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J. Biol. Chem., Vol. 280, Issue 45, 37707-37716, November 11, 2005

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The Distinct Binding Specificities Exhibited by Enterobacterial Type 1 Fimbriae Are Determined by Their Fimbrial Shafts^*

Matthew J. Duncan, Elena L. Mann, Michael S. Cohen, Itzhak Ofek¶, Nathan Sharon||, and Soman N. Abraham1

From the Molecular Genetics and Microbiology and Pathology, Duke University Medical Center, Durham, North Carolina 27710, the ^¶Department of Human Microbiology, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv 69978, Israel, and the ^||Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel

Type 1 fimbriae of enterobacteria are heteropolymeric organelles of adhesion composed of FimH, a mannose-binding lectin, and a shaft composed primarily of FimA. We compared the binding activities of recombinant clones expressing type 1 fimbriae from Escherichia coli, Klebsiella pneumoniae, and Salmonella typhimurium for gut and uroepithelial cells and for various soluble mannosylated proteins. Each fimbria was characterized by its capacity to bind particular epithelial cells and to aggregate mannoproteins. However, when each respective FimH subunit was cloned and expressed in the absence of its shaft as a fusion protein with MalE, each FimH bound a wide range of mannose-containing compounds. In addition, we found that expression of FimH on a heterologous fimbrial shaft, e.g. K. pneumoniae FimH on the E. coli fimbrial shaft or vice versa, altered the binding specificity of FimH such that it closely resembled that of the native heterologous type 1 fimbriae. Furthermore, attachment to and invasion of bladder epithelial cells, which were mediated much better by native E. coli type 1 fimbriae compared with native K. pneumoniae type 1 fimbriae, were found to be dependent on the background of the fimbrial shaft (E. coli versus K. pneumoniae) rather than the background of the FimH expressed. Thus, the distinct binding specificities of different enterobacterial type 1 fimbriae cannot be ascribed solely to the primary structure of their respective FimH subunits, but are also modulated by the fimbrial shaft on which each FimH subunit is presented, possibly through conformational constraints imposed on FimH by the fimbrial shaft. The capacity of type 1 fimbrial shafts to modulate the tissue tropism of different enterobacterial species represents a novel function for these highly organized structures.

Received for publication, February 2, 2005 , and in revised form, August 19, 2005.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY914173 [GenBank] , AY914172 [GenBank] , DQ090770 [GenBank] , and DQ090769 [GenBank] .

^* This work was supported in part by National Institutes of Health Grants AI 056101, AI 150021, and DK 050814. 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: Dept. of Pathology, Duke University Medical Center, Campus Box 3020, Durham, NC 27710. Tel.: 919-684-6942; Fax: 919-684-2021; E-mail: soman.abraham{at}duke.edu.

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