This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Farfan, M. J.
Right arrow Articles by Nataro, J. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Farfan, M. J.
Right arrow Articles by Nataro, J. P.

 Previous Article  |  Next Article 

Infection and Immunity, October 2008, p. 4378-4384, Vol. 76, No. 10
0019-9567/08/$08.00+0     doi:10.1128/IAI.00439-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

The Major Pilin Subunit of the AAF/II Fimbriae from Enteroaggregative Escherichia coli Mediates Binding to Extracellular Matrix Proteins{triangledown}

Mauricio J. Farfan,1 Keith G. Inman,1,2 and James P. Nataro1,2*

Center for Vaccine Development, Department of Pediatrics, University of Maryland School of Medicine, Baltimore, Maryland,1 Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland2

Received 9 April 2008/ Returned for modification 16 May 2008/ Accepted 25 June 2008

Enteroaggregative Escherichia coli (EAEC) adherence to human intestinal tissue is mediated by aggregative adherence fimbriae (AAF); however, the receptors involved in EAEC adherence remain uncharacterized. Adhesion to extracellular matrix proteins is commonly observed among enteric pathogens, so we addressed the hypothesis that EAEC may bind to extracellular matrix proteins commonly found in the intestine. We found that EAEC prototype strain 042 adhered more abundantly to surfaces that were precoated with the extracellular matrix proteins fibronectin, laminin, and type IV collagen. Differences in fibronectin binding of almost 2 orders of magnitude were observed between EAEC 042 and a mutant in the AAF/II major pilin gene, aafA. Purified AafA, refolded as a donor strand complementation construct, bound fibronectin in a dose-dependent manner. Addition of fibronectin to the apical surfaces of polarized T84 cell monolayers augmented EAEC 042 adherence, and this effect required expression of aafA. Finally, increased bacterial adherence was observed when apical secretion of fibronectin was induced by adenosine in polarized T84 cells. Binding to fibronectin may contribute to colonization of the gastrointestinal tract by EAEC.

* Corresponding author. Mailing address: 685 W. Baltimore St., Baltimore, MD 21201. Phone: (410) 706-5328. Fax: (410) 706-6205. E-mail: jnataro{at}medicine.umaryland.edu

{triangledown} Published ahead of print on 30 June 2008.

Editor: A. J. Bäumler

Infection and Immunity, October 2008, p. 4378-4384, Vol. 76, No. 10
0019-9567/08/$08.00+0     doi:10.1128/IAI.00439-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»