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

J. Biol. Chem., Vol. 283, Issue 17, 11596-11605, April 25, 2008

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 283/17/11596    most recent M707815200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted 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 Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Yakovenko, O. Articles by Thomas, W. E. Search for Related Content PubMed PubMed Citation Articles by Yakovenko, O. Articles by Thomas, W. E. Social Bookmarking                      What's this?

FimH Forms Catch Bonds That Are Enhanced by Mechanical Force Due to Allosteric Regulation^*

Olga Yakovenko, Shivani Sharma, Manu Forero, Veronika Tchesnokova^¶, Pavel Aprikian^¶, Brian Kidd, Albert Mach^||, Viola Vogel, Evgeni Sokurenko^¶, and Wendy E. Thomas¹

From the Departments of Bioengineering and ^¶Microbiology, University of Washington, Seattle, Washington 98195, the Department of Materials, ETH Zurich, 8093 Zurich, Switzerland, and the ^||Department of Bioengineering, University of California, Berkeley, California 94720

The bacterial adhesive protein, FimH, is the most common adhesin of Escherichia coli and mediates weak adhesion at low flow but strong adhesion at high flow. There is evidence that this occurs because FimH forms catch bonds, defined as bonds that are strengthened by tensile mechanical force. Here, we applied force to single isolated FimH bonds with an atomic force microscope in order to test this directly. If force was loaded slowly, most of the bonds broke up at low force (<60 piconewtons of rupture force). However, when force was loaded rapidly, all bonds survived until much higher force (140–180 piconewtons of rupture force), behavior that indicates a catch bond. Structural mutations or pretreatment with a monoclonal antibody, both of which allosterically stabilize a high affinity conformation of FimH, cause all bonds to survive until high forces regardless of the rate at which force is applied. Pretreatment of FimH bonds with intermediate force has the same strengthening effect on the bonds. This demonstrates that FimH forms catch bonds and that tensile force induces an allosteric switch to the high affinity, strong binding conformation of the adhesin. The catch bond behavior of FimH, the amount of force needed to regulate FimH, and the allosteric mechanism all provide insight into how bacteria bind and form biofilms in fluid flow. Additionally, these observations may provide a means for designing antiadhesive mechanisms.

Received for publication, September 18, 2007 , and in revised form, February 1, 2008.

^* This work was supported by National Institutes of Health Grant 1RO1 AI50940, National Science Foundation Grant CMMI-0654054, the Center for Nanotechnology at the University of Washington through an IGERT Fellowship Award (National Science Foundation Grant DGE-0504573), the University of Washington Initiatives Fund, the National Nanotechnology Infrastructure Network Research Experience for Undergraduates Program, and the Swiss Federal Institute of Technology, ETH Zurich. 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. 1–3.

¹ To whom correspondence should be addressed: 1705 N.E. Pacific St., Suite N430P, Seattle, WA 98195. Tel.: 206-616-3947; Fax: 206-685-4434; E-mail: wendyt{at}u.washington.edu.

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

This article has been cited by other articles:

				F. Kong, A. J. Garcia, A. P. Mould, M. J. Humphries, and C. Zhu Demonstration of catch bonds between an integrin and its ligand J. Cell Biol., June 29, 2009; 185(7): 1275 - 1284. [Abstract] [Full Text] [PDF]

				J. C. Friedland, M. H. Lee, and D. Boettiger Mechanically Activated Integrin Switch Controls {alpha}5{beta}1 Function Science, January 30, 2009; 323(5914): 642 - 644. [Abstract] [Full Text] [PDF]

				L. S. Ronald, O. Yakovenko, N. Yazvenko, S. Chattopadhyay, P. Aprikian, W. E. Thomas, and E. V. Sokurenko From the Cover: Adaptive mutations in the signal peptide of the type 1 fimbrial adhesin of uropathogenic Escherichia coli PNAS, August 5, 2008; 105(31): 10937 - 10942. [Abstract] [Full Text] [PDF]