Catch bond-mediated adhesion without a shear threshold: trimannose versus monomannose interactions with the FimH adhesin of Escherichia coli

doi:10.1074/jbc.M511496200

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Papers In Press, published online ahead of print April 19, 2006
J. Biol. Chem, 10.1074/jbc.M511496200
Submitted on October 24, 2005
Revised on March 1, 2006
Accepted on April 19, 2006

Catch bond-mediated adhesion without a shear threshold: trimannose versus monomannose interactions with the FimH adhesin of Escherichia coli

Lina M. Nilsson, Wendy E. Thomas, Elena Trintchina, Viola Vogel, and Evgeni V. Sokurenko

Microbiology, UW, University of Washington, Seattle, WA 98195-7242

Corresponding Author: evs{at}u.washington.edu

The FimH protein is the adhesive subunit of Escherichia coli type 1 fimbriae. It mediates shear-dependent bacterial binding to monomannose (1M) -coated surfaces manifested by the existence of a shear threshold for binding, below which bacteria do not adhere. The 1M-specific shear-dependent binding of FimH is consistent with so-called catch bond interactions, whose lifetime is increased by tensile force. We show here that the oligosaccharide-specific interaction of FimH with another of its ligands – tri-mannose (3M) – lacks a shear threshold for binding as the number of bacteria binding under static conditions is higher than under any flow. However, similar to 1M, the binding strength of surface-interacting bacteria is enhanced by shear: bacteria transition from rolling on the surface into firm stationary surface adhesion as the shear increases. The shear-enhanced bacterial binding strength on 3M is mediated by catch bond properties of the 1M-binding subsite within the extended oligosaccharide-binding pocket of FimH, as structural mutations in the putative force-responsive region and in the binding site affect 1M- and 3M-specific binding in an identical manner. A shear-dependent conversion of the adhesion mode is also exhibited by E. coli adhering via FimH to surfaces coated with the physiological ligand human laminin and, also, in adhesion of P-fimbriated E. coli to di-galactose surfaces.

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