Escherichia coli of human origin binds to carcinoembryonic antigen (CEA) and non-specific crossreacting antigen (NCA)

FEBS Lett. 1990 Feb 26;261(2):405-9. doi: 10.1016/0014-5793(90)80603-g.


Immobilized carcinoembryonic antigen (CEA) and non-specific crossreacting antigen (NCA) bound 3 strains of E. coli of human origin. The binding was dose dependent, saturable, and of high avidity. Binding of the bacteria to CEA and NCA was completely abolished in the presence of 10 mM alpha-methyl D-mannopyranoside. Bacteria did not bind to concanavalin A. In addition, binding to deglycosylated CEA was either absent or significantly reduced. These findings indicate that the E. coli strains bind to D-mannosyl residues in CEA and NCA. Considering the tissue distribution of CEA (brush border of colonic epithelium) and NCA (granulocytes), these glycoproteins may be involved in the recognition of bacteria.

MeSH terms

  • Antigens, Neoplasm*
  • Bacterial Adhesion / drug effects
  • Carcinoembryonic Antigen / metabolism*
  • Cell Adhesion Molecules*
  • Escherichia coli / metabolism*
  • Feces / microbiology
  • Glycoproteins / metabolism*
  • Glycosylation
  • Hemagglutination Tests
  • Humans
  • Immunoenzyme Techniques
  • Mannose / metabolism
  • Methylmannosides / pharmacology
  • Trachea / microbiology


  • Antigens, Neoplasm
  • Carcinoembryonic Antigen
  • Cell Adhesion Molecules
  • Glycoproteins
  • Methylmannosides
  • methylmannoside
  • Mannose