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Infection and Immunity, February 2006, p. 1255-1265, Vol. 74, No. 2
0019-9567/06/$08.00+0     doi:10.1128/IAI.74.2.1255-1265.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

The Established Intimin Receptor Tir and the Putative Eucaryotic Intimin Receptors Nucleolin and ß1 Integrin Localize at or near the Site of Enterohemorrhagic Escherichia coli O157:H7 Adherence to Enterocytes In Vivo

Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, Maryland,¹ Pre-Harvest Food Safety and Enteric Disease Research Unit, National Animal Disease Center, Agricultural Research Service, U.S. Department of Agriculture, Ames, Iowa²

Received 14 July 2005/ Returned for modification 29 September 2005/ Accepted 26 November 2005

For enterohemorrhagic Escherichia coli (EHEC) O157:H7 to adhere tightly to the intestinal epithelium and produce attach and efface (A/E) lesions, the organism must express the adhesin intimin and insert the bacterially encoded translocated intimin receptor Tir into the plasma membrane of the host enterocyte. Additionally, some reports based on tissue culture experiments indicate that intimin has affinity for the eucaryotic proteins nucleolin and ß1 integrin. To address the potential biological relevance of these eucaryotic proteins in the infection process in vivo, we sought to compare the proximity of Tir, nucleolin, and ß1 integrin to regions of EHEC O157:H7 attachment in intestinal sections from three different inoculated animals: piglets, neonatal calves, and mice. Piglets and neonatal calves were chosen because intimin-mediated adherence of EHEC O157:H7 and subsequent A/E lesion formation occur at high levels in these animals. Mice were selected because of their ease of manipulation but only after we first demonstrated that in competition with the normal mouse gut flora, an EHEC O157:H7 strain with a nonpolar deletion in the intimin gene was cleared faster than strains that produced wild-type or hybrid intimin. In all three animal species, we noted immunostained Tir beneath and stained nucleolin closely associated with adherent bacteria in intestinal sections. We also observed immunostained ß1 integrin clustered at locations of bacterial adherence in porcine and bovine tissue. These findings indicate that nucleolin and ß1 integrin are present on the luminal surface of intestinal epithelia and are potentially accessible as receptors for intimin during EHEC O157:H7 infection.

Editor: J. T. Barbieri

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