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J. Biol. Chem., Vol. 283, Issue 13, 8118-8124, March 28, 2008

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Binding Specificity of Salmonella Plasmid-encoded Fimbriae Assessed by Glycomics^*

Daniela Chessa, Caleb W. Dorsey, Maria Winter, and Andreas J. Baümler¹

From the Department of Medical Microbiology and Immunology, School of Medicine, University of California at Davis, Davis, California 95616-8645 and the Department of Medical Microbiology and Immunology, College of Medicine, Texas A&M University Health Science Center, College Station, Texas 77843-1114

The Salmonella enterica serotype Typhimurium (S. Typhimurium) genome encodes 12 intestinal colonization factors of the chaperone/usher fimbrial assembly class; however, the binding specificity is known for only one of these adhesins, known as type 1 fimbriae. Here we explored the utility of glycomics to determine the carbohydrate binding specificity of plasmid-encoded fimbriae from S. Typhimurium. A cosmid carrying the pef operon was introduced into Escherichia coli and expression of fimbrial filaments composed of PefA confirmed by flow cytometry and immune-electron microscopy. Plasmid-encoded fimbriae were purified from the surface of E. coli, and the resulting preparation was shown to contain PefA as the sole major protein component. The binding of purified plasmid-encoded fimbriae to a glycanarray suggested that this adhesin specifically binds the trisaccharide Galβ1–4(Fuc1–3)GlcNAc, also known as the Lewis X (Le^x) blood group antigen. Results from the glycanarray were validated by enzyme-linked immunosorbent assay (ELISA) in which plasmid-encoded fimbriae bound Le^x-coated wells in a concentration-dependent manner. The binding of plasmid-encoded fimbriae to Le^x-coated wells could be inhibited by co-incubation with soluble Le^x antigen. Our results establish glycomic analysis as a promising new approach for determining the carbohydrate binding specificity of bacterial adhesins.

Received for publication, December 11, 2007 , and in revised form, January 22, 2008.

^* This work was supported in part by Public Health Service Grants AI040124, AI044170, and AI065534. 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 Medical Microbiology and Immunology, School of Medicine, University of California at Davis, One Shields Ave., Davis, CA 95616-8645. Fax: 530-754-7240; E-mail: ajbaumler{at}ucdavis.edu.

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