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

J. Biol. Chem., Vol. 281, Issue 39, 29120-29130, September 29, 2006

This Article Full Text Full Text (PDF) All Versions of this Article: 281/39/29120    most recent M605681200v1 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 Korotkova, N. Articles by Moseley, S. L. Search for Related Content PubMed PubMed Citation Articles by Korotkova, N. Articles by Moseley, S. L. Social Bookmarking                      What's this?

A Subfamily of Dr Adhesins of Escherichia coli Bind Independently to Decay-accelerating Factor and the N-domain of Carcinoembryonic Antigen^*

Natalia Korotkova, Ernesto Cota, Yuri Lebedin^¶, Severine Monpouet, Julie Guignot^||, Alain L. Servin^||, Steve Matthews, and Steve L. Moseley¹

From the Department of Microbiology, University of Washington, Seattle, Washington 98195-7242, the Division of Molecular Biosciences, Imperial College London, South Kensington, London SW7 2AZ, United Kingdom, ^¶Xema-Medica Co., 105043 Moscow, Russia, and ^||Institut National de la Santé et de la Recherche Médicale, Unité 756, Faculté de Pharmacie, Paris XI, F-92296 Châtenay-Malabry, France

Escherichia coli expressing the Dr family of adhesins adheres to epithelial cells by binding to decay-accelerating factor (DAF) and carcinoembryonic antigen (CEA)-related cell surface proteins. The attachment of bacteria expressing Dr adhesins to DAF induces clustering of DAF around bacterial cells and also recruitment of CEA-related cell adhesion molecules. CEA, CEACAM1, and CEACAM6 have been shown to serve as receptors for some Dr adhesins (AfaE-I, AfaE-III, DraE, and DaaE). We demonstrate that AfaE-I, AfaE-V, DraE, and DaaE adhesins bind to the N-domain of CEA. To identify the residues involved in the N-CEA/DraE interaction, we performed SPR binding analyses of naturally occurring variants and a number of randomly generated mutants in DraE and N-CEA. Additionally, we used chemical shift mapping by NMR to determine the surface of DraE involved in N-CEA binding. These results show a distinct CEA binding site located primarily in the A, B, E, and D strands of the Dr adhesin. Interestingly, this site is located opposite to the -sheet encompassing the previously determined binding site for DAF, which implies that the adhesin can bind simultaneously to both receptors on the epithelial cell surface. The recognition of CEACAMs from a highly diverse DrCEA subfamily of Dr adhesins indicates that interaction with these receptors plays an important role in niche adaptation of E. coli strains expressing Dr adhesins.

Received for publication, June 14, 2006 , and in revised form, July 17, 2006.

^* This work was supported by NIDDK, National Institutes of Health, Grant DK-064229 and The Wellcome Trust. 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.

¹ To whom correspondence should be addressed: Dept. of Microbiology, University of Washington, Box 357242, Seattle, WA 98195-7242. Tel.: 206-543-2820; Fax: 206-543-8297; E-mail: moseley{at}u.washington.edu.

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

This article has been cited by other articles:

				N. Korotkova, Y. Yarova-Yarovaya, V. Tchesnokova, N. Yazvenko, M. A. Carl, A. E. Stapleton, and S. L. Moseley Escherichia coli DraE Adhesin-Associated Bacterial Internalization by Epithelial Cells Is Promoted Independently by Decay-Accelerating Factor and Carcinoembryonic Antigen-Related Cell Adhesion Molecule Binding and Does Not Require the DraD Invasin Infect. Immun., September 1, 2008; 76(9): 3869 - 3880. [Abstract] [Full Text] [PDF]

				M.-E. Charbonneau and M. Mourez Functional Organization of the Autotransporter Adhesin Involved in Diffuse Adherence J. Bacteriol., December 15, 2007; 189(24): 9020 - 9029. [Abstract] [Full Text] [PDF]

				S.-P. Nuccio and A. J. Baumler Evolution of the Chaperone/Usher Assembly Pathway: Fimbrial Classification Goes Greek Microbiol. Mol. Biol. Rev., December 1, 2007; 71(4): 551 - 575. [Abstract] [Full Text] [PDF]

				B. Zalewska, J. Stangret, K. Bury, M. Wojciechowski, J. Kur, and R. Piatek DAF- and collagen-binding properties of chimeric Dr fimbriae Microbiology, August 1, 2007; 153(8): 2733 - 2742. [Abstract] [Full Text] [PDF]