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J. Biol. Chem., Vol. 277, Issue 4, 2876-2885, January 25, 2002
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From the Department of Microbiology and Immunology, Uniformed
Services University of the Health Sciences, Bethesda, Maryland
20814-4799
Intimin-
Cell Surface-localized Nucleolin Is a Eukaryotic Receptor for the
Adhesin Intimin-
of Enterohemorrhagic Escherichia coli
O157:H7*
is an outer membrane protein of
enterohemorrhagic Escherichia coli (EHEC) O157:H7 that
is required for the organism to adhere tightly to HEp-2 cells and to
colonize experimental animals. Another EHEC O157:H7 protein, the
Transferred intimin receptor (Tir), is considered the primary receptor
for intimin-. Nevertheless, Tir-independent binding of intimin-
to HEp-2 cells has been reported. This observation suggests the
existence of a eukaryotic receptor(s) for intimin-. In this study,
we sought to identify that receptor(s). First, we determined by
equilibrium binding titration that the association of purified
intimin- with HEp-2 cells was specific and consistent with a single
host cell receptor. Second, we isolated a protein from lysates of HEp-2 cells that bound intimin- and subsequently identified this molecule as nucleolin, a protein involved in cell growth regulation that can be
cell surface-expressed. Third, we established that purified intimin-
and nucleolin were co-localized on the surface of HEp-2 cells and that
the site of EHEC O157:H7 attachment was associated with regions of
nucleolin expression. Finally, we demonstrated that mouse
anti-nucleolin sera significantly decreased the adherence of EHEC
O157:H7 to HEp-2 cells. From this, we conclude that nucleolin is the
HEp-2 cell receptor for intimin- expressed by EHEC
O157:H7.
*
This work was supported by Grants AI20148-16 from the
National Institutes of Health and by 97-35201-4578 from the United
States Department of Agriculture.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Microbiology
and Immunology, Uniformed Services University of the Health Sciences,
4301 Jones Bridge Rd., Bethesda, MD 20814-4799. Tel.: 301-295-3419;
Fax: 301-295-3773; E-mail: aobrien@usuhs.mil.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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