1. N-Terminal E-Cadherin Peptides Act as Decoy Receptors for Listeria monocytogenes
- Author
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Frank E. Aldwell, Parry Guilford, Fernanda M. Da Silva Tatley, and Anita K. Dunbier
- Subjects
Immunology ,medicine.disease_cause ,Microbiology ,Bacterial Adhesion ,Bacterial Proteins ,Listeria monocytogenes ,Extracellular ,medicine ,Humans ,Decoy receptors ,Receptor ,Pathogen ,Edetic Acid ,biology ,Cell adhesion molecule ,Cadherins ,biology.organism_classification ,Molecular Pathogenesis ,Peptide Fragments ,Infectious Diseases ,Parasitology ,Caco-2 Cells ,Bacteria ,Binding domain - Abstract
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 .
- Published
- 2003
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