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Infection and Immunity, March 2003, p. 1580-1583, Vol. 71, No. 3
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.3.1580-1583.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

N-Terminal E-Cadherin Peptides Act as Decoy Receptors for Listeria monocytogenes

Fernanda da Silva Tatley,1,2 Frank E. Aldwell,2 Anita K. Dunbier,1 and Parry J. Guilford1*

Cancer Genetics Laboratory, Department of Biochemistry,1 Department of Microbiology, University of Otago, Dunedin, Aotearoa, New Zealand2

Received 5 August 2002/ Returned for modification 30 September 2002/ Accepted 2 December 2002

The observation that E-cadherin is the principal epithelial receptor for the bacterial pathogen Listeria monocytogenes led us to investigate whether N-terminal fragments of E-cadherin containing the L. monocytogenes binding domain could inhibit entry of the bacteria into cultured epithelial cells. Here we demonstrate that a conditioned medium from a gastric cancer cell line (Kato III) that carries a truncating CDH-1 mutation 3' of the L. monocytogenes binding domain can inhibit the uptake of the bacteria into Caco-2 cells. The inhibitory activity of the Kato III conditioned medium could be mimicked by incubation of the bacteria with a recombinant 26-kDa N-terminal E-cadherin peptide prior to infection. Furthermore, these data suggest that cleavage of the 80-kDa extracellular domain of E-cadherin from the cell surface may provide an innate form of pathogen defense by acting as a decoy receptor for L. monocytogenes.

* Corresponding author. Mailing address: Cancer Genetics Laboratory, Department of Biochemistry, University of Otago, P.O. Box 56, Dunedin, New Zealand. Phone: 64-3-4795803. Fax: 64-3-479580. E-mail: parry.guilford{at}otago.ac.nz.

Editor: J. T. Barbieri

Infection and Immunity, March 2003, p. 1580-1583, Vol. 71, No. 3
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.3.1580-1583.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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