistry*
  • Adhesins, Escherichia coli / metabolism
  • Bacterial Adhesion*
  • Escherichia coli / chemistry
  • Escherichia coli / physiology
  • Fimbriae Proteins / chemistry*
  • Fimbriae Proteins / metabolism
  • Fimbriae, Bacterial / chemistry*
  • Models, Biological*
  • Protein Conformation
  • Receptors, Immunologic / chemistry
  • Receptors, Immunologic / metabolism

Substances

  • Adhesins, Escherichia coli
  • Receptors, Immunologic
  • bacterial adhesin receptor
  • fimH protein, E coli
  • Fimbriae Proteins