HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 281, Issue 24, 16656-16663, June 16, 2006

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 281/24/16656    most recent M511496200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Nilsson, L. M. Articles by Sokurenko, E. V. Search for Related Content PubMed PubMed Citation Articles by Nilsson, L. M. Articles by Sokurenko, E. V. Social Bookmarking                      What's this?

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 Vogel¹, and Evgeni V. Sokurenko^¶2

From the Departments of Bioengineering and ^¶Microbiology, University of Washington, Seattle, Washington 98195 and the Laboratory for Biologically Oriented Materials, Department of Materials, Swiss Federal Institute of Technology, ETH Zurich, Hönggerberg, CH-8093 Zürich, Switzerland

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, trimannose (3M), lacks a shear threshold for binding, since 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 into firm stationary surface adhesion as the shear increases. The shear-enhanced bacterial binding on 3M is mediated by catch bond properties of the 1M-binding subsite within the extended oligosaccharide-binding pocket of FimH, since 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 P-fimbriated E. coli adhering to digalactose surfaces.

Received for publication, October 24, 2005 , and in revised form, March 1, 2006.

^* This work was supported by National Institutes of Health Grants A145820 (to E. V. S.) and A150940 (to E. V. S.), a National Science Foundation graduate fellowship (to L. N.), and the Swiss Federal Institute of Technology, ETH Zurich (to V. V.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1 and S2.

¹ To whom correspondence may be addressed: Dept. of Material Science, Laboratory for Biologically Oriented Materials, Swiss Federal Institute of Technology, ETH Wolfgang-Pauli-Str. 10, ETH Hönggerberg, HCI F443, CH-8093 Zürich, Switzerland. Tel.: 41-44-632-08-87; Fax: 41-44-632-10-73; E-mail: viola.vogel{at}mat.ethz.ch. ² To whom correspondence may be addressed: Dept. of Microbiology, Rm. E309 HSB, University of Washington, Box 357242, Seattle, WA 98195-7242. Tel.: 206-685-2162; Fax: 206-543-8297; E-mail: evs{at}u.washington.edu.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				D. A. Rosen, J. S. Pinkner, J. N. Walker, J. S. Elam, J. M. Jones, and S. J. Hultgren Molecular Variations in Klebsiella pneumoniae and Escherichia coli FimH Affect Function and Pathogenesis in the Urinary Tract Infect. Immun., July 1, 2008; 76(7): 3346 - 3356. [Abstract] [Full Text] [PDF]

				O. Yakovenko, S. Sharma, M. Forero, V. Tchesnokova, P. Aprikian, B. Kidd, A. Mach, V. Vogel, E. Sokurenko, and W. E. Thomas FimH Forms Catch Bonds That Are Enhanced by Mechanical Force Due to Allosteric Regulation J. Biol. Chem., April 25, 2008; 283(17): 11596 - 11605. [Abstract] [Full Text] [PDF]

				V. Tchesnokova, P. Aprikian, O. Yakovenko, C. LaRock, B. Kidd, V. Vogel, W. Thomas, and E. Sokurenko Integrin-like Allosteric Properties of the Catch Bond-forming FimH Adhesin of Escherichia coli J. Biol. Chem., March 21, 2008; 283(12): 7823 - 7833. [Abstract] [Full Text] [PDF]

				P. Aprikian, V. Tchesnokova, B. Kidd, O. Yakovenko, V. Yarov-Yarovoy, E. Trinchina, V. Vogel, W. Thomas, and E. Sokurenko Interdomain Interaction in the FimH Adhesin of Escherichia coli Regulates the Affinity to Mannose J. Biol. Chem., August 10, 2007; 282(32): 23437 - 23446. [Abstract] [Full Text] [PDF]

				B. N. Anderson, A. M. Ding, L. M. Nilsson, K. Kusuma, V. Tchesnokova, V. Vogel, E. V. Sokurenko, and W. E. Thomas Weak Rolling Adhesion Enhances Bacterial Surface Colonization J. Bacteriol., March 1, 2007; 189(5): 1794 - 1802. [Abstract] [Full Text] [PDF]