Catch-bond mechanism of force-enhanced adhesion: counterintuitive, elusive, but ... widespread?

Cell Host Microbe. 2008 Oct 16;4(4):314-23. doi: 10.1016/j.chom.2008.09.005.

Abstract

Catch bonds are bonds between a ligand and its receptor that are enhanced by mechanical force pulling the ligand-receptor complex apart. To date, catch-bond formation has been documented for the most common Escherichia coli adhesin, FimH, and for P-/L-selectins, universally expressed by leukocytes, platelets, and blood vessel walls. One compelling explanation for catch bonds is that force-induced structural alterations in the receptor protein are allosterically linked to a high-affinity conformation of its ligand-binding pocket. Catch-bond properties are likely to be widespread among adhesive proteins, thus calling for a detailed understanding of their underlying mechanisms and physiological significance.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Adhesins, Escherichia coli / metabolism*
  • Bacterial Adhesion*
  • Blood Platelets / physiology
  • Cell Adhesion*
  • Endothelial Cells / physiology
  • Escherichia coli / physiology
  • Fimbriae Proteins / metabolism*
  • L-Selectin / metabolism*
  • Leukocytes / physiology
  • Models, Molecular
  • Molecular Conformation
  • P-Selectin / metabolism*
  • Stress, Mechanical*

Substances

  • Adhesins, Escherichia coli
  • P-Selectin
  • fimH protein, E coli
  • L-Selectin
  • Fimbriae Proteins