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Infection and Immunity, November 2001, p. 6573-6579, Vol. 69, No. 11
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.11.6573-6579.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Enteropathogenic Escherichia coli Virulence Factor Bundle-Forming Pilus Has a Binding Specificity for Phosphatidylethanolamine

C. Khursigara,1 M. Abul-Milh,1 B. Lau,1 J. A. Girón,2 C. A. Lingwood,3 and D. E. Barnett Foster1,3,*

Department of Chemistry, Biology and Chemical Engineering, Ryerson University,1 and Division of Infection, Immunity, Injury and Repair, Research Institute, Hospital for Sick Children,3 Toronto, Ontario, Canada, and Centro de Investigaciones en Ciencas Microbiologicas, Benemerita Universidad Autonoma de Puebla, Puebla, Mexico2

Received 19 January 2001/Returned for modification 25 May 2001/Accepted 31 July 2001

The bundle-forming pilus (BFP) of enteropathogenic Escherichia coli (EPEC), an established virulence factor encoded on the EPEC adherence factor (EAF) plasmid, has been implicated in the formation of bacterial autoaggregates and in the localized adherence of EPEC to cultured epithelial cells. While understanding of the pathogenic mechanism of this organism is rapidly improving, a receptor ligand for BFP has not yet been identified. We now report, using both solid-phase and liposome binding assays, that BFP expression correlates with phosphatidylethanolamine (PE) binding. In a thin-layer chromatogram overlay assay, specific recognition of PE was documented for BFP-expressing strains, including E2348/69, a wild-type EPEC clinical isolate, as well as a laboratory strain, HB101, transformed with a bfp-carrying plasmid. Strains which did not express BFP did not bind PE, including a bfpA disruptional mutant of E2348/69, EAF plasmid-cured E2348/69, and HB101. E2348/69 also aggregated PE-containing liposomes but not phosphatidylcholine- or phosphatidylserine-containing liposomes, while BFP-negative strains did not produce aggregates with any tested liposomes. Purified BFP preparations bound commercial PE standards as well as a PE-containing band within lipid extracts from human epithelial cells and from E2348/69. Our results therefore indicate a specific interaction between BFP and PE and suggest that PE may serve as a BFP receptor for bacterial autoaggregation and may promote localized adherence to host cells, both of which contribute to bacterial pathogenesis.

* Corresponding author. Mailing address: Department of Chemistry, Biology and Chemical Engineering, Ryerson University, Toronto, Ontario, Canada M5B 2K3. Phone: (416) 979 5000, ext. 6345. Fax: (416) 979 5044. E-mail: dfoster{at}acs.ryerson.ca.

Infection and Immunity, November 2001, p. 6573-6579, Vol. 69, No. 11
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.11.6573-6579.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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