Catch-bond mechanism of force-enhanced adhesion: counterintuitive, elusive, but ... widespread?
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.
Sokurenko
Evgeni V
EV
Department of Microbiology, University of Washington, Seattle, WA 98105, USA. evs@u.washington.edu
Vogel
Viola
V
Thomas
Wendy E
WE
D018830:Adhesins, Escherichia coli / Q000378:metabolism*; D001422:Bacterial Adhesion; D001792:Blood Platelets / Q000502:physiology; D002448:Cell Adhesion; D042783:Endothelial Cells / Q000502:physiology; D004926:Escherichia coli / Q000502:physiology; D036781:Fimbriae Proteins / Q000378:metabolism*; D019041:L-Selectin / Q000378:metabolism*; D007962:Leukocytes / Q000502:physiology; D008958:Models, Molecular; D008968:Molecular Conformation; D019007:P-Selectin / Q000378:metabolism*; D013314:Stress, Mechanical
D018830:Adhesins, Escherichia coli; D019007:P-Selectin; C058769:fimH protein, E coli; D019041:L-Selectin; D036781:Fimbriae Proteins