E-cadherin is the receptor for internalin, a surface protein required for entry of L. monocytogenes into epithelial cells

Cell. 1996 Mar 22;84(6):923-32. doi: 10.1016/s0092-8674(00)81070-3.


We report the first identification of a cellular receptor mediating entry of a gram-positive bacterium into nonphagocytotic cells. By an affinity chromatography approach, we identified E-cadherin as the ligand for internalin, an L. monocytogenes protein essential for entry into epithelial cells. Expression of the chicken homolog of E-cadherin (L-CAM) in transfected fibroblasts dramatically increases entry of L. monocytogenes and promotes that of a recombinant L. innocua strain expressing internalin but does not promote entry of the wild-type noninvasive L. innocua or that of an internalin-deficient mutant of L. monocytogenes. Furthermore, L-CAM-specific antibodies block internalin-mediated entry. In contrast to Salmonella, Listeria enters cells by a mechanism of induced phagocytosis occurring without membrane ruffling. This work reveals a novel type of heterophilic interactions for E-cadherin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibody Specificity
  • Bacterial Proteins / metabolism*
  • Caco-2 Cells / microbiology
  • Cadherins / immunology
  • Cadherins / metabolism*
  • Cell Adhesion / physiology
  • Epithelial Cells
  • Epithelium / microbiology
  • Epithelium / ultrastructure
  • Humans
  • Ligands
  • Listeria monocytogenes / cytology*
  • Mammals
  • Molecular Sequence Data
  • Receptors, Cell Surface / metabolism
  • Salmonella / cytology
  • Sequence Homology, Amino Acid


  • Bacterial Proteins
  • Cadherins
  • Ligands
  • Receptors, Cell Surface
  • internalin protein, Bacteria