N-terminal E-cadherin peptides act as decoy receptors for Listeria monocytogenes.
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.
da Silva Tatley
Fernanda
F
Cancer Genetics Laboratory, Department of Biochemistry, University of Otago, Dunedin, Aotearoa, New Zealand.
Aldwell
Frank E
FE
Dunbier
Anita K
AK
Guilford
Parry J
PJ
D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000378:metabolism; D018938:Caco-2 Cells; D015820:Cadherins / Q000737:chemistry / Q000378:metabolism*; D004492:Edetic Acid / Q000494:pharmacology; D006801:Humans; D008089:Listeria monocytogenes / Q000502:physiology*; D010446:Peptide Fragments / Q000502:physiology*
D001426:Bacterial Proteins; D015820:Cadherins; D010446:Peptide Fragments; C069761:internalin protein, Bacteria; D004492:Edetic Acid